Tokushima University / Educator and Researcher Directory --- Hosoi, Kazuo

Personal Web Page

https://researchmap.jp/read0043195 (researchmap)

https://orcid.org/0000-0001-5165-5056 (ORCID)

Field of Study

○	Molecular Cell Physiology
○	Molecular Oral Physiology

Subject of Study

○	Molecular Mechanism of Expression and Regulation of Water Channel Aquaporins in the Exocrine Glands (aquaporin, water channel proteins, exocrine glands) (Water is a fundamental component in the living system, and therefore its transport mechanism has been studied in many fields. In 1992, a first protein of water channel, aquaporin1 (AQP1), was discovered, which facilitates the water movement across the cell membrane. In mammals, 11 members of AQPs presently exist, constituting a gene family. AQP5 is strongly expressed in the tissues like the salivary gland and supposed to be an exocrine-type water channel. We are studying (1) regulation of AQP5 expression, (2) regulation of AQP5 function, (3) divergent expression of AQP5 gene, (4) regulation of AQP5 expression during development and differentiation in the tissues of the salivary and lacrimal gland, the gastrointestinal tract, and lung.)
○	Induction of Inflammation Cytokines in the Salivary Gland and the Defense System of Oral Cavity (inflammatory cytokine, innate immunity, salivary glands, Signal transduction of proinflammatory cytokine receptors) (Toll-like receptors (TLRs) play an important role in the innate immune system as microbial recognition receptors. Since inflammation cytokines are induced via TLR in the salivary gland and are secreted into the oral cavity, it is presumable that the innate immunity is active as a defense system in the oral cavity. We are studying the defense system of oral cavity, under the theory that "The oral cavity-salivary gland axiss " maintains oral hygiene.)

Book / Paper

Book:

1.	Kazuo Hosoi : Natural science Japanese for international students, 3A Corporation, Tokyo, Sep. 2020.
2.	Tetsuya Akamatsu, Chenjuan Yao and Kazuo Hosoi : Methods for animal tissue culture and techniques to prevent cell death, growth defect, and cell mutation, Technical Information Institute Co., Ltd., Apr. 2014. (Keyword) salivary gland / tissue culture / induction of differentiation
3.	Kazuo Hosoi, Chenjuan Yao and others : Handbook of proteolytic enzymes, 3rd Edition, Elsevier Scientific Publishing Company, Amsterdam, 2011. (Keyword) kallikreins / mK13 / mK26 / mouse
4.	Kazuo Hosoi and (名) others : Basic Physiology for Dental Students 5th edition (in Japanese), Ishiyaku Publishers,Inc., Tokyo, Feb. 2008.
5.	Kazuo Hosoi and others : Modern Juku for Dentistry (Japanese), Ishiyaku Publishers,Inc., Tokyo, Feb. 2007.
6.	Kazuo Hosoi, Tetsuya Akamatsu and others : Special Oral Biology - Salivary Glands, Gakken Shoin, Tokyo, Feb. 2006.
7.	Kazuo Hosoi and others : Handbook of proteolytic enzymes, 2nd Edition, Elsevier Scientific Publishing Company, Amsterdam, May 2004. (Keyword) kallikreins / mK13 / mK26 / mouse
8.	Kazuo Hosoi, Tomihiko Higuti, Masanori Kashimata, Rieko Arakaki, Naokatu Arakaki, Jun Tada, Keiko Tsumura, Tetsuya Akamatsu, Kyouko Takeda, Akemichi Ueno, Midori Suenaga, Yoshinobu Baba and others : Experimental Manual for Molecular Cell Biology, 2nd Edition, Nankodo, Tokyo, Apr. 2004. (Keyword) In situ hybridization
9.	Kazuo Hosoi, Yasuko Ishikawa, Kan Nagao and others : Teeth and mouth for health - A happy life supported by oral health sciences-, Ishiyaku Publishers,Inc., Tokyo, Aug. 1998.
10.	Kazuo Hosoi and others : Experimental Manual for Molecular Cell Biology, Nankodo, Tokyo, Sep. 1994.
11.	Koshiro Inomata, Takao Ueha, Shoji Kurahashi, Eiichi Sugaya, Shunsuke Huruyama, Kazuo Hosoi and Toshiki Murakami : Standard oral physiology, Gakkenn shoin, Tokyo, Apr. 1994.
12.	Kazuo Hosoi, Nobuo Nakanishi, Takao Ueha and others : Utilization of Animal Components - Land Animals (Dobutsu Seibun Riyoshusei -Rikusan Dobutsu Hen, R & D Planning, Tokyo, Apr. 1987.
13.	Takao Ueha, Kazuo Hosoi, Kyozo Hayashi, Shoei Hurukawa and others : Data-book in Biochemistry (Seikagaku data book), volume 2, Tokyo Kagaku Dozin C., Ltd., Tokyo, Jun. 1980.
14.	Satoru Sasaki, Kazuo Hosoi, Kyozo Hayashi, Shoei Hurukawa and others : Data Book in Biochemistry (Seikagaku data book), volume 1, Tokyo Kagaku Dozin C., Ltd., Tokyo, Nov. 1979.
15.	Kaoru Miyazaki, Kazuo Hosoi, Yasuo Suzuki, Yoshinobu Nagao, Yushi Matuo, Takekazu Horio and others : Seikagaku Jikken Koza, volume 1 (Protein Chemistry 1), Tokyo Kagaku Dozin C., Ltd., Tokyo, Mar. 1976.
16.	Takekazu Horio, Jinpei Yamashita, Katsuzo Nishikawa, Tomisaburo Kakuno, Kazuo Hosoi, Junnosuke Suzuki and Setsuko Yoshimura : Organization of energy transducing membranes, University of Tokyo Press, Tokyo, Aug. 1973.

Academic Paper (Judged Full Paper):

1.	Jing Tang, Chenjuan Yao, Yingqi Liu, Jiaming Yuan, Li Wu, Kazuo Hosoi, Shali Yu, Chunyan Huang, Haiyan Wei and Gang Chen : Arsenic trioxide induces expression of BCL-2 expression via NF-κB and p38 MAPK signaling pathways in BEAS-2B cells during apoptosis, Ecotoxicology and Environmental Safety, Vol.222, 112531, 2021. (Summary) Inorganic arsenic compounds are environmental toxicants that are widely distributed in air, water, and food. B-cell lymphoma 2 (BCL-2) is an oncogene having anti-apoptotic function. In this study, we clarify that BCL-2, as a pro-apoptotic factor, participates in AsO-induced apoptosis in BEAS-2B cells. Specifically, AsO stimulated the expression of BCL-2 mRNA and protein in a dose-dependent manner which was highly accumulated in the nucleus of BEAS-2B cell together with chromatin condensation and DNA fragmentation during apoptosis. Mechanistically, the process described above is mediated through the NF-κB and p38 MAPK signaling pathways, which can be abated by corresponding inhibitors, such as BAY11-7082 and SB203580, respectively. Additionally, BAY11-7082, actinomycin D, and cycloheximide have inhibitory effects on AsO-induced expression of BCL-2 mRNA and protein, and restore the cell viability of BEAS-2B cells. Suppression of BCL-2 protein activation by ABT-199 also restored viability of BEAS-2B cell in AsO-induced apoptosis. Furthermore, AsO increased the level of BCL-2 phosphorylation. These results suggest that in BEAS-2B cells, AsO-induced apoptosis is mainly dominated by BCL-2 upregulation, nuclear localization and phosphorylation. The study presented here provides a novel insight into the molecular mechanism of BCL-2-induced apoptosis. (Keyword) apoptosis / Arsenic Trioxide / Arsenicals / NF-kappa B / Oxides / Proto-Oncogene Proteins c-bcl-2 / p38 Mitogen-Activated Protein Kinases (Tokushima University Institutional Repository) ● Metadata: 116727 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.ecoenv.2021.112531 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34303041 ● Summary page in Scopus @ Elsevier: 2-s2.0-85110571403 (Tokushima University Institutional Repository: 116727, DOI: 10.1016/j.ecoenv.2021.112531, PubMed: 34303041, Elsevier: Scopus)
2.	Yingqi Liu, Jing Tang, Jiaming Yuan, Chenjuan Yao, Kazuo Hosoi, Yu Han, Shali Yu, Haiyan Wei and Gang Chen : Arsenite-induced downregulation of occludin in mouse lungs and BEAS-2B cells via the ROS/ERK/ELK1/MLCK and ROS/p38 MAPK signaling pathways., Toxicology Letters, Vol.332, 146-154, 2020. (Summary) inhibits occludin expression in vivo and in vitro at least partially via the ROS/ERK/ELK1/MLCK and ROS/p38 MAPK signaling pathways. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.toxlet.2020.07.010 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32683294 ● Summary page in Scopus @ Elsevier: 2-s2.0-85087966931 (DOI: 10.1016/j.toxlet.2020.07.010, PubMed: 32683294, Elsevier: Scopus)
3.	Yingqi Liu, Haiyan Wei, Jing Tang, Jiaming Yuan, Mingmin Wu, Chenjuan Yao, Kazuo Hosoi, Shali Yu, Xinyuan Zhao, Yu Han and Gang Chen : Dysfunction of pulmonary epithelial tight junction induced by silicon dioxide nanoparticles via the ROS/ERK pathway and protein degradation., Chemosphere, Vol.255, 126954, 2020. (Summary) Silica nanoparticles (SiNPs) are one of the most widely used types of nanoparticles across many industrial sectors, and are known to be present in the air year-round. In this study, we aimed to evaluate the potential adverse effects of SiNP exposure on pulmonary epithelial tight junctions, which serve as a critical barrier between the respiratory system and the circulatory system. In vivo studies confirmed that SiNPs decreased the protein expression levels of zonula occludens 1 (ZO-1), zonula occludens 2 (ZO-2), and occludin in the lungs of C57BL/6 mice. In vitro studies showed that SiNPs not only decreased the mRNA and protein expression of ZO-1 and ZO-2, but also decreased the protein expression of occludin in human bronchial epithelial (BEAS-2B) cells. In addition, SiNP exposure increased reactive oxygen species (ROS) production and activated extracellular regulated protein kinases (ERKs) and c-Jun N-terminal kinase (JNK). The inhibition of ROS and ERKs effectively protected the SiNP-induced downregulation of ZO-1 mRNA and protein expression, but had no effect on ZO-2 or occludin expression. SiNP-induced matrix metalloproteinase 9 (MMP9) protein expression appeared to be involved in occludin proteolytic degradation, in addition to SiNP-induced direct occludin protein degradation. The present study suggests that SiNPs disturb pulmonary epithelial tight junction structure and function via the ROS/ERK pathway and protein degradation. (Keyword) Animals / Bronchi / Down-Regulation / Humans / JNK Mitogen-Activated Protein Kinases / Lung / MAP Kinase Signaling System / Mice / Mice, Inbred C57BL / nanoparticles / Occludin / Phosphoproteins / Proteolysis / reactive oxygen species / Silicon Dioxide / Tight Junctions / Zonula Occludens-1 Protein (Link to Publication Site) ● Publication site (DOI): 10.1016/j.chemosphere.2020.126954 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32387908 ● Summary page in Scopus @ Elsevier: 2-s2.0-85084223128 (DOI: 10.1016/j.chemosphere.2020.126954, PubMed: 32387908, Elsevier: Scopus)
4.	Javkhlan Purevjav, Xu Guangfei, Chen Gang, Chenjuan Yao, Yuka Hiroshima, Hiroshi Yoshimura, Toshihiko Nagata and Kazuo Hosoi : Expression and LPS-Induced Elevation of Nod2 and Calprotectin in the Submandibular Gland of Wild-Type and TLR4-Knockout Male Mice, Journal of Research and Practice in Dentistry, Vol.2015, No.290259, 2015. (Link to Publication Site) ● Publication site (DOI): 10.5171/2015.290259 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.5171/2015.290259 (DOI: 10.5171/2015.290259)
5.	Gang Chen, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Hiroshi Yoshimura and Kazuo Hosoi : Effects of isoproterenol on aquaporin 5 levels in the parotid gland of mice in vivo., American Journal of Physiology, Endocrinology and Metabolism, Vol.306, No.1, E100-E108, 2014. (Summary) In the membrane fraction of mouse parotid gland (PG), the protein level of aquaporin 5 (AQP5), a member of the water channel family, was increased by injection (ip) of isoproterenol (IPR), a β-adrenergic agonist, at 1 h, and stayed at high levels until 6 h; this change occurred simultaneously as amylase secretion. The AQP5 level then decreased and returned toward the original level at 12-48 h. After IPR injection, the AQP5 mRNA gradually increased and reached a maximum at 24 h. The facts suggest a rapid appearance of AQP5 at plasma membrane by IPR and subsequent degradation/metabolism by activation of proteolytic systems. Pretreatment of animals with two calpain inhibitors, N-Ac-Leu-Leu-methininal (ALLM) and calpeptin, as well as a protein synthesis inhibitor, cycloheximide (CHX), significantly suppressed the IPR-induced AQP5 degradation in the PG membrane fraction; such suppression was not observed by two proteasome inhibitors, MG132 and lactacystin, or the lysosome denaturant chloroquine, although most of these inhibitors increased AQP5 protein levels in unstimulated mice. The AQP5 protein was also degraded by μ-calpain in vitro. Furthermore, we demonstrated that μ-calpain was colocalized with AQP5 in the acinar cells by immunohistochemistry, and its activity in the PG was increased at 6 h after IPR injection. These results suggest that the calpain system was responsible for IPR-induced AQP5 degradation in the parotid gland and that such a system was coupled to the secretory-restoration cycle of amylase in the PG. (Keyword) aquaporin 5 / parotid gland / isoproterenol (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpendo.00317.2013 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24192288 ● Summary page in Scopus @ Elsevier: 2-s2.0-84891527146 (DOI: 10.1152/ajpendo.00317.2013, PubMed: 24192288, Elsevier: Scopus)
6.	Keitaro Satoh, Yoshiteru Seo, Shinsuke Matsuo, Mileva Ratko Karabasil, Miwako Matsuki-Fukushima, Takashi Nakahari and Kazuo Hosoi : Roles of AQP5/AQP5-G103D in carbamylcholine-induced volume decrease and in reduction of the activation energy for water transport by rat parotid acinar cells, Pflügers Archiv : European Journal of Physiology, Vol.464, No.4, 375-389, 2012. (Summary) In order to assess the contribution of the water channel aquaporin-5 (AQP5) to water transport by salivary gland acinar cells, we measured the cell volume and activation energy (E (a)) of diffusive water permeability in isolated parotid acinar cells obtained from AQP5-G103D mutant and their wild-type rats. Immunohistochemistry showed that there was no change induced by carbamylcholine (CCh; 1 μM) in the AQP5 detected in the acinar cells in the wild-type rat. Acinar cells from mutant rats, producing low levels of AQP5 in the apical membrane, showed a minimal increase in the AQP5 due to the CCh. In the wild-type rat, CCh caused a transient swelling of the acinus, followed by a rapid agonist-induced cell shrinkage, reaching a plateau at 30 s. In the mutant rat, the acinus did not swell by CCh challenge, and the agonist-induced cell shrinkage was delayed by 8 s, reaching a transient minimum at around 1 min, and recovered spontaneously even though CCh was persistently present. In the unstimulated wild-type acinar cells, E (a) was 3.4 ± 0.6 kcal mol(-1) and showed no detectable change after CCh stimulation. In the unstimulated mutant acinar cells, high E (a) value (5.9 ± 0.1 kcal mol(-1)) was detected and showed a minimal decrease after CCh stimulation (5.0 ± 0.3 kcal mol(-1)). These results suggested that AQP5 was the main pathway for water transport in the acinar cells and that it was responsible for the rapid agonist-induced acinar cell shrinkage and also necessary to keep the acinar cell volume reduced during the steady secretion in the wild-type rat. (Keyword) Acinar Cells / Animals / Aquaporin 5 / Carbachol / Cell Membrane Permeability / Cell Size / Mutation / Parotid Gland / Rats / Rats, Mutant Strains / Water (Link to Publication Site) ● Publication site (DOI): 10.1007/s00424-012-1141-8 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22903161 ● Search Scopus @ Elsevier (PMID): 22903161 ● Search Scopus @ Elsevier (DOI): 10.1007/s00424-012-1141-8 (DOI: 10.1007/s00424-012-1141-8, PubMed: 22903161)
7.	Nunuk Purwanti, Mileva Ratko Karabasil, Shinsuke Matsuo, Gang Chen, Javkhlan Purevjav, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Induction of Sca-1 via activation of STAT3 system in the duct cells of the mouse submandibular gland by ligation of the main excretory duct, American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.301, No.5, G814-G824, 2011. (Summary) To examine the very initial step that takes place immediately after tissue injury and is linked to tissue regeneration, we employed the submandibular gland (SMG), which was injured by ligation of its main excretory duct (MED). Ligation of the MED of the SMG in mice induced the expression of Sca-1, a protein marker of hematopoietic stem cells. In the normal gland, a low level of Sca-1 was expressed, which was localized predominantly in the excretory duct cells. At 1 day after ligation, Sca-1 expression increased prominently in almost all of cells in the duct system, but not in the acinar cells. The level of Sca-1 mRNA had begun to increase at 6 h after ligation and continuously rose thereafter until it reached a plateau, which occurred ∼12 h after ligation. STAT3 phosphorylated at its tyrosine-705 (p-STAT3) in the ligated gland increased immediately after ligation, and it was localized in the nuclei of all duct cells. The results of an EMSA revealed the specific binding of a nuclear extract to the sequence of the γ-interferon activation site (GAS) present in the Sca-1 promoter and confirmed that such binding increased after ligation. Thus the present study suggests that STAT3, having been phosphorylated following MED ligation, was transferred to the nucleus, where it bound to the GAS element in the promoter of Sca-1 gene, resulting in promotion of Sca-1 gene expression. Actual prevention of STAT3 phosphorylation reduced the ligation-induced Sca-1 elevation. (Keyword) Animals / Antigens, Ly / Ligation / Membrane Proteins / Mice / Phosphorylation / Promoter Regions, Genetic / STAT3 Transcription Factor / Salivary Ducts / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpgi.00408.2010 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21868636 ● Search Scopus @ Elsevier (PMID): 21868636 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00408.2010 (DOI: 10.1152/ajpgi.00408.2010, PubMed: 21868636)
8.	Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Jun-ichi Kido, Toshihiko Nagata and Kazuo Hosoi : Lipopolysaccharide-mediated induction of calprotectin in the submandibular and parotid glands of mice, Inflammation, Vol.34, No.6, 668-680, 2011. (Summary) S100A8 and S100A9 constitute a heterodimeric protein, calprotectin. The mRNAs of S100A8 and S100A9, being expressed at minimal levels in the submandibular and parotid glands (SMG and PG, respectively) of C3H/HeN mice, were induced strongly and transiently by lipopolysaccharide (LPS). Among the mRNAs of members of the S100 protein family examined, those of S100A8 and S100A9 were specifically induced by LPS in the salivary glands. The induction was assumed to be mediated via toll-like receptor 4 (TLR4), since their elevation was limited in C3H/HeJ mice, a TLR4-mutant strain. These proteins became expressed in the granular convoluted tubular cells and striated duct cells in the SMG, and in both acinar and duct cells in the PG (all in the cytoplasm). The salivary calprotectin level was not increased by LPS treatment, implying that elevated calprotectin was not secreted into the saliva and that they may function in microcellular environment of the salivary gland. (Keyword) Animals / Calgranulin A / Calgranulin B / Leukocyte L1 Antigen Complex / Lipopolysaccharides / Mice / Parotid Gland / RNA, Messenger / Salivary Glands / Submandibular Gland / Transcriptional Activation (Link to Publication Site) ● Publication site (DOI): 10.1007/s10753-010-9277-1 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21125321 ● Search Scopus @ Elsevier (PMID): 21125321 ● Search Scopus @ Elsevier (DOI): 10.1007/s10753-010-9277-1 (DOI: 10.1007/s10753-010-9277-1, PubMed: 21125321)
9.	Takahiro Hasegawa, Ahmad Azlina, Javkhlan Purevjav, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling, American Journal of Physiology, Cell Physiology, Vol.301, No.3, C667-C678, 2011. (Summary) Aquaporin-5 (AQP5), a water channel, plays key roles in salivary secretion. The novel phosphorylation of AQP5 was investigated by using human salivary gland (HSG) cells and mouse salivary glands. In the HSG cells stably transfected with a wild-type mouse AQP5 construct, a protein band immunoreactive with antibody against phosphorylated PKA substrate was detected in the AQP5 immunoprecipitated sample, and its intensity was enhanced by short-term treatment of the cells with 8-bromo-cAMP, forskolin, or phorbol 12-myristate 13-acetate, but not by that with A23187 calcium ionophore. Such enhancement was inhibited in the presence of H-89, a PKA inhibitor. An AQP5 mutant (AQP5-T259A) expressed by transfection of HSG cells was not recognized by anti-phosphorylated PKA substrate antibody, even when the cells were stimulated with the protein kinase activators. Immunoblotting and immunofluorescence studies using a specific antibody detecting AQP5 phosphorylated at its Thr259 demonstrated that AQP5 was rapidly and transiently phosphorylated at the apical membrane of acinar cells in the submandibular and parotid glands after administration of isoproterenol, but not pilocarpine. Furthermore, both AQP5 and AQP5-T259A were constitutively localized at the plasma membrane in HSG cells under the resting and forskolin-stimulated conditions. These results suggest that AQP5 is phosphorylated at its Thr259 by PKA through cAMP, but not Ca(2+), signaling pathways, and that this phosphorylation does not contribute to AQP5 trafficking in the salivary gland cells. (Keyword) Amino Acid Substitution / Animals / Antibodies / Antibody Specificity / Aquaporin 5 / Calcimycin / Cell Line, Tumor / Cell Membrane / Cyclic AMP / Cyclic AMP-Dependent Protein Kinases / Detergents / Forskolin / Humans / Isoproterenol / Isoquinolines / Male / Mice / Mice, Inbred ICR / Parotid Gland / Phosphorylation / Pilocarpine / Protein Kinase Inhibitors / Protein Transport / Salivary Glands / Signal Transduction / Submandibular Gland / Sulfonamides / Tetradecanoylphorbol Acetate / Threonine / Transfection (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpcell.00058.2011 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21633078 ● Search Scopus @ Elsevier (PMID): 21633078 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpcell.00058.2011 (DOI: 10.1152/ajpcell.00058.2011, PubMed: 21633078)
10.	Nunuk Purwanti, Daisuke Tsuji, Ahmad Azlina, Mileva Ratko Karabasil, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi : Induction of Sca-1 in the duct cells of the mouse submandibular gland by obstruction of the main excretory duct, Journal of Oral Pathology & Medicine, Vol.40, No.8, 651-658, 2011. (Summary) The effect of ligation of the main excretory duct (MED) of the mouse submandibular gland (SMG) on the expression of Sca-1, a stem cell antigen, was examined by Western blotting and immunohistochemistry. By Western blotting, the expression of Sca-1 with a molecular weight of 18 kDa was identified in the normal gland. At 1 day post-ligation, the expression level of Sca-1 was strongly increased in the experimental gland and weakly in the contralateral gland, and such expression in both glands decreased at 6 days. By immunohistochemistry, Sca-1 was detected weakly in the apical membrane of excretory duct (ED) cells of the SMG under the normal condition. By duct ligation, Sca-1 became expressed strongly in most cells of the two major duct systems, i.e., the striated duct (SD) and granular convoluted tubules (GCT), but was not detected in the acinar (Ac) cells. By fluorescence-activated cell sorter (FACS) analysis, the number of side population (SP) cells in this gland was found to be increased by ligation. These results imply that Sca-1-positive cells may have a role in the duct cell proliferation in the regeneration step elicited by MED ligation-induced injury. (Keyword) Animals / Antigens, Ly / Cell Count / Cell Proliferation / Ligation / Male / Membrane Proteins / Mice / Mice, Inbred C57BL / Regeneration / Salivary Ducts / Salivation / Side-Population Cells / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1600-0714.2011.01011.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21884259 ● Search Scopus @ Elsevier (PMID): 21884259 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1600-0714.2011.01011.x (DOI: 10.1111/j.1600-0714.2011.01011.x, PubMed: 21884259)
11.	Yuka Hiroshima, Mika Bandou, Masatoshi Kataoka, Yuji Inagaki, Mark C. Herzberg, Karen F. Ross, Kazuo Hosoi, Toshihiko Nagata and Jun-ichi Kido : Regulation of antimicrobial peptide expression in human gingival keratinocytes by interleukin-1α, Archives of Oral Biology, Vol.56, No.8, 761-767, 2011. (Summary) In the oral cavity, mucosal keratinocytes resist bacterial infection, in part, by producing broad-spectrum antimicrobial peptides (AMPs) including defensin, adrenomedullin and calprotectin. Epidermal keratinocyte expression of many AMPs increases in response to interleukin-1α (IL-1α). IL-1α is produced by epidermal keratinocytes and regulates cell differentiation. To better understand innate immunity in the oral cavity, we sought to determine how IL-1α might regulate expression of AMPs by human gingival keratinocytes (HGKs) using DNA microarray and Western blot analyses. HGKs from three subjects expressed eleven AMPs, including S100A7, S100A8, S100A9, S100A12, secretory leucocyte protease inhibitor, lipocalin 2 (LCN2), cystatin C and β-defensin 2. Of the expressed AMPs, S100A7, S100A12 and LCN2 were up-regulated by IL-1α (inducible AMPs); the other AMPs were considered to be constitutive. Human gingival keratinocytes, therefore, express constitutive and IL-1α-inducible AMPs to provide a rapid and robust innate response to microbial infection. (Keyword) Acute-Phase Proteins / Adolescent / Adult / Anti-Infective Agents / Antimicrobial Cationic Peptides / Blotting, Western / Calgranulin A / Calgranulin B / Cell Culture Techniques / Cystatin C / Female / Gene Expression Regulation / Gingiva / Humans / Immunity, Innate / Interleukin-1alpha / Keratinocytes / Lipocalins / Male / Oligonucleotide Array Sequence Analysis / Proline-Rich Protein Domains / Proto-Oncogene Proteins / S100 Proteins / Secretory Leukocyte Peptidase Inhibitor / Serine Proteinase Inhibitors / Up-Regulation / Young Adult / beta-Defensins (Link to Publication Site) ● Publication site (DOI): 10.1016/j.archoralbio.2011.01.004 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21316034 ● Search Scopus @ Elsevier (PMID): 21316034 ● Search Scopus @ Elsevier (DOI): 10.1016/j.archoralbio.2011.01.004 (DOI: 10.1016/j.archoralbio.2011.01.004, PubMed: 21316034)
12.	Mileva Ratko Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Shigemasa Tomioka and Kazuo Hosoi : Effects of naturally occurring G103D point mutation of AQP5 on its water permeability, trafficking, and cellular localization in the submandibular gland of rats, Biology of the Cell, Vol.103, No.2, 69-86, 2011. (Summary) AQPs (aquaporins) are water channel proteins that are expressed in almost all living things. In mammalians, 13 members of AQPs (AQP0-12) have been identified so far. AQP5 is known to be expressed mostly in the exocrine cells, including the salivary gland acinar cells. A naturally occurring point mutation (G308A, Gly103 > Asp103) was earlier found in the rat AQP5 gene [Murdiastuti, Purwanti, Karabasil, Li, Yao, Akamatsu, Kanamori and Hosoi (2006) Am. J. Physiol. 291, G1081-G1088]; in this mutant, the rate of initial saliva secretion under stimulated and unstimulated conditions is less than that for the wt (wild-type) animals. Here the mutant molecule was characterized in detail. Using the Xenopus oocyte system, we demonstrated the mutant AQP5 to have water permeability almost the same as that of the wt molecule. Mutant and wt AQP5s, tagged with GFP (green fluorescent protein; GFP-AQP5s) and expressed in polarized MDCK-II (Madin-Darby canine kidney II) cells, first appeared in the vesicular structure(s) in the cytoplasm, and were translocated to the upper plasma membrane or apical membrane during cultivation, with the mutant GFP-AQP5 being translocated less efficiently. Thapsigargin and H-89 both induced translocation in vitro of either molecule, whereas colchicine inhibited this activity; the fraction of cells showing apical localization of mutant GFP-AQP5 was less than that showing that of the wt molecule under any of the experimental conditions used. In the mutant SMG (submandibular gland) tissue, localization of AQP5 in the apical membrane of acinar cells was extremely reduced. Vesicular structures positive for AQP5 and present in the cytoplasm of the acinar cells were co-localized with LAMP2 (lysosome-associated membrane protein 2) or cathepsin D in the mutant gland, whereas such co-localizations were very rare in the wt gland, suggesting that the mutant molecules largely entered lysosomes for degradation. Replacement of highly conserved hydrophobic Gly103 with strongly hydrophilic Asp103 in rat AQP5, though it did not affect water permeability, may possibly have resulted in less efficient membrane trafficking and increased lysosomal degradation, leading to its lower expression in the apical membrane of the acinar cells in the SMG. (Keyword) Amino Acid Sequence / Animals / Aquaporin 5 / Cell Line / Cell Membrane / Dogs / Molecular Sequence Data / Mutation, Missense / Permeability / Point Mutation / Protein Transport / Rats / Sequence Alignment / Submandibular Gland / Water / Xenopus (Link to Publication Site) ● Publication site (DOI): 10.1042/BC20100086 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21138418 ● Search Scopus @ Elsevier (PMID): 21138418 ● Search Scopus @ Elsevier (DOI): 10.1042/BC20100086 (DOI: 10.1042/BC20100086, PubMed: 21138418)
13.	Ahmad Azlina, Purevjav Javkhlan, Yuka Hiroshima, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Roles of lysosomal proteolytic systems in AQP5 degradation in the submandibular gland of rats following chorda tympani parasympathetic denervation, American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.299, No.5, G1106-G1117, 2010. (Summary) Chorda tympani denervation (CTD) of rats was earlier shown to result in loss of submandibular gland (SMG) weight (at only 1 wk) and in continued reduction in aquaporin 5 (AQP5) protein expression (until 4 wk), without affecting its mRNA synthesis (Li X, Azlina A, Karabasil MR, Purwanti N, Hasegawa T, Yao C, Akamatsu T, Hosoi K. Am J Physiol Gastrointest Liver Physiol 295: G112-G123, 2008). The present study indicated that despite elevation of bax, a proapoptosis protein, by CTD, the operation also increased the level of bcl-2, an antiapoptosis protein, in the SMG. Terminal deoxynucleotidyl transferase dUTP nick-end labeling (TUNEL assay) showed no increase in the number of apoptotic cells in the SMG. CTD, however, induced strongly and transiently (at 1-3 days) the protein expression of LC3B-II, a marker protein of autophagosomes, suggesting that the reduction in the gland weight was due to onset of autophagy by CTD. Upon CTD, Lamp2, a lysosomal marker, gradually increased in amount, reaching a peak at the 14th day. Immunohistochemical analysis revealed an increase in the number of lysosome-like structures positive for both AQP5 and Lamp2 in the acinar cells of the SMG after CTD; similar changes were observed also for AQP5 and LC3Bs. These data suggest that AQP5 in the SMG entered autophagosomes and/or lysosomes for degradation upon CTD. In vitro AQP5-degrading activity was found in the SMG extracts, and such activity was shown to be increased by CTD. Inhibitor experiments implied cathepsins B and L to be candidate enzymes for this degradation under normal and CTD conditions, respectively. (Keyword) Animals / Apoptosis / Aquaporin 5 / Blotting, Western / Chorda Tympani Nerve / Immunohistochemistry / In Situ Nick-End Labeling / Lysosomal-Associated Membrane Protein 2 / Lysosomes / Male / Parasympathectomy / Proto-Oncogene Proteins c-bcl-2 / Rats / Rats, Sprague-Dawley / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpgi.00194.2010 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20689061 ● Search Scopus @ Elsevier (PMID): 20689061 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00194.2010 (DOI: 10.1152/ajpgi.00194.2010, PubMed: 20689061)
14.	Chenjuan Yao, Nunuk Purwanti, Mileva Ratko Karabasil, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Tetsuya Akamatsu, Toru Hosoi, Koichiro Ozawa and Kazuo Hosoi : Potential down-regulation of salivary gland AQP5 by LPS via cross-coupling of NF-κB and p-c-Jun/c-Fos, The American Journal of Pathology, Vol.177, No.2, 724-734, 2010. (Summary) The mRNA and protein levels of aquaporin (AQP)5 in the parotid gland were found to be potentially decreased by lipopolysaccharide (LPS) in vivo in C3H/HeN mice, but only weakly in C3H/HeJ, a TLR4 mutant mouse strain. In the LPS-injected mice, pilocarpine-stimulated saliva production was reduced by more than 50%. In a tissue culture system, the LPS-induced decrease in the AQP5 mRNA level was blocked completely by pyrrolidine dithiocarbamate, MG132, tyrphostin AG126, SP600125, and partially by SB203580, which are inhibitors for IkappaB kinase, 26S proteasome, ERK1/2, JNK, and p38 MAPK, respectively. In contrast, the expression of AQP1 mRNA was down-regulated by LPS and such down-regulation was blocked only by SP600125. The transcription factors NF-kappaB (p65 subunit), p-c-Jun, and c-Fos were increased by LPS given in vivo, whereas the protein-binding activities of the parotid gland extract toward the sequences for NF-kappaB but not AP-1-responsive elements present at the promoter region of the AQP5 gene were increased by LPS injection. Co-immunoprecipitation by using antibody columns suggested the physical association of the three transcription factors. These results suggest that LPS-induced potential down-regulation of expression of AQP5 mRNA in the parotid gland is mediated via a complex(es) of these two classes of transcription factors, NF-kappaB and p-c-Jun/c-Fos. (Keyword) Animals / Aquaporin 1 / Aquaporin 5 / Cells, Cultured / Enzyme Inhibitors / Humans / JNK Mitogen-Activated Protein Kinases / Lipopolysaccharides / Male / Mice / Mice, Inbred C3H / Mice, Inbred C57BL / NF-kappa B / Nitrates / Nitrites / Proto-Oncogene Proteins c-fos / Salivary Glands (Link to Publication Site) ● Publication site (DOI): 10.2353/ajpath.2010.090282 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20522648 ● Search Scopus @ Elsevier (PMID): 20522648 ● Search Scopus @ Elsevier (DOI): 10.2353/ajpath.2010.090282 (DOI: 10.2353/ajpath.2010.090282, PubMed: 20522648)
15.	Mileva Ratko Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Javkhlan Purevjav, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Trafficking of GFP-AQP5 chimeric proteins conferred with unphosphorylated amino acids at their PKA-target motif (¹⁵²SRRTS) in MDCK-II cells, The Journal of Medical Investigation : JMI, Vol.56, No.1, 2, 55-63, 2009. (Summary) Three constructs having mutated PKA-target motif at (152)SRRTS of AQP5, an exocrine type water channel, were prepared and fused to C-terminus of green fluorescence protein cDNA to examine the effects of blocking of phosphorylation at (152)SRRTS (a consensus PKA-target motif of AQP5) on translocation or trafficking of the chimeric proteins expressed in the Madin-Darby canine kidney-II (MDCK-II) cells. H-89 treatment increased translocation of wild-type GFP-AQP5 to the apical membrane. All 3 mutant molecules translocated 1.5 to 2 times more than the control wild-type GFP-AQP5. Colchicine but not cytochalasin B inhibited the translocation of wild-type GFP-AQP5. Present results suggest dephosphorylation of this consensus sequence increase GFP-AQP5 translocation, and that microtubules but not microfilaments are involved in this event. (Keyword) Amino Acid Motifs / Amino Acids / Animals / Aquaporin 5 / Cell Line / Cell Membrane / Chimera / Colchicine / Cyclic AMP-Dependent Protein Kinases / Cytochalasin B / Dogs / Green Fluorescent Proteins / Isoquinolines / Kidney / Phosphorylation / Protein Transport / Sulfonamides (Tokushima University Institutional Repository) ● Metadata: 111308 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.55 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19262015 ● Search Scopus @ Elsevier (PMID): 19262015 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.55 (Tokushima University Institutional Repository: 111308, DOI: 10.2152/jmi.56.55, PubMed: 19262015)
16.	Shingo Kurabuchi and Kazuo Hosoi : Immunocytochemical study of granular duct cells with a hormonally enhanced granular cell phenotype in the mouse parotid gland, Odontology, Vol.97, No.1, 57-61, 2009. (Summary) In the parotid glands (PGs) of intact male mice (12 weeks of age, ICR strain), immunofluorescence labels for a true tissue kallikrein, mK1, and for nerve growth factor (NGF) were recognized through the subluminal edges of the striated duct (SD) segments and interlobular duct segments. Because of their small size, secretory granules were not detectable by light microscopy in any of the duct cells. Full-fledged granular cells, containing large secretory granules that were visible by light microscopy, were induced in the SD segments of male mice after the injection of 5alpha-dehydrotestosterone (DHT) and triiodothyronine (T(3)), given either alone or in combination every other day for 2 weeks. A stronger effect was detected in the mice that were concomitantly injected with DHT and T(3), and more abundant, fully developed granular cells appeared in the SD segments of these mice. These full-fledged granular cells were immunoreactive for mK1, NGF, and epidermal growth factor, but not for renin. The present results indicate that some of the SD cells with small granules in the mouse PG can develop a granular cell phenotype, producing more kinds of growth factors, as a result of the actions of androgen and thyroid hormone. (Keyword) Animals / Dihydrotestosterone / Epidermal Growth Factor / Fluorescent Antibody Technique, Indirect / Immunohistochemistry / Male / Mice / Mice, Inbred ICR / Nerve Growth Factor / Parotid Gland / Phenotype / Renin / Salivary Ducts / Secretory Vesicles / Tissue Kallikreins / Triiodothyronine (Link to Publication Site) ● Publication site (DOI): 10.1007/s10266-008-0090-3 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19184300 ● CiNii @ National Institute of Informatics (CRID): 1573387451010251520 ● Search Scopus @ Elsevier (PMID): 19184300 ● Search Scopus @ Elsevier (DOI): 10.1007/s10266-008-0090-3 (DOI: 10.1007/s10266-008-0090-3, PubMed: 19184300, CiNii: 1573387451010251520)
17.	Tetsuya Akamatsu, Ahmad Azlina, Nunuk Purwanti, Mileva Ratko Karabasil, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi : Inhibition and transcriptional silencing of a subtilisin-like proprotein convertase, PACE4/SPC4, reduces the branching morphogenesis of and AQP5 expression in rat embryonic submandibular gland, Developmental Biology, Vol.325, No.2, 434-443, 2009. (Summary) The submandibular gland (SMG) develops through the epithelial-mesenchymal interaction mediated by many growth/differentiation factors including activin and BMPs, which are synthesized as inactive precursors and activated by subtilisin-like proprotein convertases (SPC) following cleavage at their R-X-K/R-R site. Here, we found that Dec-RVKR-CMK, a potent inhibitor of SPC, inhibited the branching morphogenesis of the rat embryonic SMG, and caused low expression of a water channel AQP5, in an organ culture system. Dec-RVKR-CMK also decreased the expression of PACE4, a SPC member, but not furin, another SPC member, suggesting the involvement of PACE4 in the SMG development. Heparin, which is known to translocate PACE4 in the extracellular matrix into the medium, and an antibody specific for the catalytic domain of PACE4, both reduced the branching morphogenesis and AQP5 expression in the SMG. The inhibitory effects of Dec-RVKR-CMK were partially rescued by the addition of recombinant BMP2, whose precursor is one of the candidate substrates for PACE4 in vivo. Further, the suppression of PACE4 expression by siRNAs resulted in decreased expression of AQP5 and inhibition of the branching morphogenesis in the present organ culture system. These observations suggest that PACE4 regulates the SMG development via the activation of some growth/differentiation factors. (Keyword) Amino Acid Chloromethyl Ketones / Animals / Aquaporin 5 / Extracellular Matrix / Furin / Gene Silencing / Heparin / Morphogenesis / Organ Culture Techniques / Proprotein Convertases / Rats / Rats, Sprague-Dawley / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1016/j.ydbio.2008.10.015 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19013448 ● Search Scopus @ Elsevier (PMID): 19013448 ● Search Scopus @ Elsevier (DOI): 10.1016/j.ydbio.2008.10.015 (DOI: 10.1016/j.ydbio.2008.10.015, PubMed: 19013448)
18.	Shingo Kurabuchi, Edward W Gresik, Chenjuan Yao and Kazuo Hosoi : Hypophysectomy and hormonal therapy modulate mK1-immunoreactive duct cells in the mice sublingual glands, Journal of Molecular Histology, Vol.39, No.5, 499-507, 2008. (Summary) The immunocytochemical localization of a true tissue kallikrein, mK1, in mouse sublingual glands (SLGs) was examined following hypophysectomy and hormonal replacement therapy. In the glands of intact mice (14 weeks of age), mK1 was detected in the striated ducts (SDs). Full-fledged granular cells were scattered in the SDs of male mice (but not in those of female mice), showing a cellular mosaic distribution of mK1 with some being positive and others being negative. mK1 was also detected in transitional-type granular cells, though the secretory granules were too small and scarce to be visible by a light microscopy. Hypophysectomy in male mice resulted in the atrophy and loss of secretory granules in many SD cells. Granulation recovered after the repeated injection of 5alpha-dihydrotestosterone (DHT), 3,5,3'-triiodo-L: thyronine (T3), and dexamethasone (Dex), given either alone or in combination to the hypophysectomized mice. The concomitant injection of DHT and T3, with or without Dex, resulted in the reappearance of the full-fledged granular cells, only some of which were mK1-positive. Electron microscopy revealed mK1 to be present exclusively in the secretory granules of these mK1-positive cells, and no ultrastructural differences were observed between mK1-positive and mK1-negative full-fledged granular cells. These results show that the differentiation of the granular cell phenotype in the mouse SLG duct system requires the concomitant action of androgen and thyroid hormone and retards mK1 synthesis. (Keyword) Animals / Dexamethasone / Dihydrotestosterone / Female / Glucocorticoids / Hormone Replacement Therapy / Hypophysectomy / Male / Mice / Mice, Inbred ICR / Secretory Vesicles / Sex Characteristics / Sublingual Gland / Tissue Kallikreins / Triiodothyronine (Link to Publication Site) ● Publication site (DOI): 10.1007/s10735-008-9189-7 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18716886 ● Search Scopus @ Elsevier (PMID): 18716886 ● Search Scopus @ Elsevier (DOI): 10.1007/s10735-008-9189-7 (DOI: 10.1007/s10735-008-9189-7, PubMed: 18716886)
19.	Xuefei Li, Ahmad Azlina, Mileva Ratko Karabasil, Nunuk Purwanti, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Degradation of submandibular gland AQP5 by parasympathetic denervation of chorda tympani and its recovery by cevimeline, an M3 muscarinic agonist, American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.295, No.1, G112-G123, 2008. (Summary) By chorda tympani denervation (CTD, parasympathectomy), the aquaporin 5 (AQP5), but not AQP1, protein level in the rat submandibular gland (SMG) was significantly decreased, dropping to 37% of that of the contralateral gland at 4 wk. The protein levels of AQP5 and AQP1 were not significantly affected by denervation of the cervical sympathetic trunk (sympathectomy). Administration of cevimeline hydrochloride, an M3 muscarinic receptor agonist (10 mg/kg for 7 days po), but not pilocarpine (0.3 mg/kg for 7 days po), recovered the AQP5 protein level reduced by CTD and increased the AQP1 protein level above the control one. The mRNA level of AQP5 was scarcely affected by CTD and cevimeline hydrochloride administration. Administration of chloroquine (50 mg/kg for 7 days po), a denaturant of lysosomes, increased the AQP5 protein level reduced by CTD. An extract obtained from the submandibular lysosomal fraction degraded the AQP5 protein in the total membrane fraction in vitro. These results suggest the possible regulation of the AQP5 protein level in the SMG by the parasympathetic nerves/M3 muscarinic receptor agonist and imply the involvement of lysosomal enzymes, but not a transcriptional mechanism, in this regulation. (Keyword) Animals / Aquaporin 1 / Aquaporin 5 / Chorda Tympani Nerve / Gene Expression Regulation / Lysosomes / Male / Muscarinic Agonists / Parasympathectomy / Pilocarpine / Quinuclidines / RNA, Messenger / Rats / Rats, Sprague-Dawley / Submandibular Gland / Sympathectomy / Thiophenes / Time Factors (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpgi.00359.2007 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18450949 ● Search Scopus @ Elsevier (PMID): 18450949 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00359.2007 (DOI: 10.1152/ajpgi.00359.2007, PubMed: 18450949)
20.	Tetsuya Akamatsu, Nunuk Purwanti, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Temporospatially regulated expression of subtilisin-like proprotein convertase PACE4 (SPC4) during development of the rat submandibular gland, Developmental Dynamics, Vol.236, No.1, 314-320, 2007. (Summary) The temporospatial expression of PACE4, a member of the mammalian subtilisin-like proprotein convertase family involved in the activation of growth/differentiation factors, was investigated by in situ hybridization during the development of the rat submandibular gland (SMG). At the initiation stage (day 15.5 of gestation; E15), PACE4 was intensely expressed in the submandibular epithelium, but weakly expressed in the mesenchymal cells. At E16 when the branching morphogenesis becomes obvious, the expression of PACE4 in the mesenchyme was further decreased, although its level in the submandibular epithelium had not changed remarkably from that at E15. During the next stage of embryonic development (E17-E20), PACE4 was expressed in the cells derived from the submandibular epithelium, which include the proacinar, terminal tubular, and presumptive ductal cells. In the perinatal SMG, PACE4 was still expressed intensely in the terminal portion of the SMG containing the proacinar and terminal tubular cells, whereas its expression in the ductal cells was obviously decreased at the second postnatal day (P2) and at P6. Acinar cells expressing no PACE4 appeared, and their numbers increased following their development (P9-P20). At P30 when the PACE4 expression in the acinar cells was completely suppressed, its expression in the ductal cells became intense again. This temporospatially regulated expression of PACE4 suggests its apparent association with the proliferation, differentiation, and establishment of functional acinar and ductal cells of the SMG. (Keyword) Animals / Female / Gene Expression Regulation, Developmental / Gene Expression Regulation, Enzymologic / In Situ Hybridization / Morphogenesis / Pregnancy / Proprotein Convertases / RNA, Messenger / Rats / Rats, Sprague-Dawley / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1002/dvdy.21008 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17083113 ● Search Scopus @ Elsevier (PMID): 17083113 ● Search Scopus @ Elsevier (DOI): 10.1002/dvdy.21008 (DOI: 10.1002/dvdy.21008, PubMed: 17083113)
21.	Kwartarini Murdiastuti, Nunuk Purwanti, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : A naturally occurring point mutation in the rat aquaporin 5 gene, influencing its protein production by and secretion of water from salivary glands, American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.291, No.6, GI1081-GI1088, 2006. (Summary) A greater than twofold diversity in the expression level of aquaporin 5 (AQP5) has been observed in the membrane fraction of the submandibular gland (SMG) in Sprague-Dawley rats (Murdiastuti K, Miki O, Yao C, Parvin MN, Kosugi-Tanaka C, Akamatsu T, Kanamori N, and Hosoi K. Pflügers Arch 445: 405-412, 2002). In the present study, breeding between brother and sister rats was repeated within high AQP5 producers and low ones to obtain inbred offspring. High- and low-producer rats from 3rd to 18th generations were used for experiments. By Western blotting, levels of AQP5 proteins in the parotid and lacrimal glands, and lungs were all low in low producers, whereas they were all high in high producers, implying genetic variations of the gene for this water channel. Despite this implication, AQP5 mRNA levels were almost the same between the two groups by Northern blotting, suggesting the irrelevance of transcriptional regulation for this diversity. AQP5 cDNAs from the SMGs of the two groups were sequenced. The nucleotide sequence of AQP5 cDNA from low producers indicated the existence of a point mutation at nt 308 (G308A), leading to a replacement of (103)Gly with (103)Asp in the third transmembrane domain, but no alteration was detected in the Kozak area. The existence of such a mutation was confirmed by the assessment of genomic DNA also. This mutation may have resulted in an abnormal membrane insertion or ineffective trafficking of AQP5, since the rats having this mutation showed extremely low membrane expression of AQP5 in the SMG acinar cells and decreased water secretion from their salivary glands. (Keyword) Amino Acid Sequence / Animals / Aquaporin 5 / Base Sequence / Body Water / Molecular Sequence Data / Point Mutation / Rats / Salivary Glands / Sequence Homology, Amino Acid / Structure-Activity Relationship (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpgi.00449.2005 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16901987 ● Search Scopus @ Elsevier (PMID): 16901987 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00449.2005 (DOI: 10.1152/ajpgi.00449.2005, PubMed: 16901987)
22.	Chisato Kosugi, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Protein kinase A-regulated membrane trafficking of a green fluorescent protein-aquaporin 5 chimera in MDCK cells, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1763, No.4, 337-344, 2006. (Summary) The green fluorescent protein (GFP) of the jellyfish, Aeqorea victoria, was used as an autofluorescent tag to track the trafficking of aquaporin 5 (AQP5), an exocrine gland-type water channel. Two groups of chimeric proteins were constructed; one in which GFP was fused to the amino-terminus of AQP5 (GFP-AQP5) and the other, in which it was fused to the carboxyl terminus of it (AQP5-GFP). In each group, 2 chimeras were produced, a wild-type AQP5 with its normal sequence and a mutant AQP5 having a mutated amino acid at 259, i.e., GFP-AQP5-T259A and AQP5-GFP-T259A. They were used to transfect Madin-Darby canine kidney (MDCK) cells. The GFP-AQP5 chimera was localized in the intracellular vesicles, which trafficked to the plasma membrane in response to N(6), 2'-O-dibutyryladenosine 3', 5'-cyclic monophosphate (dbcAMP). Membrane trafficking was inhibited by N-[2-(p-bromocinnamylamino)ethyl]-5-isoquimolinesulfonamide (H-89) but not by palmitoyl-dl-carnitine chloride (PCC). In contrast, the AQP5-GFP chimera expressed in MDCK cells was localized constitutively on the plasma membrane. The cellular localization of the latter chimera was not affected by stimulation with dbcAMP in the presence or absence of H-89 or PCC. Replacement of Thr-259 with Ala-259 did not affect the dbcAMP-induced translocation of the chimeric protein, suggesting that phosphorylation of Thr-259 was not necessary for AQP5 trafficking under the present experimental conditions. Thus, the GFP-AQP5 chimera will be a useful tool to study AQP5 trafficking in vitro, whereas the constitutive membrane localization of the AQP5-GFP chimera suggests the importance of the carboxyl terminus of the AQP5 protein for its sorting, whether it is translocated to intracellular vesicles or to the plasma membrane. (Keyword) Animals / Aquaporin 5 / Cell Line / Cell Membrane / Cyclic AMP-Dependent Protein Kinases / Dogs / Green Fluorescent Proteins / Protein Transport / Recombinant Fusion Proteins (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbamcr.2006.02.005 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16603260 ● Search Scopus @ Elsevier (PMID): 16603260 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbamcr.2006.02.005 (DOI: 10.1016/j.bbamcr.2006.02.005, PubMed: 16603260)
23.	Masataka Murakami, Kwartarini Murdiastuti, Kazuo Hosoi and Adrian E Hill : AQP and the control of fluid transport in a salivary gland, The Journal of Membrane Biology, Vol.210, No.2, 91-103, 2006. (Summary) Experiments were performed with the perfused rat submandibular gland in vitro to investigate the nature of the coupling between transported salt and water by varying the osmolarity of the source bath and observing the changes in secretory volume flow. Glands were submitted to hypertonic step changes by changing the saline perfusate to one containing different levels of sucrose. The flow rate responded by falling to a lower value, establishing a new steady-state flow. The rate changes did not correspond to those expected from a system in which fluid production is due to simple osmotic equilibration, but were much larger. The changes were fitted to a model in which fluid production is largely paracellular, the rate of which is controlled by an osmosensor system in the basal membrane. The same experiments were done with glands from rats that had been bred to have very low levels of AQP5 (the principal aquaporin of the salivary acinar cell) in which little AQP5 is expressed at the basal membrane. In these rats, salivary secretion rates after hypertonic challenges were small and best modelled by simple osmotic equilibration. In rats which had intermediate AQP5 levels the changes in flow rate were similar to those of normal rats although their AQP5 levels were reduced.Finally, perfused normal glands were subject to retrograde ductal injection of salines containing different levels of Hg(2+) ions (0, 10 and 100 microM: ) which would act as inhibitors of AQP5 at the apical acinar membrane. The overall flow rates were progressively diminished with rising Hg(2+) concentration, but after hypertonic challenge the changes in flow rates were unchanged and similar to those of normal rats. All these results are difficult to explain by a cellular osmotic model but can be explained by a model in which paracellular flow is controlled by an osmosensor (presumably AQP5) present on the basal membrane. (Keyword) Animals / Aquaporin 5 / Biological Transport / Cell Membrane Permeability / Mercury / Models, Biological / Organ Culture Techniques / Osmolar Concentration / Perfusion / Rats / Rats, Sprague-Dawley / Salivation / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1007/s00232-005-0848-2 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16868676 ● Search Scopus @ Elsevier (PMID): 16868676 ● Search Scopus @ Elsevier (DOI): 10.1007/s00232-005-0848-2 (DOI: 10.1007/s00232-005-0848-2, PubMed: 16868676)
24.	Chenjuan Yao, Mileva Ratko Karabasil, Nunuk Purwanti, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Tissue kallikrein mK13 is a candidate processing enzyme for the precursor of interleukin-1b in the submandibular gland of mice, The Journal of Biological Chemistry, Vol.281, No.12, 7968-7976, 2006. (Summary) By using Western blot analysis, high levels of 17.5- and 20-kDa interleukin-1beta (IL-1beta) proteins were detected in the submandibular gland (SMG) of mice. Despite this fact, the amount of pro-IL-1beta protein, a precursor of IL-1beta, with a molecular size of 35 kDa in this tissue was below the detectable level, although strong expression of pro-IL-1beta mRNA was observed. A large amount of 17.5-kDa IL-1beta also appeared in the saliva of mice injected with lipopolysaccharide, suggesting that this IL-1beta is a secretory form produced by the SMG. The protein for IL-1beta-converting enzyme, a processing enzyme for pro-IL-1beta, was expressed only at a low level in the SMG as compared with its level in various epithelial tissues or lipopolysaccharide-stimulated macrophages. On the other hand, mK1, mK9, mK13, and mK22, members of the kallikrein family, were detected strongly in the SMG but not in other tissues. By incubation with mK13, but not with mK1, mK9, or mK22, the 35-kDa pro-IL-1beta was cleaved into two major products with molecular masses of 17.5 and 22 kDa, and production was inhibited by phenylmethylsulfonyl fluoride, a serine protease inhibitor, but not by IL-1beta-converting enzyme inhibitors. A peptide segment corresponding to amino acid residues 107-121 of mouse pro-IL-1beta (107WDDDDNLLVCDVPIR) was cleaved by incubation with mK13, generating two peptides, 107WDDDDNL and 114LVCDVPIR. Therefore, kallikrein mK13 would appear to hydrolyze pro-IL-1beta between its Leu113 and Leu114 residues. The results of immunohistochemistry and an autonomic therapy experiment showed that IL-1beta and kallikrein mK13 were co-localized in the secretory granules of granular convoluted tubular cells. Our present results thus suggest kallikrein mK13 is a plausible candidate for the processing enzyme for pro-IL-1beta in the SMG of mice. (Keyword) Animals / Blotting, Western / Caspases / Electrophoresis / Enzyme Inhibitors / Enzyme-Linked Immunosorbent Assay / Epithelium / Hydrolysis / Immunoblotting / Immunohistochemistry / Interleukin-1 / Isoenzymes / Kallikreins / Leucine / Lipopolysaccharides / Macrophages / Mice / Mice, Inbred C3H / Models, Genetic / Peptides / Phenylmethylsulfonyl Fluoride / Protease Inhibitors / Protein Binding / RNA, Messenger / Reverse Transcriptase Polymerase Chain Reaction / Saliva / Serine Endopeptidases / Submandibular Gland / Time Factors / Tissue Kallikreins (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.M507705200 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16423834 ● Search Scopus @ Elsevier (PMID): 16423834 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M507705200 (DOI: 10.1074/jbc.M507705200, PubMed: 16423834)
25.	Mohammad Alizadeh, Fusao Ota, Kazuo Hosoi, Makoto Kato, Tohru Sakai and Mohammed A. Satter : Altered allergic cytokine and antibody response in mice treated with Bisphenol A, The Journal of Medical Investigation : JMI, Vol.53, No.1, 2, 70-80, 2006. (Summary) The objective of this study was to elucidate if Bisphenol A (BPA) administration modulates T helper (Th) cell component of immune responses in a mouse challenged with ovalbumin (OVA), a major food antigen. BALB/c mice, (6 weeks old, female) were orally given either OVA (OVA-fed) or water (Water-fed), immunized intraperitoneally with OVA and injected with either BPA in corn oil or the vehicle alone. After subsequent 2nd immunization, serum titers of total IgE, OVA-specific IgE, IgG, IgG1 IgG2a and ability of their splenocytes for production of interferon (IFN) -gamma, interleukin (IL) -4 and IL-12 were examined by ELISA. Lymphocyte proliferation assay against concanavalin A (Con A) or OVA was also performed for 3H-Thymidine incorporation. In Water-fed groups, treatment with BPA resulted in lower titers of total IgE (P<0.01) and higher levels IgG2a (P<0.05) followed by a higher IFN-gamma (P<0.05) and IL-12 (P<0.05) with an intact IL-4. When OVA-fed groups were examined, the compound did not change production of total and OVA-specific IgE and -IgG2a but resulted in lower production of IFN-gamma (P<0.05). Also, BPA resulted in impaired lymphocyte proliferation to Con A in Water-fed groups (P<0.05) but not in tolerated animals. The findings indicate that BPA results in augmentation of Th1 immune responses but no significant effect on an established tolerance to OVA. (Keyword) Animals / Antibody Formation / Cytokines / Endocrine Disruptors / Lymphocyte Activation / Mice / Mice, Inbred BALB C / Ovalbumin / Phenols / T-Lymphocytes, Helper-Inducer (Tokushima University Institutional Repository) ● Metadata: 110790 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.53.70 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16537998 ● Search Scopus @ Elsevier (PMID): 16537998 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.53.70 (Tokushima University Institutional Repository: 110790, DOI: 10.2152/jmi.53.70, PubMed: 16537998)
26.	Keiko Tsumura, Xuefei Li, Kwartarini Murdiastuti, Most Nahid Parvin, Tetsuya Akamatsu, Chenjuan Yao, Norio Kanamori, Kiyotoshi Inenaga, Hiroshi Yamashita and Kazuo Hosoi : Downregulation of AQP2 expression in the kidney of polydipsic STR/N mice, American Journal of Physiology, Renal Physiology, Vol.290, No.2, F478-F485, 2006. (Summary) Aquaporin-2 (AQP2) is responsible for the concentration of urine in the kidney collecting tubule under the regulation of vasopressin. The mRNA level of this water channel in polydipsic STR/N mice was extremely reduced compared with that in normal ICR mice. In male mice, reduction of the AQP2 mRNA level was not evident at 3 wk of age, at which time water intake was not increased. At 10 wk of age, however, the AQP2 mRNA level was reduced to 10% of that in control mice, whereas water intake was increased by 36%. At 44 wk, the water intake became five times that of the control ICR mice, and the AQP2 mRNA level in these polydipsic mice was only approximately 5% of control. Similar changes were observed in the AQP2 protein level, suggesting that the mRNA level of AQP2 reflects the protein level of AQP2. These inverse changes in the AQP2 mRNA level and water intake were also evident in female mice. The data imply that polydipsia in STR/N mice may have affected AQP2 mRNA transcription in the kidney, resulting in reduced AQP2 expression, which would contribute to a reduction in overretention of water. (Keyword) Age Factors / Animals / Aquaporin 2 / Aquaporins / Body Weight / Diuresis / Down-Regulation / Drinking Behavior / Female / Kidney / Male / Mice / Mice, Inbred ICR / Mice, Inbred Strains / Osmolar Concentration / Polyuria / RNA, Messenger / Reverse Transcriptase Polymerase Chain Reaction / Thirst (Link to Publication Site) ● Publication site (DOI): 10.1152/ajprenal.00029.2005 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16144968 ● Summary page in Scopus @ Elsevier: 2-s2.0-33644865281 (DOI: 10.1152/ajprenal.00029.2005, PubMed: 16144968, Elsevier: Scopus)
27.	Chenjuan Yao, Xuefei Li, Murdiastuti Kwartarini, Chisato Kosugi, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Lipopolysaccharide-induced elevation and secretion of Interleukin-1b in the submandibular gland of male mice, Immunology, Vol.116, No.2, 213-222, 2005. (Summary) The intraperitoneal injection of lipopolysaccharide (LPS) (400 microg/kg body weight) induced the expression of mRNAs of inflammatory cytokines such as interleukin (IL)-1beta, IL-6 and tumour necrosis factor (TNF)-alpha in the submandibular gland (SMG) of C3H/HeN mice but not that of C3H/HeJ mice, a mutant strain for Toll-like receptor-4 (TLR-4(-) mutant). The mRNA levels of these cytokines in the SMG of the wild-type mice increased as early as 3 hr after injection, peaked at 3-6 hr, and had decreased again by 24 hr. In this study, we particularly focused on IL-1beta, and induction by this endotoxin was investigated in detail. Denervation of the superior cervical trunk and chorda tympani nerve did not diminish the LPS-induced elevation of IL-1beta mRNA in the SMG, indicating the irrelevance of the central nervous system in this induction. TLR-4 mRNA and protein were shown to be strongly expressed in the SMG, suggesting the direct action of LPS on this gland. IL-1beta proteins were localized in the secretory granules of granular convoluted tubular (GCT) cells, and their molecular weights in the gland were 17.5 and 20 kDa. IL-1beta of the same size appeared in the saliva 6 hr after LPS injection in C3H/HeN but not in C3H/HeJ mice. The present study thus suggests that IL-1beta, an inflammation cytokine, is induced and secreted into the saliva in response to endotoxin injected intraperitoneally. (Keyword) Animals / Blotting, Western / Cytokines / Gene Expression Regulation / Injections, Intraperitoneal / Interleukin-1 / Lipopolysaccharides / Male / Mice / Mice, Inbred C3H / RNA, Messenger / Reverse Transcriptase Polymerase Chain Reaction / Saliva / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1365-2567.2005.02212.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16162270 ● Search Scopus @ Elsevier (PMID): 16162270 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1365-2567.2005.02212.x (DOI: 10.1111/j.1365-2567.2005.02212.x, PubMed: 16162270)
28.	Chenjuan Yao, Wei Wei, Xuefei Li and Kazuo Hosoi : Acute phase protein induction by experimental inflammation in the salivary gland, Journal of Oral Pathology & Medicine, Vol.34, No.6, 364-367, 2005. (Summary) The submandibular gland (SMG) is a major salivary gland, which plays an important role in maintenance the oral health. In this study, we intended to explore the role of the SMG's defense system of the animals in which experimental inflammation is induced. The levels of mRNAs for inflammation cytokines and acute phase proteins were detected by reverse transcriptase-polymerase chain reaction (RT-PCR). The mRNAs for acute phase proteins were found to be increased in the SMG and extraorbital and intraorbital lacrimal gland (ELG and ILG) of rats at 24 h after subcutaneous injection of turpentine oil. The induction of mRNA for these inflammatory proteins by turpentine oil was preceded by a transient increase in the level of mRNAs for IL-1beta, IL-6 and TNF-alpha at 6 h after subcutaneous injection of the oil. Such cytokine induction was similarly seen by lipopolysaccharide (LPS) injection, and involvement of Toll-like receptor 4 (TLR4) was strongly suggested from experiment using C3H/HeJ mice, a TLR4-deficient mutant strain. The up-regulation of acute phase proteins and inflammation cytokines in the SMG, ELG and ILG by experimental inflammation suggests the existence of a strict defense system via the innate immune system in the SMG and other exocrine gland. (Keyword) Acute-Phase Proteins / Animals / Cysteine Proteinase Inhibitors / Cytokines / Interleukin-1 / Interleukin-6 / Irritants / Kininogens / Lacrimal Apparatus / Lipopolysaccharides / Male / Membrane Glycoproteins / Mice / Mice, Inbred C3H / Mice, Inbred Strains / Mice, Mutant Strains / Rats / Rats, Wistar / Receptors, Cell Surface / Sialadenitis / Submandibular Gland Diseases / Time Factors / Toll-Like Receptor 4 / Toll-Like Receptors / Tumor Necrosis Factor-alpha / Turpentine / Up-Regulation (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1600-0714.2005.00321.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15946185 ● Search Scopus @ Elsevier (PMID): 15946185 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1600-0714.2005.00321.x (DOI: 10.1111/j.1600-0714.2005.00321.x, PubMed: 15946185)
29.	Most Nahid Parvin, Shingo Kurabuchi, Kwartarini Murdiastuti, Chenjuan Yao, Chisato Kosugi, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Subcellular redistribution of AQP5 by vasoactive intestinal polypeptide (VIP) in the Brunner's gland of the rat duodenum, American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.288, No.6, G1283-G1291, 2005. (Summary) Aquaporin (AQP)5, an exocrine-type water channel, was detected in the rat duodenum by Western blot analysis, and was localized by immunohistochemistry in the secretory granule membranes as well as in the apical and lateral aspects of the plasma membrane of Brunner's gland cells. Incubation of duodenal slices with vasoactive intestinal polypeptide (VIP) in vitro significantly increased the amount of AQP5 in the apical membrane fraction in a dose- and time-dependent manner with the amount reaching a plateau at 100 nM VIP and becoming near maximal after a 30-s incubation. Protein kinase inhibitors, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride (H-7, 50 muM), and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89; PKA-specific, 1 muM) blocked this increase, but PKC-specific inhibitor calphostin C did not, implying the involvement of PKA but not PKC in this cellular event. Intravenous injection with VIP (40 mug/kg body wt) provoked dilation of the lumen of the Brunner's gland at 2 and 7 min and increased the staining intensity of AQP5 in the apical and lateral membranes. AQP1 (both nonglycosylated and glycosylated forms) was also found to localize in the apical and basolateral membranes of cells of Brunner's gland. VIP, however, did not provoke any significant change in the AQP1 level in the apical membrane, as judged from the results of the above in vitro and in vivo experiments. These results suggest that VIP induced the exocytosis of granule contents and simultaneously caused translocation of AQP5 but not of AQP1 to the apical membrane in Brunner's gland cells. (Keyword) Animals / Aquaporin 1 / Aquaporin 5 / Aquaporins / Brunner Glands / Dose-Response Relationship, Drug / Exocytosis / Intracellular Signaling Peptides and Proteins / Male / Membrane Proteins / Protein Kinases / Rats / Rats, Sprague-Dawley / Vasoactive Intestinal Peptide (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpgi.00030.2004 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15650134 ● Search Scopus @ Elsevier (PMID): 15650134 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00030.2004 (DOI: 10.1152/ajpgi.00030.2004, PubMed: 15650134)
30.	Shingo Kurabuchi, Edward W Gresik and Kazuo Hosoi : Additive and/or synergistic action (downregulation) of androgens and thyroid hormones on the cellular distribution and Localization of a true tissue kallikrein, mK1, in the mouse submandibular gland, The Journal of Histochemistry and Cytochemistry, Vol.52, No.11, 1437-1446, 2004. (Summary) We investigated the effects of 5alpha-dihydrotestosterone (DHT), 3,5,3'-triiodo-l-thyronine (T(3)), and dexamethasone (Dex) on the expression of mK1 in the granular convoluted tubule (GCT) cells of the submandibular gland (SMG) of hypophysectomized (Hypox) male mice by indirect enzyme-labeled antibody and immunogold antibody methods for light and electron microscopy. Hypox resulted in considerable atrophy of the GCT cells, which were always immunoreactive for mK1, and the cells were characterized by apical small dense secretory granules labeled with gold particles suggesting the presence of mK1, small Golgi apparatus, sparse rough endoplasmic reticulum (RER), and developed basal infoldings. Each of the hormones, DHT, T(3), and Dex, enhanced the GCT phenotype to various degrees in Hypox male mice. Both DHT alone and T(3) alone moderately inhibited mK1 synthesis by increasing the number of mK1-immunonegative GCT cells in Hypox males, but Dex alone had no inhibitory effect on mK1 synthesis. A significant trophic effect on GCT cells was induced by combined injection of DHT and T(3) or of all three hormones, and was reflected in the appearance of abundant large secretory granules, well-developed Golgi apparatus and RER, and reduced basal infoldings. Only a few such GCT cells were immunopositive for mK1, and the pattern of immunopositive and immunonegative cells very closely resembled the mosaic pattern seen in normal male GCTs. These findings suggested that the sexual dimorphism of mK1 expression and the morphological appearance of GCT cells can be induced by treatment with two hormones, DHT and T(3), but not by either of them alone. T(3) appears to have a permissive effect on committed GCT cells that results in downregulation of mK1 expression in these cells. (Keyword) Androgens / Animals / Dexamethasone / Dihydrotestosterone / Down-Regulation / Female / Immunohistochemistry / Male / Mice / Mice, Inbred ICR / Microscopy, Electron / Submandibular Gland / Thyroid Hormones / Tissue Kallikreins / Triiodothyronine (Link to Publication Site) ● Publication site (DOI): 10.1369/jhc.4A6333.2004 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15505338 ● Search Scopus @ Elsevier (PMID): 15505338 ● Search Scopus @ Elsevier (DOI): 10.1369/jhc.4A6333.2004 (DOI: 10.1369/jhc.4A6333.2004, PubMed: 15505338)
31.	Shingo Kurabuchi and Kazuo Hosoi : Immunocytochemical localization of mK1, a true tissue kallikrein, in the mouse parotid gland: sexual dimorphism and effects of castration and hypophysectomy, Odontology, Vol.92, No.1, 73-76, 2004. (Summary) In the normal parotid glands of mice at 12 weeks of age, mK1, a true tissue kallikrein, was detected at the apical rim of the striated ducts (SDs). Sexual dimorphism in the immunostaining intensity in parotid glands was seen, i.e., immunostaining was more intense in males than in females. Under electron microscopy, secretory granules, being small in size, and condensed at the subluminal cytoplasm, were labeled with immunogold particles showing the presence of mK1. These secretory granules were rather abundant and large in males. Castration in males reduced the immunoreactivity of mK1 in the SD cells because of a decrease in the number and size of secretory granules as revealed by electron microscopy. Hypophysectomy in male mice resulted in considerable loss of immunoreactivity for mK1, which was characterized under electron microscopy by complete disappearance or significant reduction of secretory granules in many SD cells. These results suggest that mK1 expression in the SD cells of murine parotid glands is regulated by pituitary-dependent hormones, and sexual dimorphism of mK1 expression is regulated by androgens. (Keyword) A true tissue kallikrein / Immunocytochemistry / Parotid gland / Castration / Hypophysectomy / Mouse (Link to Publication Site) ● Publication site (DOI): 10.1007/s10266-004-0040-7 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15490309 ● CiNii @ National Institute of Informatics (CRID): 1571980074816943104 ● Search Scopus @ Elsevier (PMID): 15490309 ● Search Scopus @ Elsevier (DOI): 10.1007/s10266-004-0040-7 (DOI: 10.1007/s10266-004-0040-7, PubMed: 15490309, CiNii: 1571980074816943104)
32.	Sandro E. Fogaça, Robson L. Melo, Daniel C. Pimenta, Kazuo Hosoi, Luiz Juliano and Maria A. Juliano : Difference in substrate and inhibitor sequence specificity of human, mouse and rat tissue kallikreins, The Biochemical Journal, Vol.380, No.Pt3, 775-781, 2004. (Summary) The kininogenase activities of mouse (mK1), rat (rK1) and human (hK1) tissue kallikreins were assayed with the bradykinin-containing synthetic peptides Abz-MTEMARRPPGFSPFRSVTVQNH2 (where Abz stands for o-aminobenzoyl) and Abz-MTSVIRRPPGFSPFRAPRV-NH2, which correspond to fragments Met374-Gln393 and Met375-Val393 of mouse and rat LMWKs (low-molecular-mass kininogens) with the addition of Abz. Bradykinin was released from these peptides by the mK1- and rK1-mediated hydrolysis of Arg-Arg and Arg-Ser (or Arg-Ala) peptide bonds. However, owing to preferential hydrolysis of Phe-Arg compared with the Arg-Ala bond in the peptide derived from rat LMWK, hK1 released bradykinin only from the mouse LMWK fragment and preferentially released des-[Arg9]bradykinin from the rat LMWK fragment (Abz-MTSVIRRPPGFSPFRAPRV-NH2). The formation of these hydrolysis products was examined in more detail by determining the kinetic parameters for the hydrolysis of synthetic, internally quenched fluorescent peptides containing six N- or C-terminal amino acids of bradykinin added to the five downstream or upstream residues of mouse and rat kininogens respectively. One of these peptides, Abz-GFSPFRAPRVQ-EDDnp (where EDDnp stands for ethylenediamine 2,4-dinitrophenyl), was preferentially hydrolysed at the Phe-Arg bond, confirming the potential des-[Arg9]bradykinin-releasing activity of hK1 on rat kininogen. The proline residue that is two residues upstream of bradykinin in rat kininogen is, in part, responsible for this pattern of hydrolysis, since the peptide Abz-GFSPFRASRVQ-EDDnp was preferentially cleaved at the Arg-Ala bond by hK1. Since this peptidase accepts the arginine or phenylalanine residue at its S1 subsite, this preference seems to be determined by the prime site of the substrates. These findings also suggested that the effects observed in rats overexpressing hK1 should consider the activation of B1 receptors by des-[Arg9]bradykinin. For further comparison, two short internally quenched fluorescent peptides that bind to hK1 with affinity in the nM range and some inhibitors described previously for hK1 were also assayed with mK1 and rK1. (Keyword) Amino Acid Sequence / Animals / Bradykinin / Enzyme Inhibitors / Female / Fluorescent Dyes / Humans / Hydrolysis / Kinins / Mice / Mice, Inbred ICR / Molecular Sequence Data / Peptide Fragments / Peptides / Rats / Substrate Specificity / Tissue Kallikreins (Link to Publication Site) ● Publication site (DOI): 10.1042/BJ20031047 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15040788 ● Search Scopus @ Elsevier (PMID): 15040788 ● Search Scopus @ Elsevier (DOI): 10.1042/BJ20031047 (DOI: 10.1042/BJ20031047, PubMed: 15040788)
33.	Tetsuya Akamatsu, Most Nahid Parvin, Kwartarini Murdiastuti, Chisato Kosugi, Chenjuan Yao, Osamu Miki, Norio Kanamori and Kazuo Hosoi : Expression and localization of aquaporins, members of the water channel family, during development of the rat submandibular gland., Pflügers Archiv : European Journal of Physiology, Vol.446, No.6, 641-651, 2003. (Summary) The expression and localization of aquaporins (AQP1-AQP5), members of the water channel family, in the developing rat submandibular gland were analysed using RT-PCR, Northern blotting and immunohistochemistry to explore their relation to the development of this salivary gland. RT-PCR analysis revealed unique expression patterns of each AQP. AQP1 was expressed constitutively during prenatal development, whereas the expression of AQP5 became more intense in the course of development from embryonic day 16.5 (E16) to E20. These expression patterns concurred with the results of Northern blot analysis. AQP3 and AQP4 mRNAs in the prenatal development were not detected in Northern blots, although they were detected by RT-PCR. During postnatal development, AQP5 and AQP1 mRNAs were expressed continuously, but no message for AQP3 or AQP4 was detected. AQP2 mRNA was not detected during either prenatal or postnatal development in this tissue. Immunohistochemical studies revealed that AQP5 was first localized at the apical membrane of proacinar cells at E18, and then became clearly distributed at the apical membrane of acinar cells in accordance with the differentiation and establishment of the mature acini. In addition, some vasculature also showed immunoreactivity for AQP5. AQP1 was immunolocalized in the blood vessels, including capillaries, of the gland throughout development. These observations suggest the existence of transcriptional regulation of rat AQP5, which is one of the most probable regulators of saliva production and secretion, during the establishment of the functional submandibular salivary gland. (Keyword) Aging / Amino Acid Sequence / Animals / Aquaporins / Biological Transport, Active / Blotting, Northern / Body Water / Female / Immunohistochemistry / Molecular Sequence Data / Pregnancy / RNA / RNA, Antisense / Rats / Rats, Sprague-Dawley / Reverse Transcriptase Polymerase Chain Reaction / Sodium-Potassium-Exchanging ATPase / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1007/s00424-003-1109-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12838423 ● Search Scopus @ Elsevier (PMID): 12838423 ● Search Scopus @ Elsevier (DOI): 10.1007/s00424-003-1109-9 (DOI: 10.1007/s00424-003-1109-9, PubMed: 12838423)
34.	Kwartarini Murdiastuti, Osamu Miki, Chenjuan Yao, Most Nahid Parvin, Chisato Kosugi, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Divergent expression and localization of aquaporin 5, an exocrine-type water channel, in the submandibular gland of Sprague-Dawley rats., Pflügers Archiv : European Journal of Physiology, Vol.445, No.3, 405-412, 2002. (Summary) 正常SDラット唾液腺(顎下腺)のAQP5蛋白質発現レベルを調べた所，高発現ラットおよび低発現ラットが存在する事を見いだした．2種のラットを近交化する目的で兄妹交配を進め，現在高発現ラットは8代目に，また低発現ラットは4代目に到った．これらのラットでは発現レベルの差は100倍以上に達した．AQP5蛋白質発現レベルの差は耳下腺，肺，涙腺においても認められたが，AQP5 mRNAレベルはいずれの臓器においても両グループ間で差はなかった．したがって，上記2グループ間で認められたAQP5蛋白質発現レベルの差異はAQP5遺伝子あるいはそのプロモーターに発生した遺伝的変異に基づくものと考えられた． (Keyword) aquaporin 5 / genetic variation / Sprague-Dawley (SD) rat / submandibular gland / KIDNEY COLLECTING DUCT / MOLECULAR-CLONING / FUNCTIONAL EXPRESSION / BASOLATERAL MEMBRANE / EPITHELIAL-CELLS / LACRIMAL GLANDS / PROTEIN / IMMUNOLOCALIZATION / GLYCEROL / UREA (Link to Publication Site) ● Publication site (DOI): 10.1007/s00424-002-0940-8 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1007/s00424-002-0940-8 (DOI: 10.1007/s00424-002-0940-8)
35.	Shingo Kurabuchi, Kazuo Hosoi and Edward W Gresik : Developmental and androgenic regulation of the immunocytochemical distribution of mK1, a true tissue kallikrein, in the granular convoluted tubule of the mouse submandibular gland, The Journal of Histochemistry and Cytochemistry, Vol.50, No.2, 135-145, 2002. (Summary) The action of androgens on the immunocytochemical distribution of mK1, a true tissue kallikrein, was examined in the submandibular gland (SMG) of developing and adult mice by indirect enzyme-labeled and immunogold-labeled antibody methods for light and electron microscopy, respectively. In both sexes at 3 weeks of age, essentially all of the immature granular convoluted tubule (GCT) cells were uniformly immunostained. At 4 weeks of age (the onset of puberty), morphological differences between the two sexes appeared in the GCTs, in which some cells became immunonegative. Thereafter, the immunonegative GCT cells became more abundant in the SMG of males than of females and considerable intercellular variation in staining intensity for mK1 was seen, especially in males. A few slender GCT cells with strong immunoreactivity appeared in GCT segments only in males. Castration of males resulted in an increase in the number of immunopositive GCT cells, whereas administration of dihydrotestosterone (DHT) decreased the number of immunopositive GCT cells in the SMGs of both sexes. Slender GCT cells immunoreactive for mK1 were seen in females treated with DHT for 6 days. However, there were no immunostained slender GCT cells in female SMGs after injection of DHT for 2 weeks. Immunoelectron microscopy disclosed this type of cell in male SMGs, which closely resembles immature GCT cells of prepubertal mice, with a few small secretory granules uniformly labeled with gold particles, a sparse Golgi apparatus and RER, and basal infoldings. In mature male SMGs and in SMGs of DHT-treated females and castrated males, typical GCT cells had a well-developed Golgi apparatus and a net-like RER but few to no basal infoldings, whereas in the female gland equivalent cells had moderately developed RER and some basal infoldings. These results suggest that mK1 is one of the enzymes characteristically present in immature GCT cells and that its synthesis is inhibited in part by androgens, resulting in decreased numbers of immunopositive cells. (Keyword) Aging / Animals / Castration / Dihydrotestosterone / Female / Immunohistochemistry / Male / Mice / Mice, Inbred ICR / Sex Factors / Submandibular Gland / Tissue Kallikreins (Link to Publication Site) ● Publication site (DOI): 10.1177/002215540205000202 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11799133 ● Search Scopus @ Elsevier (PMID): 11799133 ● Search Scopus @ Elsevier (DOI): 10.1177/002215540205000202 (DOI: 10.1177/002215540205000202, PubMed: 11799133)
36.	Most Nahid Parvin, Keiko Tsumura, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Expression and localization of AOP5 in the stomach and duodenum of the rat., Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1542, No.1-3, 116-124, 2002. (Summary) 消化管におけるアクアポリン5(AQP5)の発現を，RT-PCRおよびウェッスタンブロッティングによってしらべ，下部胃および十二指腸にその強い発現を認めた．検出したAQP5蛋白質は従来の報告のとおり27kDaであった．発現部位は胃では幽門腺，十二指腸ではブルーナー腺であった．これらの結果はAQP5は胃および十二指腸における水分泌に関与する可能性を示唆する． (Keyword) Animals / Aquaporin 5 / Aquaporins / Biological Transport / Duodenum / Fluorescein-5-isothiocyanate / Gastric Mucosa / Immunohistochemistry / Male / Membrane Proteins / RNA, Messenger / Rats / Rats, Sprague-Dawley / Reverse Transcriptase Polymerase Chain Reaction / Stomach / Water (Link to Publication Site) ● Publication site (DOI): 10.1016/S0167-4889(01)00172-0 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11853885 ● Search Scopus @ Elsevier (PMID): 11853885 ● Search Scopus @ Elsevier (DOI): 10.1016/S0167-4889(01)00172-0 (DOI: 10.1016/S0167-4889(01)00172-0, PubMed: 11853885)
37.	Norio Kanamori, Tetsuya Akamatsu, Chisato Kosugi, Most Nahid Parvin and Kazuo Hosoi : Methylene blue as a vascular filling dye., ITE Leters on Batteries, New Technologies & Medicine (with News), Vol.3, No.1, 75-77, 2002. (Summary) メチレンブルー溶液とピクリン酸溶液とを混合すると，色素の濃度に依存して，ゲル状∼ゴム状の沈澱を生ずることを見出した．この沈殿物を回収してその吸収パターンを計測した結果，メチレンブルーそのものであり，ピクリン酸との化合物や共沈殿物ではないことが判明した．すなわち，ピクリン酸による塩析効果によって色素が沈澱する．ピクリン酸を含むブアン液によって潅流固定した実験動物の血管内にメチレンブルー溶液を注入することにより，生成したゴム状またはゲル状の茶色の色素によって血管内を満たすことができる．通常の色素による染色では，すべての血管が染色され，組織は瀰慢性に濃染してしまう．この新たに開発した方法は，色素濃度を加減することによって生成物の粘性を選ぶことができ，色素進入の血管径を選択できるので，太い血管から順に色素を充填することが可能で，血管網のin situ観察に高い利用価値を有する．
38.	Shingo Kurabuchi, Kazuo Hosoi and Edward W Gresik : Androgen regulation of the cellular distribution of the true tissue kallikrein mK1 in the submandibular gland of the mouse, The Journal of Histochemistry and Cytochemistry, Vol.49, No.6, 801-802, 2001. (Summary) The kallikrein gene family encodes for at least four different proteases in the mouse submandibular gland (SMG): mK1 (true tissue kallikrein), mK9, mK13, and mK22. These enzymes and many other biologically active proteins are synthesized by the granular convoluted tubule (GCT), a specialized segment of the SMG duct system. The GCT is under multihormonal regulation by androgens, thyroid hormones, and adrenocortical hormones. Androgens suppress synthesis of mK1 in the SMG but enhance expression of the other three kallikreins. We prepared an antibody with limited immunoreactivity for mK1 and used it to examine the effects of androgen status on the distribution of this isozyme in the SMGs of developing and mature mice by immunoperoxidase staining for the light microscope and immunogold labeling for the electron microscope. In prepubertal mice, every immature GCT cell contains mK1, confined to an accumulation of small granules in the subluminal cytoplasm. In mature mice, not every GCT cell contains mK1, and in those cells that do there is considerable intergranular variation in the intensity of staining for mK1. GCT cells containing mK1 are much more abundant in the glands of females than of males, resulting in a peculiar sexually dimorphic mosaic distribution of this isozyme in the mature SMG. Castration of adult males increases the number of GCT cells expressing mK1. Administration of androgen to intact or castrated males or to intact females reduces the number of cells staining for mK1. In all cases, immunogold labeling for mK1 is confined to secretory granules. No fine structural differences were noted between cells that were positively or negatively stained for mK1. Therefore, although GCT cells appear to be composed of a uniform population of cells on the basis of morphology alone, they are not homogeneous in their content of secretory proteins. These results indicate that androgen regulation of GCT cells is more complex than has been appreciated to date. (Keyword) Androgens / Animals / Antibody Specificity / Female / Immunoenzyme Techniques / Isoenzymes / Male / Mice / Phenotype / Sex Characteristics / Sexual Maturation / Submandibular Gland / Tissue Distribution / Tissue Kallikreins (Link to Publication Site) ● Publication site (DOI): 10.1177/002215540104900618 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11373331 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034971585 (DOI: 10.1177/002215540104900618, PubMed: 11373331, Elsevier: Scopus)
39.	Wei Wei, Most Nahid Parvin, Keiko Tsumura, Tetsuya Akamatsu, Jun Tada, Norio Kanamori and Kazuo Hosoi : Induction of C-reactive protein, serum amyloid P component, and kininogens in the submandibular and lacrimal glands of rats with experimentally induced inflammation., Life Sciences, Vol.69, No.3, 359-368, 2001. (Summary) テルペンチン油を投与した実験的炎症モデルラットにおいて，投与24時間後に，C-反応生蛋白質，血清アミロイド蛋白質，H-およびT-キニノーゲンのmRNAが，顎下腺，眼窩内および眼窩外涙腺に誘導されることを見いだした．投与6時間後に，この誘導に先立って，TNF-αmRNAが誘導された．顎下腺，眼窩内および眼窩外涙腺におけるこれら急性期蛋白質の誘導は，外分泌腺に強い防御系が存在することを示唆するものと考えられる．
40.	Most Nahid Parvin, Kwartarini Murdiastuti, Tetsuya Akamatsu, Norio Kanamori, Norihiko Maeda and Kazuo Hosoi : Expression and locarization of AQP4 in the crypt epithelial cells of the rat duodenum., Biomedical Research (India), Vol.12, No.2, 77-82, 2001. (Summary) RT-PCRによってアクアポリン4(AQP4)の消化管における発現を調べた．AQP4は下部胃，十二指腸，空腸，回腸，盲腸，大腸，および直腸に発現していたが上部胃ニは発現を認めなかった．ウェッスタンブロッティングで十二指腸に30kDaのAQP4蛋白質の発現を認めた．滅め貴組織化学実験によりAQP4は十二指腸上皮の陰窩細胞の基底側膜に局在したが絨毛細胞には局在しなかった．
41.	Norio Kanamori, Tetsuya Akamatsu, Jun Tada, Keiko Tsumura, Most Nahid Parvin, Kwartarini Murdiastui, Wei Wei and Kazuo Hosoi : Search for the dye that stains the vascular system., ITE Leters on Batteries, New Technologies & Medicine (with News), Vol.2, No.1, 116-119, 2001. (Summary) 血管系の，特に動脈系に特異的なin situ染色法を開発する目的で，数種の染料を選び，その染色性その他の諸性質を検討した．いくつかの候補の中から，ルクソールファストブルーが最も望ましい性質を有することを明らかにした．すなわち，同色素溶液はピクリン酸溶液と接触すると複塩または錯塩を生成し，原色素とは異なる吸収曲線を呈する沈澱を生じる．ピクリン酸を含む固定液で潅流したのち左心室より同色素液を注入すると，動脈系だけが染色される．このようなin situ血管染色法は，今までになかったものである．
42.	Tetsuya Akamatsu, Yoshiko Matsuda, Keiko Tsumura, Jun Tada, Most Nahid Parvin, Wei Wei, Norio Kanamori and Kazuo Hosoi : Highly regulated expression of subtilisin-like proprotein convertase PACE4 (SPC4) during dentinogenesis., Biochemical and Biophysical Research Communications, Vol.272, No.2, 410-415, 2000. (Summary) Expressions of mRNAs for four subtilisin-like proprotein convertases (SPCs: furin, PACE4, PC6, and PC8) and bone morphogenetic protein 4 (BMP4) in the rat molar tooth during development were analyzed by Northern blotting, reverse transcriptase-polymerase chain reaction (RT-PCR), and in situ hybridization to explore the possible involvement of SPCs in the processing of proBMPs. We found a temporospacial expression of PACE4, but not one of the other SPCs, in this tissue; i.e., RT-PCR analysis revealed that the level of PACE4 mRNA, but not that of the other SPC mRNAs became high around the second postnatal day. This increase was in good accordance with the increase in BMP4 mRNA, indicating an apparent association of these molecules with the differentiation and establishment of functional ameloblasts and odontoblasts. During dentinogenesis, PACE4 mRNA was localized in the ameloblasts and odontoblasts. These observations suggest that PACE4 plays a crucial role in dentinogenesis, especially via the activation of BMPs. (Keyword) Processing protease / PACE4 / Dentinogenesis / Gene expression (Link to Publication Site) ● Publication site (DOI): 10.1006/bbrc.2000.2752 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10833428 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034616641 (DOI: 10.1006/bbrc.2000.2752, PubMed: 10833428, Elsevier: Scopus)
43.	Kazuo Hosoi, Sachiko Matsuura, Keiko Tsumura, Wei Wei, Most Nahid Parvin, Jun Tada, Tetsuya Akamatsu, Norio Kanamori and Kazuo Suzuki : Expression of kininogens in the connective tissue-type mast cells of the rats., Immunology, Vol.101, No.4, 531-540, 2000. (Summary) The connective tissue-type mast cells present in the submandibular gland (SMG) and peritoneal cavity of rats were found to express kininogens (KGs), the expression of which was demonstrated by Western blotting, reverse transcription-polymerase chain reaction (RT-PCR), RT-PCR Southern blotting, and light- and electron-microscopic immunocytochemistry. In the SMG, the analysis of cDNA amplified by RT-PCR revealed that the molecular species of mRNAs expressed were high-molecular-weight (HMW)-K KG and T-I KG. Light microscopic immunocytochemistry exclusively localized the KG protein(s) in the mast cells present in the SMG. The signals in the mast cells were very strong, but no positive reaction was observed in the granular convoluted tubular cells, acinar cells or striated duct cells. As determined by using electron microscopy, extremely strong labelling with immunogold was observed in the secretory granules of the mast cells, but no labelling in their nucleus or cytoplasm. Analysis by Western blotting and RT-PCR Southern blotting indicated that both protein and mRNA of KGs were present in the mast cells separated from the peritoneal cavity, indicating de novo synthesis of KG in these cells. Preliminary experiments implied that the connective tissue-type mast cells in other rat tissues also expressed KG. (Keyword) Animals / Ascitic Fluid / Blotting, Western / Gene Expression / Immunoenzyme Techniques / Kininogens / Male / Mast Cells / Molecular Weight / RNA, Messenger / Rats / Rats, Wistar / Reverse Transcriptase Polymerase Chain Reaction / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1046/j.1365-2567.2000.00132.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11122457 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034537325 (DOI: 10.1046/j.1365-2567.2000.00132.x, PubMed: 11122457, Elsevier: Scopus)
44.	Tetsuo Ichikawa, Yoko Terada, Katsuhiko Hirota, Yoichiro Miyake and Kazuo Hosoi : Study on oral health care and general health of elderly (in Japanese), Dentistry in Japan, Vol.19, 75-80, 2000. (Keyword) 高齢者 / 口腔 / 咽頭細菌 / 唾液 / 舌
45.	Jun Tada, Takamasa Sawa, Naoki Yamanaka, Masayuki Shono, Tetsuya Akamatsu, Keiko Tsumura, Most Nahid Parvin, Norio Kanamori and Kazuo Hosoi : Involvement of vesicle-cytoskeleton interaction in AQP5 trafficking in AQP5-gene-transfected HSG cells., Biochemical and Biophysical Research Communications, Vol.266, No.2, 443-447, 1999. (Summary) ヒト唾液腺細胞にアクアポリン5(AQP5)を遺伝子導入したところ，AQP5蛋白質は細胞内の小胞に発現した．タプシガージン等により細胞内カルシウムを上昇させると小胞のAQP5蛋白質は細胞膜へ移動した．さらに微小管阻害剤である，コルヒチンおよびビンブラスチンはこの移動を抑制した．AQP5のトラッフィッキングは微小管が関与して入る可能性が示唆された． (Keyword) Aquaporin 5 / Water channel / Trafficking / Cytoskeleton
46.	Tetsuya Akamatsu, Yoshiko Matsuda, Keiko Tsumura, Jun Tada, Most Nahid Parvin, Norio Kanamori and Kazuo Hosoi : Subtilisin-like proprotein convertase PACE4 (SPC4) is a candidate processing enzyme of bone morphogenetic proteins during tooth formation, Developmental Dynamics, Vol.216, No.4/5, 481-488, 1999. (Summary) サチライシン様プロセシング酵素PACE4が歯牙形成過程において時期·空間特異的に発現し，歯牙形成に必須の骨形成蛋白質群(BMPs)と一致して局在することから， PACE4が歯牙形成時の最も有力なBMPsプロセシング酵素で， BMPsの活性化によりエナメル芽細胞と象牙芽細胞の分化成熟と密接に関わることを見い出した． (Keyword) Processing protease / PACE4 / Bone morphogenetic protein / Tooth / Development
47.	Shingo Kurabuchi, Jun Tada, Edward W Gresik and Kazuo Hosoi : An unusual sexually dimorphic mosaic distribution of a subset of kallikreins in the granular convoluted tubule of the mouse submandibular gland detected by an antibody with restricted immunoreactivity, The Histochemical Journal, Vol.31, No.1, 19-28, 1999.
48.	Norihiko Maeda, Koichi Ogata, Setsuko Suemune, Yuji Yoshiko, Shumpei Niida, Mitsuteru Hosoi, Keita Hirano, Kazuo Hosoi and Katsunobu Miyata : Co-localization of estrogen and androgen receptors immunoreactivities in the trigeminal motor nucleus, Biomedical Research (India), Vol.9, No.3, 187-193, 1998.
49.	Kazuo Hosoi, Jun Tada, Keiko Tsumura, Norio Kanamori and Naoki Yamanaka : Expression of an alloenzyme of prorenin-converting enzyme in the submandibular gland of DBA/2N mice., The Journal of Biochemistry, Vol.124, No.2, 368-376, 1998. (Summary) DBA/2Nマウス顎下腺抽出液に等電点8.7の新種カリクレイン酵素を見いだした．本酵素のアミノ酸配列はmK13およびmK26(プロレニン変換酵素1及2)と酷似していた．本酵素に対応するcDNAをクローニングし，その配列を解析し，このcDNAは全783塩基中，mKlk13およびmKlk26とそれぞれ6および12塩基異なる事を明らかにした．本酵素はmK13アロ酵素(mK13b)であると考えられた．
50.	Yamato Kikkawa, Naoki Yamanaka, Jun Tada, Norio Kanamori, Keiko Tsumura and Kazuo Hosoi : Prorenin processing and restricted endoproteolysis by mouse tissue kallikrein family ezymes (mK1, mK2, mK13, and mK22)., Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol.1382, No.1, 55-64, 1998. (Summary) Four members of the tissue kallikrein family, mK1, mK9, mK13, and mK22, all of which exhibit extensive homology in amino acid sequence among themselves, were obtained from the submandibular gland of ICR mice and examined for their ability to cleave prorenin. Tissue kallikrein mK13 was confirmed to be a prorenin-converting enzyme; and mK9, which was earlier shown to be an EGF-binding protein, was found to cleave mouse Ren 2 prorenin specifically and convert it to mature renin with an activity of approximately 1/10 of that of mK13. With the same substrate, mK22 (beta-NGF endopeptidase) gave two products, renin and arginyl-renin; whereas mK1 (true tissue kallikrein) did not process it at all. The endoproteolytic activity of tissue kallikreins was examined with various peptide-MCA substrates. The substrates contained three key structures; X(Y)-Arg-Arg, X(Y)-Lys-Arg and X-Lys-Lys motifs (where X and Y are hydrophilic and hydrophobic amino acids, respectively). We found that mK1, mK9 and mK13 preferentially cleaved the former two types of substrate, except Y-Arg-Arg-MCA. The substrate X-Lys-Lys-MCA was hardly cleaved by these three tissue kallikreins but was preferentially cleaved by mK22. The four tissue kallikreins seem to have the ability to process precursor proteins containing a pair of basic amino acid residues; the specificities of three of the enzymes (mK1, mK9 and mK13) were similar to each other but were different from that of mK22. (Keyword) Amino Acid Sequence / Animals / Enzyme Precursors / Isoenzymes / Kallikreins / Kinetics / Male / Mice / Mice, Inbred ICR / Molecular Sequence Data / Protein Processing, Post-Translational / Renin / Submandibular Gland / Substrate Specificity (Link to Publication Site) ● Publication site (DOI): 10.1016/S0167-4838(97)00144-1 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9507064 ● Summary page in Scopus @ Elsevier: 2-s2.0-0031911945 (DOI: 10.1016/S0167-4838(97)00144-1, PubMed: 9507064, Elsevier: Scopus)
51.	Kinji Kurihara, Shichiro Maruyama, Kazuo Hosoi, Seiichi Sato, Takao Ueha and Edward W Gresik : Regulation of Na+,K+-ATPase in submandibular glands of hypophysectomized male mice by steroid and thyroid hormones, The Journal of Histochemistry and Cytochemistry, Vol.44, No.7, 703-711, 1996.
52.	Yoshifumi Tajima, Kohtaro Kato, Shichiro Maruyama and Kazuo Hosoi : In vivo modulation of proliferating cell nuclear antigen in growth plate chondrocytes from normal, hypophysectomized, and growth hormone-treated hypophysectomized rats -A comparative immunohistochemical study with image analysis-, The Journal of Histochemistry and Cytochemistry, Vol.44, No.7, 713-720, 1996.
53.	Kazuo Hosoi, Yoshimi Shioda, Takao Ueha, Toshiko Atsumi, Kenji Sugita and Kinji Kurihara : ATP- and EGF-stimulated phosphatidylinositol synthesis by two different pathways, phospholipase D and diacylglycerol kinase, in A-431 epidermoid carcinoma cells, Biochemistry and Cell Biology, Vol.74, No.2, 197-209, 1996.
54.	Kinji Kurihara, Shichiro Maruyama, Kazuo Hosoi, Edward W Gresik and Takao Ueha : Effects of steroids and thyroid hormones on Na+,K+-ATPase activity and localization of its a subunit protein in submandibular gland of hypophysectomized mice (in Japanese), Journal of the Japan Salivary Gland Society, Vol.36, 41-43, 1995.
55.	Kazuo Hosoi : The molecular diversity of salivary kallikreins (prorenin converting enzymes)(in Japanese), Journal of the Japan Salivary Gland Society, Vol.36, 60-61, 1995.
56.	Kenji Sugita, Kinji Kurihara, Kazuo Hosoi, Toshiko Atsumi, Tsutomu Takahashi, Minoru Kohno and Takao Ueha : Effects of pertussis toxin on signal transduction via P2-purinergic receptors in A-431 human epidermoidal carcinoma cells, Enzyme and Protein, Vol.48, No.4, 222-228, 1995.
57.	Hiroshi Kamioka, Yoshiki Miki, Koji Sumitani, Kahori Tagami, Kunihiro Terai, Kazuo Hosoi and Terushige Kawata : Extracellular calcium causes the release of calcium from intracellular stores in chick osteocytes, Biochemical and Biophysical Research Communications, Vol.212, No.2, 692-696, 1995.
58.	Jianxiang Qu, Kazuo Hosoi, Takahiro Shimojima, Tsuyoshi Oi and Katsumi Ikeda : Effects of FMLP and LPS on [Ca²⁺]i of peritoneal exudate polymorphonuclear leukocytes following onset of inflammation, Journal of Periodontal Research, Vol.30, No.3, 153-158, 1995.
59.	Kazuo Hosoi, Kinji Kurihara and Takao Ueha : The molecular diversity and physiological function of salivary kallikreins (in Japanese), Journal of the Japan Salivary Gland Society, Vol.35, 50-52, 1994.
60.	Yoshifumi Tajima, Kohtaro Kato, Nobuo Utsumi and Kazuo Hosoi : Computer-aided image analysis applied to immunogold-silver staining: evaluation of proliferating cell nuclear antigen (PCNA)-reactive sites in paraffin sections, Histochemistry, Vol.102, No.3, 177-181, 1994.
61.	Toshiko Atsumi, Kazuo Hosoi and Takao Ueha : Involvement of high-affinity binding site for EGF receptor in formation of rounding in A-431 epidermoid carcinoma cells, Hormone and Metabolic Research, Vol.26, No.3, 141-144, 1994.
62.	Kazuo Hosoi, Susumu Tsunasawa, Kinji Kurihara, Hideyuki Aoyama, Takao Ueha, Toyoaki Murai and Fumio Sakiyama : Identification of mK1, a true tissue (glandular) kallikrein of mouse submandibular gland: Tissue distribution and a comparison of kinin-releasing activity with other submandibular kallikreins, The Journal of Biochemistry, Vol.115, No.1, 137-143, 1994.
63.	Kinji Kurihara, Kazuo Hosoi, Takao Ueha, Nobuo Nakanishi and Shozo Yamada : Effects of nerve growth factor and dexamethasone on Na+,K+-ATPase of cultured PC12 cells, Hormone and Metabolic Research, Vol.26, No.1, 14-18, 1994.
64.	Kazuo Hosoi, Kinji Kurihara and Takao Ueha : Bradykinin-stimulated transient modulation of epidermal growth factor receptors in A-431 human epidermoid carcinoma cells, Journal of Cellular Physiology, Vol.157, No.1, 1-12, 1993.
65.	Shichiro Maruyama, Kazuo Hosoi, Takao Ueha, Masamichi Tajima, Seiichi Sato and Edward W Gresik : Effects of female hormones and 3,5,3'-triiodothyronine or dexamethasone on induction of epidermal growth factor and proteinases F, D, A, and P in the submandibular glands of hypophysectomized male mice, Endocrinology, Vol.133, No.3, 1051-1060, 1993.
66.	Shichiro Maruyama, Kazuo Hosoi, Takao Ueha, Edward W Gresik, Masamichi Tajima and Seiichi Sato : Effects of single or combined injection of female, thyroid and adrenocortical hormones on the proteinase isozyme (F, D, A, P) activities and EGF contents in the submandibular gland of hypophysectomized mice (in Japanese), Journal of the Japan Salivary Gland Society, Vol.33, 35-39, 1992.
67.	Kinji Kurihara, Kazuo Hosoi and Takao Ueha : Characterization of ecto-nucleoside triphosphatase on A-431 human epidermoidal carcinoma cells, Enzyme, Vol.46, No.4,5, 213-220, 1992.
68.	Kazuo Hosoi, Mariko Fujishita, Kenji Sugita, Kinji Kurihara and Takao Ueha : P2-Purinergic receptors and cellular calcium metabolism in A 431 human epidermoid carcinoma cells, American Journal of Physiology, Cell Physiology, Vol.262, No.31, 635-643, 1992.
69.	Kazuo Hosoi, Shichiro Maruyama, Takao Ueha, Seiichi Sato and Edward W Gresik : Additive and/or synergistic effects of 5a-dihydrotestosterone, dexamethasone, and triiodo-L-thyronine on induction of proteinases and epidermal growth factor in the submandibular gland of hypophysectomized mice, Endocrinology, Vol.130, No.2, 1044-1055, 1992.
70.	Shichiro Maruyama, Kazuo Hosoi, Takao Ueha and Seiichi Sato : Effects of various hormones on a-amylase and proteinase activity in salivary glands of hypophysectomized mice (in Japanese), Journal of the Japan Salivary Gland Society, Vol.32, 55-57, 1991.
71.	Kazuo Hosoi, Kenji Sugita, Yoshimi Shioda, Akiko Kodama and Takao Ueha : Involvement of cellular calcium incorporated from the medium in production of inositol trisphosphate in A431 cells, Cellular Signalling, Vol.3, No.1, 79-84, 1991.
72.	Kenji Sugita, Kazuo Hosoi, Yoshimi Shioda and Takao Ueha : Effects of Ca²⁺ and Mg²⁺ on ATP-dependent 45Ca²⁺ influx in A-431 human epidermoidal carcinoma cells, Biochemistry and Cell Biology, Vol.69, No.1, 29-35, 1991.
73.	Kazuo Hosoi, Takao Ueha, Hidekazu Fukuuchi, Minoru Kohno and Tsutomu Takahashi : Reversal of relative proteinase F activity and onset of androgen-dependent proteinases in the submandibular gland of postnatal mice, Biochemistry International, Vol.22, No.1, 179-187, 1990.
74.	Kinji Kurihara, Kazuo Hosoi, Akiko Kodama and Takao Ueha : A new electrophoretic variant of a subunit of Na⁺,K⁺-ATPase from the submandibular gland of rats, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol.1039, No.2, 234-240, 1990. (Summary) The alpha catalytic subunits of Na+/K(+)-ATPase were isolated from the kidney and brain of rats (alpha 1 and alpha 2, respectively). The antisera raised against these subunits were used as probes to analyze the isoform of catalytic subunits of Na+/K(+)-ATPase in various tissues of rats. Of 27 rat tissues examined, most had a catalytic subunit identical to alpha 1 but some, such as the nervous and muscle tissues, had both alpha 1 and alpha 2 isoforms as judged by their reactivities to antisera and their electrophoretic mobility. We found that the submandibular gland contained a new electrophoretic variant of immunoreactive alpha subunit (designated alpha(S) in this report) in addition to alpha 1 identical to those found in kidney and brain. The new variant, alpha(S), strongly cross-reacted with anti-alpha 1 antiserum, but to a lesser extent with anti-alpha 2 antiserum. The alpha(S) had a molecular mass which was found to be slightly less (approx. 90 kDa) than brain and kidney alpha 1. We examined whether or not the alpha(S) is formed by proteolytic cleavage of alpha subunits during preparation and concluded that this is not the case. The alpha(S) reacted with [gamma-32P]ATP, resulting in the formation of radioactive alpha subunit which was stabilized by 2 mM ouabain but which was labile in the presence of 70 mM potassium chloride. Since N-terminal amino acid sequence of alpha(S) protein [G()DKY()PAAVS] corresponds exactly and uniquely with the sequence of the alpha 1 chain between residues 1 and 11, it is very probable that alpha(S) protein originated from alpha 1 protein following the post-translational processing. (Keyword) Amino Acid Sequence / Animals / Blotting, Western / Brain / Genetic Variation / Immune Sera / Isoenzymes / Kidney / Macromolecular Substances / Male / Microsomes / Molecular Sequence Data / Organ Specificity / Rats / Rats, Inbred Strains / Sequence Homology, Nucleic Acid / Sodium-Potassium-Exchanging ATPase / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1016/0167-4838(90)90191-H (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 2163680 ● Search Scopus @ Elsevier (PMID): 2163680 ● Search Scopus @ Elsevier (DOI): 10.1016/0167-4838(90)90191-H (DOI: 10.1016/0167-4838(90)90191-H, PubMed: 2163680)
75.	Kazuo Hosoi, Toshiko Atsumi and Takao Ueha : A human-mouse hybrid cell line expressing both HLA and H-2 antigens, The Japanese Journal of Physiology, Vol.40, No.2, 297-304, 1990.
76.	Kazuo Hosoi and Mariko Fujishita : Measurement of intracellular calcium in single cells by a fluorescence analysis using laser beam (in Japanese), Journal of Clinical and Experimental Medicine, Vol.150, No.9, 590, 1989.
77.	Kazuo Hosoi and Michael Edidin : Exogenous ATP and other nucleoside phosphates modulate epidermal growth factor receptors of A-431 epidermoid carcinoma cells, The Proceedings of The National Academy of Sciences USA, Vol.86, No.12, 4510-4514, 1989.
78.	Kazuo Hosoi, Kinji Kurihara, Akiko Kodama, Yoshimi Shioda, Kenji Sugita and Takao Ueha : Postnatal changes in an a-subunit isoform, a(S), of Na+,K+-ATPase in the submandibular gland of rats, Enzyme, Vol.42, No.3, 152-159, 1989.
79.	Kazuo Hosoi, Yoshimi Shioda, Akiko Kodama, Kenji Sugita, Kinji Kurihara, Toyoaki Murai, Akira Nemoto, Toshiko Atsumi and Takao Ueha : A simple and rapid purification procedure for the tetramethylrhodamine-labeled antibodies, The Japanese Journal of Physiology, Vol.39, No.2, 317-324, 1989. (Summary) A conjugate preparation of antibody (Fab) and tetramethylrhodamine (TMR) generally adsorbs free TMR which is very difficult to remove because of its strong hydrophobic binding. On the basis of criteria such as sodium dodecyl sulfate (SDS) gel electrophoresis and staining of the plasma membrane of live cells, we found that simple extraction with n-butyl alcohol or iso-amyl alcohol could remove the contaminating free dye. The procedure is especially useful when one needs to prepare conjugates with low nonspecific binding for the study of lateral diffusion of cell membrane-associated antigens. (Keyword) 1-Butanol / Butanols / Carcinoma, Squamous Cell / Cell Line / Electrophoresis, Polyacrylamide Gel / Immunoglobulin Fab Fragments / Pentanols / Rhodamines / Xanthenes (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 2761125 ● Search Scopus @ Elsevier (PMID): 2761125 (PubMed: 2761125)
80.	Kazuo Hosoi, Dilip S. Kittur and Michael Edidin : Modulation of HLA antigens in response to the binding of epidermal growth factor by A431 cells, FEBS Letters, Vol.231, No.2, 371-377, 1988.
81.	Toyoaki Murai, Kinji Kurihara, Kenji Sugita, Kazuo Hosoi and Takao Ueha : Androgen responsiveness of proteinase F in the submandibular salivary glands of inbred mice, The Japanese Journal of Physiology, Vol.37, No.5, 871-879, 1987. (Summary) Using the radioimmunoassay technique, we studied androgenic regulations of proteinase F in the submandibular salivary glands (SMG) of various mouse strains (ICR, BALB/CA, C3H/HeN, C57BL/10N, and DBA/2N). The proteinase contents in BALB/CA and DBA/2N mice were almost the same between males and females. However, prominent sex differences in enzyme content were seen in all other strains; i.e., male glands of C3H/HeN and C57BL/10N contained more proteinase F than female glands did. On the contrary, the enzyme level in the ICR was exceedingly higher in females than in males. The enzyme contents in ICR SMG increased in males following castration and decreased after androgen injection in both castrated males and normal females. On the contrary, the enzyme level in C3H/HeN was decreased by castration and increased by androgen injection. Therefore, these sex differences in ICR and C3H/HeN mice depend on androgen, though the direction of the response is opposite. (Keyword) Animals / Female / Injections, Subcutaneous / Isoelectric Focusing / Male / Mice / Mice, Inbred Strains / Orchiectomy / Radioimmunoassay / Serine Endopeptidases / Submandibular Gland / Testosterone (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 3482464 ● Search Scopus @ Elsevier (PMID): 3482464 (PubMed: 3482464)
82.	Shigeyasu Tanaka, Kazuo Hosoi, Izumi Tanaka, Masayoshi Kumegawa and Takao Ueha : Immunocytochemical study of proteinase F in the mouse submandibular gland, The Journal of Histochemistry and Cytochemistry, Vol.32, No.6, 585-592, 1984.
83.	Kazuo Hosoi, Izumi Tanaka, Toyoaki Murai and Takao Ueha : Inhibitory effect of androgen on the synthesis of proteinase F in the male mouse submandibular gland, The Journal of Endocrinology, Vol.100, No.2, 253-262, 1984.
84.	Kazuo Hosoi, Izumi Tanaka, Yukihito Ishii and Takao Ueha : A new esteroproteinase (proteinase F) from the submandibular gland of female mice, Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.756, No.2, 163-170, 1983. (Summary) One of the esteroproteinases present in the submandibular glands of female mice was purified and characterized. The enzyme, designated proteinase F in this report, had a pI value of 4.6 and a molecular weight of 27600, being comprised of two subunits of 10000 and 18000 daltons. The amino acid composition of proteinase F resembled that of the epidermal growth factor-binding protein, but antiserum against proteinase F only reacted weakly against the binding protein. Proteinase F had an optimum pH at around 9.0 and was strongly inhibited by Cu2+ and Hg2+ (42 and 76% inhibition, respectively, at a concentration of 4 x 10(-6) M). It was also inhibited by aprotinin, phenylmethylsulfonylfluoride, iodoacetamide, leupeptin, antipain, and benzamidine but neither by trypsin inhibitors from pancrease, soybean, or ovomucoid, nor by TLCK, TPCK, and epsilon-amino-n-caproic acid. Although its actual physiological function has yet to be determined, these properties indicate that proteinase F is a new enzyme, being distinguished from known proteinases, kallikrein, plasmin, trypsin, chymotrypsin, tonin, angiotensin-converting enzyme, proteinase A (beta-nerve growth factor endopeptidase), proteinase D (epidermal growth factor-binding protein), P-esterase, renin A, and renin C. Proteinase F was present in the submandibular glands of female mice more abundantly than in those of males, but it increased in males following castration. Thus, proteinase F appears to be affected by male hormones in vivo. (Keyword) Amino Acids / Animals / Castration / Chemical Phenomena / Chemistry / Endopeptidases / Female / Male / Mice / Mice, Inbred ICR / Protease Inhibitors / Serine Endopeptidases / Sex Factors / Submandibular Gland (Link to Publication Site) ● Publication site (DOI): 10.1016/0304-4165(83)90088-0 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 6338933 ● Search Scopus @ Elsevier (PMID): 6338933 ● Search Scopus @ Elsevier (DOI): 10.1016/0304-4165(83)90088-0 (DOI: 10.1016/0304-4165(83)90088-0, PubMed: 6338933)
85.	Kazuo Hosoi, Shizuko Kamiyama, Toshiko Atsumi, Akira Nemoto, Izumi Tanaka and Takao Ueha : Characterization of two esteroproteases from the male mouse submandibular gland, Archives of Oral Biology, Vol.28, No.1, 5-11, 1983.
86.	Kazuo Hosoi, Izumi Tanaka and Takao Ueha : Induction of epidermal growth factor by tri-iodo-L-thyronine in the submandibular glands of mice with testicular feminization, The Journal of Biochemistry, Vol.90, No.1, 267-270, 1981.
87.	Kazuo Hosoi, Tadayoshi Kida and Takao Ueha : Induction of various androgen-dependent esteroproteases (trypsin-like and chymotrypsin-like enzymes) by tri-iodo-L-thyronine in the submandibular glands of female mice and mice with testicular feminization, The Journal of Biochemistry, Vol.89, No.6, 1793-1798, 1981.
88.	Shizuko Kobayashi, Kazuo Hosoi and Takao Ueha : Purification and properties of b-N-acetylhexosaminidase from mouse submandibular gland, Archives of Oral Biology, Vol.25, No.11,12, 753-758, 1980.
89.	Masahiko Hiramatsu, Keiko Hatakeyama, Kazuo Hosoi and Naomi Minami : Effect of autonomic agents on the secretion of N-acetyl b-glucuronidase of mouse submaxillary gland, Journal of Dental Research, Vol.59, No.8, 1439-1441, 1980.
90.	Kazuo Hosoi, Shizuko Kobayashi, Takao Ueha, Shichiro Maruyama, Seiichi Sato, Taishin Takuma and Masayoshi Kumegawa : Induction of androgen-dependent protease and serous-like granules by tri-iodothyronine in the submandibular gland of mice with testicular feminization, The Journal of Endocrinology, Vol.83, No.3, 429-434, 1979.
91.	Masahiko Hiramatsu, Keiko Hatakeyama, Kazuo Hosoi and Naomi Minami : Regulation of delayed-hypersensitivity response by the submandibular gland of male mice, Immunology, Vol.37, No.4, 869-872, 1979.
92.	Kazuo Hosoi, Shizuko Kobayashi, Masahiko Hiramatsu, Naomi Minami and Takao Ueha : Androgenic regulation of N-acetyl b-glucuronidase activity in the submandibular glands of mice, The Journal of Biochemistry, Vol.85, No.6, 1483-1488, 1979.
93.	Kazuo Hosoi, Shizuko Kobayashi and Takao Ueha : Affinity adsorption of L-glutamine D-fructose-6-phosphate aminotransferase to Sepharose coupled with p-chloromercuribenzoate, Biochemical and Biophysical Research Communications, Vol.85, No.2, 558-563, 1978.
94.	Kazuo Hosoi, Shizuko Kobayashi and Takao Ueha : Sex difference in L-glutamine D-fructose-6-phosphate aminotransferase activity of mouse submandibular gland, Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.543, No.3, 283-292, 1978. (Summary) L-Glutamine D-fructose-6-phosphate aminotransferase (2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase (amino-transferring), EC 5.3.1.19) activities in the three main salivary glands of male and female mice were measured. It was found that the activity in the submandibular gland was about 10 times more in females than in males, whereas the activities in the sublingual and parotid glands of males and females were similar. The activity in the submandibular gland of female mice was not affected appreciably by ovariectomy but it decreased to the level in males on injection of testosterone. The activity in males was not affected appreciably by injection of progesterone or 17beta-estradiol, but it increased to the level in females after castration. The increased activity in castrated male mice was decreased again to the normal level by testosterone injection. Thus, this sex difference is caused by androgen, not by female hormones. On the basis of in vivo experiments using actinomycin D, it was suggested that testosterone produced an "enzyme inhibitor", which suppressed the enzyme activity in the submandibular glands of androgen-rich animals. (Keyword) Animals / Carbohydrate Epimerases / Castration / Dactinomycin / Female / Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / Gonadal Steroid Hormones / Male / Mice / Sex / Subcellular Fractions / Submandibular Gland / Testosterone (Link to Publication Site) ● Publication site (DOI): 10.1016/0304-4165(78)90046-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 708787 ● Search Scopus @ Elsevier (PMID): 708787 ● Search Scopus @ Elsevier (DOI): 10.1016/0304-4165(78)90046-6 (DOI: 10.1016/0304-4165(78)90046-6, PubMed: 708787)
95.	Kazuo Hosoi, Shizuko Kobayashi and Takao Ueha : Influence of androgen on b-glucuronidase activity in liver, kidney and submandibular salivary gland of the mouse, Archives of Oral Biology, Vol.23, No.10, 905-909, 1978.
96.	Kazuo Hosoi, Kazushi Aoyama and Takao Ueha : Effect of autonomic agents on the amount of androgen-dependent granules in convoluted tubular cells of the mouse submandibular gland, Canadian Journal of Physiology and Pharmacology, Vol.56, No.4, 634-641, 1978.
97.	Kazuo Hosoi, Kazushi Aoyama and Takao Ueha : Regulation of the secretory process of granular components from the convoluted tubular cells of the mouse submandibular gland, Journal of Dental Research, Vol.57, No.1, 87-90, 1978.
98.	Kazuo Hosoi and Takao Ueha : Androgenic control of the submandibular gland of mice, Symposium for the salivary gland, No.18, 33-35, 1977.
99.	Kazuo Hosoi and Takao Ueha : Effects of sex hormones on synthesis of proteins contained in granules present in convoluted tubular cells of mouse submandibular glands, The Journal of Biochemistry, Vol.82, No.2, 351-358, 1977.
100.	Kazuo Hosoi and Toshikazu Nakamura : Effect of testosterone on the amount of serous-like granules in convoluted tubular cells of mouse submandibular glands, The Journal of Biochemistry, Vol.81, No.3, 739-748, 1977.
101.	Taishin Takuma, Toshikazu Nakamura, Kazuo Hosoi and Masayoshi Kumegawa : Binding protein for 5α-dihydrotestosterone in mouse submandibular gland, Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.496, No.1, 175-181, 1977. (Summary) The changes in the levels of the binding protein for 5 alpha-dihydrotestosterone in cytoplasmic extract of the submandibular glands during development were compared in male and female mice using a DEAE-cellulose filter assay. The binding protein was first detectable 5 days after birth in both sexes, at a time coincident with androgen-independent cytodifferentiation of the convoluted tubular cells in the submadibular gland. The level of the binding protein in female mice was maintained at 5 pmol/mg protein after birth, whereas in males it began to decrease from 3 weeks after birth with inccrease in serum testosterone, becoming much less than a quarter of the level in females or immature mice by 4 weeks after birth. However, after castration, the level of detectable binding protein in mature male mice increased within 7 days to the same level as that in females or immature mice. This suggests that the low binding capacity for exogenous hormone in mature male mice is due to occupancy of the binding sites by endogenous hormone. (Keyword) Age Factors / Animals / Castration / Cytoplasm / Dihydrotestosterone / Female / Hydrogen-Ion Concentration / Male / Mice / Mice, Inbred ICR / Sex Hormone-Binding Globulin / Structure-Activity Relationship / Submandibular Gland / Testosterone (Link to Publication Site) ● Publication site (DOI): 10.1016/0304-4165(77)90125-8 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 13860 ● Search Scopus @ Elsevier (PMID): 13860 ● Search Scopus @ Elsevier (DOI): 10.1016/0304-4165(77)90125-8 (DOI: 10.1016/0304-4165(77)90125-8, PubMed: 13860)
102.	Kazuo Hosoi, Kazushi Aoyama and Takao Ueha : Regulation of secretion of the components in androgen-dependent granules in convoluted tubular cells of mouse submandibular glands (in Japanese), Journal of Physiological Society of Japan, Vol.38, No.10, 416-420, 1976.
103.	Kazuo Hosoi, Masumi Murayama and Ueha Tkao : Quantitative measurement of androgen dependent granules in the mouse submandibular gland and effects of various sex hormones (in Japanese), Journal of Clinical and Experimental Medicine, Vol.97, No.11, 764-765, 1976.
104.	Kazuo Hosoi, Gilbu Soe, Tomisaburo Kakuno and Takekazu Horio : Effects of pH indicators on various activities by chromatophores of Rhodospirillum rubrum, The Journal of Biochemistry, Vol.78, No.6, 1331-1346, 1975.
105.	Tatsuo Oku, Kazuo Hosoi, Gilbu Soe, Tomisaburo Kakuno and Takekazu Horio : Energization of NTP-NDP kinase by acid base transition leading to ATP formation, The Journal of Biochemistry, Vol.76, No.1, 233-235, 1974.
106.	Tomisaburo Kakuno, Kazuo Hosoi, Tomihiko Higuti and Takekazu Horio : Electron and proton transports in Rhodospirillum rubrum chromatophores, The Journal of Biochemistry, Vol.74, No.6, 1193-1203, 1973.
107.	Kazuo Hosoi, Setsuko Yoshimura, Gilbu Soe, Tomisaburo Kakuno and Takekazu Horio : Competition between Pi and pH indicators in photosynthetic ATP formation with chromatophores of Rhodospirillum rubrum, The Journal of Biochemistry, Vol.74, No.6, 1275-1278, 1973.
108.	Katsuzo Nishikawa, Kazuo Hosoi, Junnosuke Suzuki, Setsuko Yoshimura and Takekazu Horio : Formation and decomposition of pyrophosphate related to bacterial photophosphorylation, The Journal of Biochemistry, Vol.73, No.3, 537-553, 1973.
109.	Toshikazu Nakamura, Kazuo Hosoi, Katsuzo Nishikawa and Takekazu Horio : Effects of injection of chromatins from Rhodamine sarcoma into rats on pI-isozymes of liver pyruvate kinase, Gann : Japanese Journal of Cancer Research, Vol.63, No.2, 239-250, 1972.

Academic Paper (Unrefereed Paper):

1.	Kazuo Hosoi : For learners aiming to study science in Japan, Ja-Net, No.94, 7, 2020.
2.	Masanori Nakano, Kazuo Hosoi and Hiroki Iga : Report: Chosun University School of Dentistry (in Japanese), Shikoku Dental Research, Vol.21, No.1, 287-288, 2008. (Tokushima University Institutional Repository) ● Metadata: 109773 (Tokushima University Institutional Repository: 109773)
3.	Toshio Sakata, Shichiro Maruyama, Akihiko Tamura, Masamichi Tajima, Kazuo Hosoi, Takao Ueha, Seiichi Sato and Naomi Minami : Effects of hypophysectomy and hormonal replacement on the amylase activity in parotid gland of mice (2)(in Japanese), Journal of Meikai University School of Dentistry, Vol.23, No.1, 104-110, 1994.
4.	Toshiko Atsumi, Kazuo Hosoi and Takao Ueha : Relation between cell rounding induced by epidermal growth factor (EGF) and high affinity binding sites for EGF in A-431 human epidermoid carcinoma cells (in Japanese), Journal of Meikai University, School of Dentistry, Vol.22, No.1, 72-84, 1993.
5.	Toshiko Atsumi, Kazuo Hosoi and Takao Ueha : Stability of HLA and H-2 expression on the surface of human-mouse hybrid cells prepared by cell hybridization technique, Journal of Meikai University, School of Dentistry, Vol.20, No.2, 158-169, 1991.
6.	Akiko Kodama, Kazuo Hosoi, KInji Kurihara, Toshiko Atsumi, Kenji Sugita, Yoshimi Shioda, Hidekazu Fukuuchi and Takao Ueha : Effects of L-ascorbic acid and bone metabolism factors on alkaline phosphatase activity of and 45Ca²⁺ incorporation by ROS 17/2.8 cells (in Japanese), The Journal of Meikai University School of Dentistry, Vol.19, No.1, 109-116, 1990.
7.	Akiko Kodama, Yoshimi Shioda, Kenji Sugita, Kinji Kurihara, Kazuo Hosoi and Takao Ueha : Effects of various factors involved in bone metabolism on 45Ca²⁺ incorporation and alkaline phosphatase activity of ROS 17/2.8 cells (in Japanese), The Journal of Meikai University School of Dentistry, Vol.18, No.1, 82-87, 1989.
8.	Kazuo Hosoi, Izumi Tanaka, Yukihito Ishii and Takao Ueha : Two esteroproteases from mouse submandibular gland (in Japanese), Bulletin of Josai Dental University, Vol.11, No.2, 221-225, 1982.
9.	Izumi Tanaka, Kazuo Hosoi, Minoru Kohno and Takao Ueha : Developmental changes of various esteroprotease isozymes in the mouse submandibular gland (in Japanese), Bulletin of Josai Dental University, Vol.10, No.1, 9-14, 1981.
10.	Tadayoshi Kida, Takao Ueha, Akira Nemoto and Kazuo Hosoi : Histochemical localization of Na+,K+-ATPase in rat submandibular gland -The effects of mineralocorticoid and sodium ion- (in Japanese), Bulletin of Josai Dental University, Vol.9, No.2, 155-158, 1980.
11.	Kazuo Hosoi, Akira Nemoto, Izumi Tanaka, MInoru Kohno and Takao Ueha : Induction of androgen-dependent esteroproteases (trypsin-like and chymotrypsin-like) by tri-iodothyronine in the submandibular glands of female mice and mice with testicular feminization (in Japanese), Bulletin of Josai Dental University, Vol.9, No.2, 147-153, 1980.
12.	Shizuko Kobayashi, Kazuo Hosoi, MInoru Kohno and Takao Ueha : Purification and properties of N-acetyl b-D-glucuronidase from mouse submandibular gland (in Japanese), Bulletin of Josai Dental University, Vol.8, No.2, 157-165, 1979.
13.	Tadayoshi Kida, Takao Ueha and Kazuo Hosoi : The effect of mineralocorticoids and sodium ion on Na+,K+-ATPase activity in rat submandibular gland (in Japanese), Bulletin of Josai Dental University, Vol.8, No.2, 149-156, 1979.
14.	Shizuko Kobayashi, Kazuo Hosoi and Takao Ueha : Separation and purification of glutamine fructose-6-phosphate aminotransferase by affinity chromatography (in Japanese), Bulletin of Josai Dental University, Vol.7, No.1, 27-32, 1978.
15.	Kazuo Hosoi, Shizuko Kobayashi and Takao Ueha : Sex difference in the activity of L-glutamine D-fructose-6-phosphate aminotransferase in the submandibular glands of mice (in Japanese), Bulletin of Josai Dental University, Vol.6, No.1, 37-41, 1977.
16.	Kazuo Hosoi, Kazushi Aoyama, Masumi Murayama, Shizuko Kobayashi and Takao Ueha : Studies on secretory granules in the convoluted tubules of mouse submandibular gland (3) A role of a-adrenergic receptor in the secretory process of granular components (in Japanese), Bulletin of Josai Dental University, Vol.5, No.1, 35-38, 1976.
17.	Taishin Takuma, Nakamura Toshikazu, Kazuo Hosoi and Masayoshi Kumegawa : Binding protein for 5a-dihydrotestosterone in mouse submandibular gland (in Japanese), Bulletin of Josai Dental University, Vol.5, No.1, 1-6, 1976.
18.	Kazuo Hosoi, Toshikazu Nakamura and Takao Ueha : Studies on secretory granules in the convoluted tubules of mouse submandibular gland (2) Changes in granular components determined by immunochemical methods (in Japanese), Bulletin of Josai Dental University, Vol.4, No.1, 37-40, 1975.
19.	Kazuo Hosoi, Masumi Toma and Takao Ueha : Studies on secretory granules in the convoluted tubules of mouse submandibular gland (1) Preparation of granule specific anti-serum (in Japanese)", Bulletin of Josai Dental University, Vol.4, No.1, 31-35, 1975.

Review, Commentary:

1.	Kazuo Hosoi, Mileva Karabasil and Kwartarini Murdiastuti : Naturally occurring AQP5 mutations in rats and humans and their affected phenotypes, Veterinarski Glasnik, Vol.75, No.1, 1-19, 2021. (Link to Publication Site) ● Publication site (DOI): 10.2298/VETGL200928013H (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.2298/VETGL200928013H (DOI: 10.2298/VETGL200928013H)
2.	Kazuo Hosoi, Chenjuan Yao, Takahiro Hasegawa, Hiroshi Yoshimura and Tetsuya Akamatsu : Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions, International Journal of Molecular Sciences, Vol.21, No.4, 1182, Feb. 2020. (Tokushima University Institutional Repository) ● Metadata: 114575 (Link to Publication Site) ● Publication site (DOI): 10.3390/ijms21041182 (Link to Search Site for Scientific Articles) ● Summary page in Scopus @ Elsevier: 2-s2.0-85079334066 (Tokushima University Institutional Repository: 114575, DOI: 10.3390/ijms21041182, Elsevier: Scopus)
3.	Shingo Kurabuchi, Chenjuan Yao, Gang Chen and Kazuo Hosoi : Reversible Conversion among Subtypes of Salivary Gland Duct Cells as Identified by Production of a Variety of Bioactive Polypeptides, Acta Histochemica et Cytochemica, Vol.52, No.4, 59-65, Aug. 2019. (Summary) Four major kallikreins (mK1, mK22, mK9, and mK13) were identified in the mouse submandibular gland (SMG). mK1, a true tissue kallikrein, was used as a protein marker to identify different types of SMG granular convoluted tubule (GCT) cells along with epidermal growth factor (EGF), nerve growth factor (NGF), and renin. Kallikrein mK1 was localized in a very small number (~5%) of GCT cells, which were scattered throughout the GCT, indicating that the majority of GCT cells are mK1-negative. Among mK1-positive cells, particularly strong signals were observed in a small number of narrow cells, recognized as slender granular cells (SG cells, Type IV), in the GCT. After postnatal development of the SMG, GCT cells are no longer uniform based on the bioactive substances (mK1, EGF, NGF, and renin) that they produce and secrete. GCT cells were classified into four subtypes, Types I-IV, and it became clear that these subtypes are complicatedly and reversibly converted by the endocrine hormones 5α-dihydrotestosterone (DHT) and triiodothyronine (T). Duct segments with similar morphology or hormone dependency were recognized in the sublingual and parotid glands. The presence of duct cells with such characteristics is therefore a common feature of the three major salivary glands of rodents. (Keyword) 5α-dihydrotestosterone / epidermal growth factor / granular convoluted tubular cells / mK1 / submandibular gland (Tokushima University Institutional Repository) ● Metadata: 114977 (Link to Publication Site) ● Publication site (DOI): 10.1267/ahc.19014 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31602049 ● Search Scopus @ Elsevier (PMID): 31602049 ● Search Scopus @ Elsevier (DOI): 10.1267/ahc.19014 (Tokushima University Institutional Repository: 114977, DOI: 10.1267/ahc.19014, PubMed: 31602049)
4.	Kazuo Hosoi, Javkhlan Purevjav and Chenjuan Yao : Possible Existence of a Salivary Gland-Oral Mucosa/Gingiva Axis Under Challenges by Endotoxins, Journal of Molecular and Cellular Biology Forecast, Vol.1, No.1, 1002, Jan. 2018.
5.	Kazuo Hosoi : Physiological role of aquaporin 5 in salivary glands, Pflügers Archiv : European Journal of Physiology, Vol.468, No.4, 519-539, Nov. 2015. (Summary) Regarding the 13 known mammalian aquaporins (AQPs), their functions in their expressing tissues, effects of their mutation/polymorphisms in humans, and effects of knockout of their genes are summarized in this review article. The roles of AQP5, an exocrine gland-type water channel, in the salivary gland under normal and pathophysiological conditions are reviewed in detail. First, the involvement of AQP5 in water secretion from acinar cells was demonstrated by measuring volume changes of acini/acinar cells, as well as activation energy (E a) in transepithelial water movement by NMR spectrometry, and a functional linkage between AQP5 and TRPV4 was suggested. Next, involvement of the parasympathetic nervous system on the AQP5 levels in the acinar cells of the submandibular and that of a β-adrenergic agonist on those in the parotid gland are described. That is, chorda tympani denervation induces autophagy of the submandibular gland, causing AQP5 degradation/metabolism, whereas isoproterenol, a β-adrenergic agonist, causes first an increase then decrease in AQP5 levels in the parotid gland, which action is coupled with the secretory-restoration cycle of amylase-containing secretory granules. The PG also responded to endotoxin, a lipopolysaccharide that activates NF-κB and MAPK pathways. Elevated NF-κB and AP-1 (c-Fos/c-Jun) form a complex that can bind to the NF-κB-responsive element on the AQP5 promoter and thus potentially downregulate AQP5 transcription. Salivary gland pathologies and conditions involving AQP5 and possible treatments are described as well. (Link to Publication Site) ● Publication site (DOI): 10.1007/s00424-015-1749-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26537593 ● Summary page in Scopus @ Elsevier: 2-s2.0-84961155864 (DOI: 10.1007/s00424-015-1749-6, PubMed: 26537593, Elsevier: Scopus)
6.	Kazuo Hosoi : Expression of AQP5 in the salivary gland and its autonomic regulation (in Japanese),, Journal of the Japan Salivary Gland Society, Vol.53, 53-66, Nov. 2012.
7.	Kazuo Hosoi : Effects of naturally occurring mutation in rat aquaporin 5 (in Japanese), Shikoku Dental Research, Vol.24, No.2, 1-8, Jan. 2012. (Tokushima University Institutional Repository) ● Metadata: 109816 (Tokushima University Institutional Repository: 109816)
8.	Kazuo Hosoi and Chenjuan Yao : Suppression of aquaporin 5 gene expression by endotoxin via cross-coupling of transcription factors (In Japanese), Seikagaku, Vol.83, No.7, 632-638, Jul. 2011. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520009407217492352 ● Summary page in Scopus @ Elsevier: 2-s2.0-80053453855 (CiNii: 1520009407217492352, Elsevier: Scopus)
9.	Kazuo Hosoi : International Exchange and Internationalization in the Graduate School of Oral Scieces and School of Dentistry, the University of Tokushima (in Japanese), The Nippon Dental Review, Vol.71, No.4, 165-167, Apr. 2011.
10.	Shingo Kurabuchi and Kazuo Hosoi : Sexual dimorphism and hormonal regulation of granular convoluted tubule (GCT) cells of mouse submandibular gland -Immunohistochemical analysis- (In Japanese), Journal of Japanese Society for Mastication Science and Health Promotion, Vol.10, No.2, 61-70, May 2001.
11.	Most Parvin Nahid, Jun Tada, Tetsuya Akamatsu and Kazuo Hosoi : Structure, function, and transcriptional regulation of aquaporins, proteins of the water channel family, Dentistry in Japan, Vol.37, 26-31, Mar. 2001.
12.	Edward W Gresik, Kazuo Hosoi, Kinji Kurihara, Shichiro Maruyama and Takao Ueha : The rodent granular convoluted tubule cell - An update, European Journal of Morphology, Vol.34, 221-224, Aug. 1996.
13.	Kazuo Hosoi and Shichiro Maruyama : Processing of the growth factor precursors by kallikreins (in Japanese), Journal of the Japan Salivary Gland Society, Vol.36, 1-13, Nov. 1995.
14.	Kazuo Hosoi : Expression of EGF and related proteinases in the salivary gland (in Japanese), Shikoku Dental Research, Vol.7, No.2, 147-158, Jan. 1995.
15.	Kazuo Hosoi : Effects of mastication on salivary bioactive substances (in Japanese), Journal of Japanese Society for Mastication Science and Health Promotion, Vol.3, No.1, 11-16, Dec. 1993.
16.	Kazuo Hosoi and Takao Ueha : The Biologically active substances and the cells which produce them in the salivary gland -Recent progress regarding the development and biochemistry- (in Japanese), Journal of Clinical and Experimental Medicine, Vol.127, No.2, 77-84, Oct. 1983.
17.	Kazuo Hosoi and Takao Ueha : Biologically active substances in the salivary gland (in Japanese), Japanese Journal of Oral Biology, Vol.24, No.1, 1-13, Mar. 1982.
18.	Kazuo Hosoi, Gilbu Soe and Takekazu Horio : Studies on molecular level reaction mechanism of photosynthetic ATP formation by solubilization of chromatophore membrane (in Japanese), Protein, Nucleic Acid and Enzymes, supplemented volume 2, Vol.2, 39-48, Dec. 1974.
19.	Kazuo Hosoi, Gilbu Soe and Takekazu Horio : Preparation of chromatophores from photosynthetic bacteria (in Japanese), Protein, Nucleic Acid and Enzyme, supplemented, Vol.1, 321-326, May 1974.

Proceeding of International Conference:

1.	Mileva Ratko Karabasil, Kwartarini Murdiastuti, Nunuk Purwanti, Azlina Ahmad, Javkhlan Purevjav, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Effects of natural point mutation of rat aquaporin 5 expressed in vitro on its capacity of water permeability and membrane trafficking, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 398-400, Tokushima, Dec. 2009. (Summary) In the colony of Sprague-Dawley (SD) strain, we found that there were rats expressing a mutant AQP5, which has a point mutation at nt 308 (G308A), leading to a replacement of (103)Gly with (103)Asp in the 3rd transmembrane domain. The mutant molecule scarcely expressed in the acinar cells, probably because of ineffective trafficking. The mutant molecule, however, showed normal water permeability when assessed by the oocyte system. (Keyword) Amino Acid Sequence / Animals / Aquaporin 5 / Biological Transport / Cell Membrane Permeability / Female / Models, Animal / Molecular Sequence Data / Oocytes / Point Mutation / Rats / Rats, Sprague-Dawley / Submandibular Gland / water channel / Xenopus laevis (Tokushima University Institutional Repository) ● Metadata: 111488 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.398 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224238 ● Search Scopus @ Elsevier (PMID): 20224238 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.398 (Tokushima University Institutional Repository: 111488, DOI: 10.2152/jmi.56.398, PubMed: 20224238)
2.	Purevjav Javkhlan, Yuka Hiroshima, Azlina Ahmad, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Jun-ichi Kido, Toshihiko Nagata and Kazuo Hosoi : Induction of calprotectin mRNAs by lipopolysaccharide in the salivary gland of mice, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 287-289, Tokushima, Dec. 2009. (Summary) Calprotectin is a major cytosolic calcium-binding protein of leukocytes which belongs to the S100 protein family. S100A8 and S100A9, major types of calprotectin are heterodimeric complexes being composed of light- and heavy-chain subunits. The calprotectin levels in the plasma, feces, synovial fluid, gingival crevicular fluid, dental calculus and saliva change when the host animal suffers from several inflammatory diseases. Members of Toll-like receptor (TLR) family are pattern-recognition receptors for lipopolysaccharide (LPS) and other pathogens. Here we examined if the biological role of TLR receptor is reflected to the calprotectin expression in the salivary gland. Time course study by using real-time RT-PCR detected higher levels of S100A8 and S100A9 mRNA at 1.5-3 h after injection of LPS in both the submandibular gland (SMG) and parotid gland (PG) of C3H/HeN mice but not in the same tissues of C3H/HeJ, a TLR-4 mutant strain, indicating that this induction is mediated via the TLR-4. These results indicate that, an inflammatory marker, calprotectin, is expressed in the mouse salivary gland and that LPS stimulated its synthesis. Calprotectin (S100A8/A9) showed minimum expression in all cellular segments in the SMG except excretory duct cells, which showed strong signal at the cytoplasm. LPS induced their expressions in the granular convoluted tubular cells and striated duct cells. In the PG, these proteins were expressed very weakly in both duct and acinar cells with a little stronger staining for the former cells. LPS injection induced calprotectin (S100A8/A9) in both duct and acinar cells especially in the former cells. (Keyword) Animals / Calgranulin A / Calgranulin B / Leukocyte L1 Antigen Complex / Lipopolysaccharides / Mice / Mice, Inbred C3H / Mice, Mutant Strains / Parotid Gland / RNA, Messenger / salivary glands / Submandibular Gland / Toll-Like Receptor 4 (Tokushima University Institutional Repository) ● Metadata: 111354 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.287 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224205 ● Search Scopus @ Elsevier (PMID): 20224205 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.287 (Tokushima University Institutional Repository: 111354, DOI: 10.2152/jmi.56.287, PubMed: 20224205)
3.	Azlina Ahmad, Xuefei Li, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Down-regulation of submandibular gland AQP5 following parasympathetic denervation in rats, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 273-276, Tokushima, Dec. 2009. (Summary) Following chorda tympani denervation (CTD, parasympathetomy), the protein levels of aquaporin5 (AQP5) as well as AQP1 and Na(+)K(+)ATPase alpha-subunit in the rat submandibular gland (SMG) were found to be decreased significantly. However, the level of another membrane protein, dipeptidyl peptidase IV was not affected by CTD, suggesting a selective reduction of AQP5, AQP1, and Na(+)K(+)ATPase alpha -subunit proteins by CTD. However, the AQP5 mRNA level was scarcely affected by CTD, which suggested that transcription process of AQP5 was unaffected by this operation. AQP5 protein was shown to be degraded in vitro by the extract of the SMG obtained from normal rat; inhibitor experiments in vitro suggested cathepsin B was a responsible enzyme. Co-localization of AQP5 and LAMP-2, a lysosomal marker, implicated AQP5 is degraded in lysosomes. A significant increase in the protein levels of LC3-II, an autophagy marker, at day 1 after CTD, and co-localization of the LC3 protein and AQP5, suggested that CTD activated autophagy of SMG, leading to AQP5 degradation. (Keyword) Animals / Aquaporin 1 / Aquaporin 5 / autophagy / Chorda Tympani Nerve / Down-Regulation / Lysosomal-Associated Membrane Protein 2 / Male / Microtubule-Associated Proteins / Parasympathectomy / RNA, Messenger / Rats / Rats, Sprague-Dawley / Sodium-Potassium-Exchanging ATPase / Submandibular Gland (Tokushima University Institutional Repository) ● Metadata: 111348 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.273 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224200 ● Search Scopus @ Elsevier (PMID): 20224200 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.273 (Tokushima University Institutional Repository: 111348, DOI: 10.2152/jmi.56.273, PubMed: 20224200)
4.	Nunuk Purwanti, Azlina Ahmad, Mileva Ratko Karabasil, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Involvement of the IL-6/STAT3/Sca-1 system in proliferation of duct cells following duct ligation in the submandibular gland of mice, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 253-254, Tokushima, Dec. 2009. (Summary) Ligation of the main excretory duct (MED) of the mouse submandibular gland (SMG) induced the expression of Sca-1, a stem cell marker. Sca-1 expression increased prominently in almost all of cells in the duct system, except the acinar cells. Sca-1 induction was accompanied with phosphorylated-STAT3 (Y705) elevation, which was localized in the nuclei of all duct cells. Electrophoretic mobility shift assay (EMSA) confirmed the specific binding of STAT3 to the GAS sequence, a biding site of gamma interferon activating site. Present study suggested one of the initial steps of the tissue regeneration after injury includes STAT3 pathway. (Keyword) Animals / Antigens, Ly / Cell Proliferation / inflammation / Interleukin-6 / Ligation / male / Membrane Proteins / Mice / Mice, Inbred C57BL / regeneration / STAT3 Transcription Factor / signal transduction / Submandibular Gland (Tokushima University Institutional Repository) ● Metadata: 111340 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.253 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224192 ● Search Scopus @ Elsevier (PMID): 20224192 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.253 (Tokushima University Institutional Repository: 111340, DOI: 10.2152/jmi.56.253, PubMed: 20224192)
5.	Tetsuya Akamatsu, Azlina Ahmad, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi : Salivary Gland Development: Its mediation by a subtilisin-like proprotein convertase, PACE4, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 241-246, Tokushima, Dec. 2009. (Summary) The submandibular gland (SMG) develops under the epithelial-mesenchymal interaction. Its process is regulated by various growth/differentiation factors, which are synthesized as inactive precursors and activated via the limited proteolysis at their multi basic amino acid site(s) such as Arg-X-Lys/Arg-Arg. Although many of these processing steps are elucidated to be catalyzed by subtilisin-like proprotein convertases (SPCs), little is known about the role of SPCs in the SMG development. Here, we focused upon the physiological role of PACE4 (SPC4), a member of SPC family, in the SMG development. In the organ culture system of rat embryonic SMG (E15), Dec-RVKR-CMK, a potent inhibitor for SPCs, inhibited the salivary branching and the expression of an exocrine gland type water channel, AQP5. However, other peptidyl-CMKs and inhibitors for trypsin-like serine proteases including leupeptin did not affect the salivary branching and AQP5 expression. Dec-RVKR-CMK also suppressed the expression of PACE4, but not furin, another member of the family. The specific antibody for the catalytic domain of PACE4 suppressed the salivary branching and AQP5 expression similarly. These inhibitory effects of Dec-RVKR-CMK were partially rescued by the addition of recombinant BMP2 whose precursor is a candidate for the physiological substrates of PACE4. Further, the transcriptional silencing of PACE4 by its specific siRNAs caused the suppression of both the salivary branching and AQP5 expression in the present organ culture system. These observations strongly support the idea that PACE4 mediates the SMG development. (Keyword) Animals / Aquaporin 5 / Bone Morphogenetic Protein 2 / Morphogenesis / Proprotein Convertases / Rats / Salivary Glands / Signal Transduction (Tokushima University Institutional Repository) ● Metadata: 111337 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.241 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224189 ● Search Scopus @ Elsevier (PMID): 20224189 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.241 (Tokushima University Institutional Repository: 111337, DOI: 10.2152/jmi.56.241, PubMed: 20224189)
6.	Chun Wang, Gang Chen, Junkang Jiang, Lianglin Qiu, Kazuo Hosoi and Chenjuan Yao : Aquaglyceroporins are involved in uptake of arsenite into murine gastrointestinal tissues, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 343-346, Tokushima, Dec. 2009. (Summary) Aquaglyceroporins (AQGPs) are members of aquaporin (AQP) family and belong to a subgroup of this water channel family; they are transmembrane proteins that transport water as well as glycerol and other solutes of small molecules. Recent studies have also identified that AQGPs are important transporters of trivalent metalloid in some mammalian cells. However, the uptake routes of arsenite in mammals are still less defined. In this study, to understand the routes of arsenite intake in mammals, mice were treated with Hg(II), glycerol, and As(III) and uptake of As(III) into the gastrointestinal tissues was measured. The level of inorganic arsenic (iAs) in gastrointestinal tissues after As(III) stimulation was much higher than Hg(II) +As(III) or glycerol+As(III) group. RT-PCR results showed that AQGPs were extensively expressed in gastrointestinal tissues of mice. We also treated Caco-2 cells with Hg(II) and As(III); the level of iAs in a group treated with Hg(II)+As(III) decreased compared with As(III)-treated group. Our results suggested that AQGPs could be important transporters in arsenite uptake into gastrointestinal tissues of mice, but more data are need to prove if AQGPs is the only pathway involved in As transport in mammals or just one of them. (Keyword) Animals / Aquaglyceroporins / Arsenites / Biological Transport / Cell Line / Gastrointestinal Tract / Glycerol / Humans / Male / Mercury / Mice / Mice, Inbred ICR / Signal Transduction (Tokushima University Institutional Repository) ● Metadata: 111458 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.343 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224220 ● Search Scopus @ Elsevier (PMID): 20224220 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.343 (Tokushima University Institutional Repository: 111458, DOI: 10.2152/jmi.56.343, PubMed: 20224220)
7.	Shingo Kurabuchi, Takanori Matsuoka and Kazuo Hosoi : Hormone-induced granular convoluted tubule-like cells in mouse parotid gland, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 290-295, Tokushima, Dec. 2009. (Summary) Most striated duct (SD) cells in the adult mouse parotid gland (PAG) have a few small secretory granules. These granules, however, are usually too small and sparse to be detected using light microscopy. Our serial studies have suggested that these PAG SD cells belong to a group of hormone-responsive granular duct cells, similar to the granular convoluted tubule (GCT) cells found in the submandibular gland. These studies also indicate that and some PAG SD cells may be capable of developing a granular cell phenotype under supraphysiological conditions of androgenic and thyroid hormones, leading to more abundant, and more kinds of GCT-specific secretory polypeptides. Here, the cytology of hormone-modulated SD cells, the immunocytochemistry of their secretory products, and their secretory responses to some autonomic agents are reviewed. Finally, the close similarity of the duct systems of the three major salivary glands in mice is critically emphasized. (Keyword) Animals / Female / Gonadal Steroid Hormones / Male / Mice / Parotid Gland / Peptides / Secretory Vesicles / Sex Characteristics / Submandibular Gland (Tokushima University Institutional Repository) ● Metadata: 111355 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.290 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224206 ● Search Scopus @ Elsevier (PMID): 20224206 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.290 (Tokushima University Institutional Repository: 111355, DOI: 10.2152/jmi.56.290, PubMed: 20224206)
8.	Kazuo Hosoi, Masataka Murakami and Ivana Novak : The report on the 11th international symposium on exocrine secretion, The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 171-178, Tokushima, Dec. 2009. (Keyword) Animals / Exocrine Glands / Humans / International Cooperation / Japan (Tokushima University Institutional Repository) ● Metadata: 111325 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.56.171 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224177 ● Search Scopus @ Elsevier (PMID): 20224177 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.171 (Tokushima University Institutional Repository: 111325, DOI: 10.2152/jmi.56.171, PubMed: 20224177)
9.	Kazumi Takaishi, Shigemasa Tomioka, Fumiaki Kawano and Kazuo Hosoi : Local anesthetics inhibit bradykinin-stimulated increment of [Ca2+]i in cultured bovine aortic endothelial cells, The Annual Meeting of the American Society of Anesthesiologists, Oct. 2009.
10.	Chenjuan Yao, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Potential down-regulation of parotid gland AQP5 by LPS via cross-coupling of NF-κB/AP1, The 11th International Symposium on Exocrine Secretion, Tokushima 09 ''Exocrine Secretion Mechanism and Disease'', Tokushima, Jul. 2009.
11.	Ahmad Azlina, Nunuk Purwanti, Mileva R. Karabasil, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Is AQP5 down-regulated via autophagic pathway following chorda tympani denervation?, The International Symposium on Oral Sciences to Improve the Quality of Life, organized by Toshihiko Nagata, Tokushima, Sep. 2008.
12.	Mileva R. Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Shigemasa Tomioka and Kazuo Hosoi : Analyses of rat AQP5 G103D mutant expressed in MDCK-II cells and Xenopus oocytes, The International Symposium on Oral Sciences to Improve the Quality of Life, organized by Toshihiko Nagata, Tokushima, Sep. 2008.
13.	Nunuk Puwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi : Activation of IL-6/STAT3/Sca-1 system induces proliferation of duct cells in the duct-ligated mouse submandibular gland, The 2nd International Symposium on The Future Direction of Oral Sciences in The 21st Century-Oral Sciences for Our Healthy Life-, organized by Toshihiko Nagata, Tokushima, Dec. 2007.
14.	Mileva R. Karabasil, Kwartarini Murdiastuti, Takahiro Hasegawa, Nunuk Purwanti, Ahmad Azlina, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : A naturally occurring point mutation in rat AQP5 influencing its membrane trafficking in and water secretion from salivary gland, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
15.	Xuefei Li, Ahmad Azlina, Mileva R. Karabasil, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Effects of autonomic denervation and administration of M3 muscarinic receptor agonist on the AQP5 expression in the rat submandibular gland, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
16.	Chenjuan Yao, Mileva R. Karabasil, Nunuk Purwanti, Ahmad Azlina, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : LPS induces down-regulation of AQP5 and AQP1 via Nf-kB and MAPK pathways in the mouse parotid gland, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
17.	Tetsuya Akamatsu, Nunuk Purwanti, Ahmad Azlina, Mileva R. Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Prenatal expression of rat salivary AQP5 is dependent on the submandibular gland development mediated by a subtilisin-like proprotein convertase PACE4, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
18.	Nunuk Puwanti, Daisuke Tsuji, Ahmad Azlina, Mileva Ratko Karabasil, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : Alterations of AQP5, cellular markers of duct, and Sca-1 expression in the duct-ligated mouse submandibular gland, The 5th International Conference of Aquaporin, Nara, Jul. 2007.
19.	Mileva R. Karabasil, Takahiro Hasegawa, Nunuk Purwanti, Kwartarini Murdiastuti, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Point mutation of AQP5 in Sprague-Dawley rats and its implication for salivary gland physiology, The 1st International Symposium and Workshop on The Future Direction of Oral Sciences in The 21st Century, organized by Bando, E., Awaji, Mar. 2007.
20.	Xuefei Li, Mileva R. Karabasil, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Effects of autonomic denervation and administration of muscarinic receptor agonist on the expression of AQPs in the rat submandibular gland, The 1st International Symposium and Workshop on The Future Direction of Oral Sciences in The 21st Century, organized by Bando, E., Awaji, Mar. 2007.
21.	Nunuk Purwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : Changes of cellular markers of duct/acinni and side populations in the duct-ligated mouse submandibular gland, The 1st International Symposium and Workshop on The Future Direction of Oral Sciences in The 21st Century, organized by Bando, E., Awaji, Mar. 2007.
22.	Mileva R. Karabasil, Takahiro Hasegawa, Nunuk Purwanti, Kwartarini Murdiastuti, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Molecular and cellular analyses of mutant AQP5 which occurred naturally in Spraque - Dawley rats, 3rd International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki, Japan, Oct. 2006.
23.	Xuefei Li, Mileva R. Karabasil, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Effects of autonomic denervation and administration of SNI-2011 on the expression of AQPs in the rat salivary gland, The 3rd International Symposium on Salivary Glands in honor of Niels Stensen, Okazaki, Japan, Oct. 2006.
24.	Chenjuan Yao, Mileva R. Karabasil, Nunuk Purwanti, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Tissue kallikrein mK13 is a candidate of the processing enzyme for pro-IL-1β in the mouse submandibular gland, The 3rd International Symposium on Salivary Glands in honor of Niels Stensen, Okazaki, Japan, Oct. 2006.
25.	Tetsuya Akamatsu, Nunuk Purwanti, Mileva R. Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Involvement of a subtilisin-like proprotein convertase, PACE4, in branching morphogenesis and AQP5 expression in the rat embryonic submandibular gland., The 3rd International Symposium on Salivary Glands in honor of Niels Stensen, Okazaki, Japan, Oct. 2006.
26.	Nunuk Purwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : The expression of cellular markers of duct/acini and side population dynamics in the duct-ligated mouse submandibular gland., 3rd International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki, Oct. 2006.
27.	Chenjuan Yao, Mileva R. Karabasil, Nunuk Purwanti, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Proteolytic processing of the precursor of interleukin-1β by tissue kallikrein mK13 in the submandibular gland of mice., International symposium on "Medical and Biological Perspectives in Proteases and Their Inhibitors", Satellite meeting of the 20th IUBMB International Congress of Biochemistry and Molecular Biology & the 11th FAOBMB Congress, Awaji, Japan, Jun. 2006.
28.	Tetsuya Akamatsu, Nunuk Purwanti, Mileva R. Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Inhibition of subtilisin-like proprotein convertase PACE4 reduces the branching morphogenesis and expression of AQP5 in the organ culture system of rat embryonic submandibular gland, International symposium on "Medical and Biological Perspectives in Proteases and Their Inhibitors", Satellite meeting of the 20th IUBMB International Congress of Biochemistry and Molecular Biology & the 11th FAOBMB Congress, Awaji, Japan, Jun. 2006.
29.	Tetsuya Akamatsu, Nunuk Purwanti, Mileva R. Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Inhibition of subtilisin-like proprotein convertase PACE4 reduces the branching morphogenesis and expression of AQP5 in the organ culture system of rat embryonic submandibular gland, 20th IUBMB International Congress of Biochemistry and Molecular Biology & 11th FAOBMB Congress, 第79回日本生化学会大会 & 第29回日本分子生物学会年会, also 第59回日本細胞生物学会大会, Kyoto, Jun. 2006.
30.	Chenjuan Yao, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Induction, processing, and secretion of IL-1βin the submandibular gland of mice, The 35th International Congress of Physiological Sciences (IUPS2005) and Experimental Biology 2005, San Diego, Mar. 2005.
31.	Tetsuya Akamatsu, Chenjuan Yao, Xuefei Li, Norio Kanamori and Kazuo Hosoi : ECM-bound proprotein convertase PACE4 is involved in the branching morphogenesis of rat submandibular gland, The 35th International Congress of Physiological Sciences (IUPS2005) and Experimental Biology 2005, San Diego, Mar. 2005.
32.	Shingo Kurabuchi and Kazuo Hosoi : Localization and hormonal induction of epidermal growth factor (EGF) and nervegrowth factor (NGF) in the mouse parotid gland, Proceedings of 16th International Congress of the IFAA (Morphological Sciences as the Basis of New Life Sciences in the 21st Century) and 109th Annual Meeting of Japanese Association of Anatomists, 412, Monduzzi Editore, Italy, 2004.
33.	Yoko Yano, Ryoji Ozono, Hidekatu Nakashima, Yoshihiko Oishi, Masayuki Kambe, Kazuo Hosoi and Tetsuya Oshima : Immunohistochemical distributions of the tissue kallikrein-kinin system in ischemic and non-ischemic mouse heart, Journal of Cardiovascular Pharmacology, Vol.42, No.Suppl.1, S49-S53, Dec. 2003. (Summary) Kinins have been shown to play a cardioprotective role during myocardial ischemia. However, the localization of each of the components of the kallikrein-kinin system in the heart has not been determined in a cell type-specific manner. Recently, mK1 has been identified as the major tissue kallikrein with the strongest bradykinin-forming activity among the products of the mouse tissue kallikrein gene superfamily. In the study presented here, we investigated the localizations of mK1, kininogen and bradykinin B2 receptors (B2Rs) in ischemic and non-ischemic left ventricles by immunohistochemistry. Kininogen, which contains bradykinin as a surface epitope, was detected by an anti-bradykinin antibody. Changes in the amounts of mK1 and B2R were evaluated by Western blot analysis. Myocardial ischemia was induced by ligation of the left anterior descending coronary artery for 60 min followed by reperfusion for 24 h. mK1 and B2Rs were most abundantly expressed in the vascular endothelium and, to a lesser extent, in fibroblasts. No immunohistochemical signal of these molecules was detected in myocytes. Kininogen was localized in the vascular endothelium and the smooth muscle layer. Myocardial ischemia, although it had no effect on the localization of these molecules, increased the amounts of mK1 and B2R. We have obtained immunohistochemical evidence that all components of the tissue kallikrein-kinin system are present in the mouse heart. The coronary artery is the major site of kallikrein-kinin activity both in ischemic and non-ischemic hearts. (Keyword) Animals / Blotting, Western / Bradykinin / Coronary Vessels / Endothelium, Vascular / Epitopes / Heart Ventricles / Immunoenzyme Techniques / Kallikrein-Kinin System / Kininogen, High-Molecular-Weight / Kininogen, Low-Molecular-Weight / Ligation / Male / Mice / Mice, Inbred C57BL / Myocardial Ischemia / Receptor, Bradykinin B2 / Reperfusion / Time Factors / Tissue Kallikreins (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14871029 ● Search Scopus @ Elsevier (PMID): 14871029 (PubMed: 14871029)
34.	Shingo Kurabuchi, Kazuo Hosoi and Edward W Gresik : Multihormonal regulation of granular convoluted tubular cells expressing mK1, a true tissue kallikrein, in the mouse submandibular gland, Proceedings of the 21st Conference of European Comparative Endocrinologists, 527-530, Monduzzi Editore, Italy, Aug. 2002.
35.	Kazuo Hosoi, 松浦幸子, 倉淵真悟, 津村恵子, 多田淳, 澤孝賢, Norio Kanamori and Tetsuya Akamatsu : Mast cell kininogen and salivary gland kallikrein-kinin system, The 1st meeting for international collaborative research project 1998-2000., 愛知, Jan. 1999.
36.	Kazuo Hosoi, Shingo Kurabuchi, Yamato Kikkawa, Jun Tada, Tetsuya Akamatsu, Naoki Yamanaka, Takuya Matsumoto, Norio Kanamori and Keiko Tsumura : Salivary gland tissue kallikrein family and processing of growth factor precursors and proenzymes., European Journal of Morphology, Vol.36, No.suppl, 82-85, Cagliari, Italy, Aug. 1998. (Summary) マウスの唾液腺(顎下腺)から得られる主要な組織カリクレインを同定しこれら酵素の有する成長因子前駆体プロセッシング活性について調べた．本研究ではこれら酵素の基質として天然の基質蛋白質(キニノゲン，およびプロレニン)に加えて各種合成基質を用いた．その結果，キニノーゲナーゼ活性の弱い組織カリクレインほど強いプロレニン変換活性を示すことがあきらかになった．
37.	Norio Kanamori, Hiroyoshi Sei and Kazuo Hosoi : Phase diagram analysis of sleep-wakefulness cycle: triplet subsystems as the reciprocal control factors., Sleep Res., Vol.24A, 2, Nassau, Bahamas, Sep. 1995.
38.	Takao Ueha, Tadayoshi Kida and Kazuo Hosoi : Relationships between mineralocorticoids and Na+,K+-ATPase in rat submandibular gland, Advances in Physiological Science, Vol.28, 79-84, Budapest, May 1981.

Proceeding of Domestic Conference:

1.	Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺細胞におけるアクアポリン5の翻訳後修飾, 第53回歯科基礎医学会学術大会サテライトシンポジウムSS11, Sep. 2011.
2.	Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺細胞におけるアクアポリン5の翻訳後修飾, Journal of Oral Biosciences, Vol.53, No.Supplement, 104, Sep. 2011.
3.	Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Toshihiko Nagata and Kazuo Hosoi : Calprotectin expression in the mouse salivary gland: Induction by lipopolysaccharide, 第52回歯科基礎医学会(2010年9月20-22日), Sep. 2010.
4.	Yuka Hiroshima, Purevjav Javkhlan, Ahmad Azlina, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Porphyromonas gingivalis由来LPSはヒト好中球からのレジスチンの遊離を促進する, 第52回歯科基礎医学会(2010年9月20-22日), Sep. 2010.
5.	Takahiro Hasegawa, Ahmad Azlina, Purevjav Javkhlan, Yuka Hiroshima, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺細胞におけるアクアポリン5リン酸化のシグナル伝達機構, 第52回歯科基礎医学会(2010年9月20-22日), Sep. 2010.
6.	Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Toshihiko Nagata and Kazuo Hosoi : Calprotectin expression in the mouse salivary gland: Induction by lipopolysaccharide, Journal of Oral Biosciences, Vol.52, No.supplement, 94, Sep. 2010.
7.	Yuka Hiroshima, Javkhlan Purevjav, Ahmad Azlina, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Porphyromonas gingivalis由来LPSはヒト好中球からのレジスチンの遊離を促進する, Journal of Oral Biosciences, Vol.52, No.supplement, 148, Sep. 2010.
8.	Takahiro Hasegawa, Ahmad Azlina, Javkhlan Purevjav, Yuka Hiroshima, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺細胞におけるアクアポリン5リン酸化のシグナル伝達機構, Journal of Oral Biosciences, Vol.52, No.supplement, 164, Sep. 2010.
9.	Chenjuan Yao, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : NF-κB/AP-1の複合体を介した耳下腺AQP5のLPSによるdown-regulation, 第51回歯科基礎医学会, Sep. 2009.
10.	Tetsuya Akamatsu, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi : 唾液腺の発生と細胞分化, 第51回歯科基礎医学会, Sep. 2009.
11.	Takahiro Hasegawa, Ahmad Azlina, Javkhlan Purevjav, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : アクアポリン5のユビキチン化とその細胞内膜輸送系における役割, 第51回歯科基礎医学会, Sep. 2009.
12.	Javkhlan Purevjav, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Toshihiko Nagata and Kazuo Hosoi : Calprotectin induction by lipopolysaccharide in the salivary gland of mice, 第51回歯科基礎医学会, Sep. 2009.
13.	Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : AQP5 degradation via autophagy following parasympathetic denervation in the rat SMG., 第51回歯科基礎医学会, Sep. 2009.
14.	カラバシルミレーバ, Takahiro Hasegawa, アズリナアハマド, プルワンティヌヌク, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : An AQP5 G103D mutant found in SD rats shows normal water permeability but reduced membrane trafficking, 第50回歯科基礎医学会, Sep. 2008.
15.	Chenjuan Yao, アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺AQP5のLPSによるdown-regulationの機構, 第50回歯科基礎医学会, Sep. 2008.
16.	アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Down regulation of submandibular gland AQP5 by chorda tympany denervation, 第50回歯科基礎医学会, Sep. 2008.
17.	プルワンティヌヌク, アズリナアハマド, カラバシルミレーバ, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Involvement of IL-6-STAT3-Sca-1 system in the proliferation of duct cells in the ligated mouse submandibular gland, 第50回歯科基礎医学会, Sep. 2008.
18.	Chenjuan Yao, アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : LPSによる耳下腺AQP5の発現制御とそのシグナル伝達経路, 第59回日本生理学会中国四国地方会, Nov. 2007.
19.	Tetsuya Akamatsu, アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi : 唾液腺腺房細胞の発生・分化・成熟化と水チャネルAQP5発現, 第59回日本生理学会中国四国地方会, Nov. 2007.
20.	プルワンティヌヌク, Daisuke Tsuji, アズリナアハマド, カラバシルミレーバ, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi : Transient increase in IL-6 by duct ligation leading to continuous elevation of Sca-1, a stem cells marker, in the mouse submandibular gland, 第49回歯科基礎医学会学術大会, Aug. 2007.
21.	カラバシルミレーバ, Takahiro Hasegawa, アズリナアハマド, プルワンティヌヌク, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi : Analyses of function of rat mutant AQP5 expressed in MDCK II cells, 第49回歯科基礎医学会, Aug. 2007.
22.	アズリナアハマド, カラバシルミレーバ, プルワンティヌヌク, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : Regulation of submandibular gland AQP5 protein expression by lysosomal system, 第49回歯科基礎医学会, Aug. 2007.
23.	Chenjuan Yao, アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi : 唾液腺AQP5およびAQP1発現のLPSによるdown-regulation, 第49回歯科基礎医学会, Aug. 2007.
24.	Tetsuya Akamatsu, アズリナアハマド, プルワンティヌヌク, カラバシルミレーバ, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi : 唾液腺腺房細胞の分化とAQP5発現, 第49回歯科基礎医学会, Aug. 2007.
25.	カラバシルミレーバ, Takahiro Hasegawa, プルワンティヌヌク, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Functional analyses of rat mutant AQP5 expressed in vitro system and it's implication to abnormal saliva secretion, 第48回歯科基礎医学会, Sep. 2006.
26.	Xuefei Li, Nunuk Purwanti, Mileva R. Karabasil, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : ラット唾液腺AQP5，AQP1，及びリソゾーム酵素系に対する自律神経切除とSNI2011投与の影響, 第48回歯科基礎医学会, Sep. 2006.
27.	Chenjuan Yao, Mileva R. Karabasil, Nunuk Purwanti, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : LPSによる唾液腺AQP5およびAQP1の発現制御とそのシグナル伝達経路, 第48回歯科基礎医学会, Sep. 2006.
28.	Tetsuya Akamatsu, Nunuk Purwanti, Mileva R. Karabasil, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : 顎下腺の分枝形成とAQP5発現は前駆体蛋白質変換酵素PACE4により調節される, 第48回歯科基礎医学会, Sep. 2006.
29.	プルワンティヌヌク, Daisuke Tsuji, カラバシルミレーバ, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, Kouji Itou and Kazuo Hosoi : Effect of duct ligation on the expression of cellular markers of duct/acini and side population dynamics of the mouse submandibular gland, 第48回歯科基礎医学会学術大会, Sep. 2006.
30.	Tetsuya Akamatsu, プルワンティヌヌク, カラバシルミレーバ, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : 唾液腺発生におけるsubtilisin-like proprotein convertaseの役割, 第28回分子生物学会年会, ワークショップW3G「プロテアーゼによる細胞分化・機能制御, 植物から動物まで/Proteases as biomodulators in bacteria, plant and animal」, Dec. 2005.
31.	Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Effects of sympathectomy, parasympathectomy, administration of SNI-2011 on the expression of AQP5 and AQP1 in the rat submandibular gland, 第78回日本生化学会大会, Oct. 2005.
32.	Chenjuan Yao, Nunuk Purwanti, Chisato Kosugi-Tanaka, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Kallikrein mK13 is a candidate of pro-IL-1βprocessing enzyme in the mouse salivary gland, 第78回日本生化学会大会, Oct. 2005.
33.	Tetsuya Akamatsu, Nunuk Purwanti, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : Developmental regulation of the submandibular gland by ECM-bound proprotein convertase PACE4, 第78回日本生化学会大会, Oct. 2005.
34.	Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : ラット顎下腺AQP5並びにAQP1に対する交感神経切除・副交感神経切除及びSNI-2011投与の影響, 第47回歯科基礎医学会, Sep. 2005.
35.	Chenjuan Yao, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : マウス唾液腺カリクレインmK13はpro-IL-1βプロセシング酵素の候補である, 第47回歯科基礎医学会, Sep. 2005.
36.	Tetsuya Akamatsu, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : 顎下腺発生における前駆体蛋白質変換酵素PACE4の関与, 第47回歯科基礎医学会, Sep. 2005.
37.	Kazuo Hosoi, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori, ミレーバカラバシル and ヌヌクプルワンティ : 外分泌腺における水チャネル，アクアポリンの発現と機能調節, 第47回歯科基礎医学会サテライトシンポジウム「唾液分泌機構研究の最近の進歩」, Sep. 2005.
38.	Tetsuya Akamatsu, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : ECM-bound proprotein convertase PACE4 is a candidate regulator in the branching morphogenesis of rat submandibular gland, 第77回日本生化学会大会, Oct. 2004.
39.	Chenjuan Yao, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : マウス顎下腺におけるカリクレインmK13によるpro-IL1βの活性化, 第46回歯科基礎医学会, Sep. 2004.
40.	Tetsuya Akamatsu, Xuefei Li, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : 顎下腺の分枝形成と機能発現, 第46回歯科基礎医学会, Sep. 2004.
41.	Kawartarini Murdiastuti, Nahid Parvin, Chenjuan Yao, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : 水チャネル，アクアポリンの外分泌腺における発現と機能調節, 第45回日本生化学会中国・四国支部例会, May 2004.
42.	Tetsuya Akamatsu, Xuefei Li, Chenjuan Yao, Kawartarini Murdiastuti, Chisato Kosugi, Norio Kanamori and Kazuo Hosoi : ラット顎下腺の発生・分化・成熟と機能発現, 第45回日本生化学会中国・四国支部例会, May 2004.
43.	Chenjuan Yao, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : 実験的炎症による唾液腺サイトカインの誘導, 第45回歯科基礎医学会, Sep. 2003.
44.	Norio Kanamori, Tetsuya Akamatsu, Chisato Kosugi, Kawartarini Murdiastuti, Most. Nahid Parvin, Chenjuan Yao, Osamu Miki, Xuefei Li and Kazuo Hosoi : Jumping: An index behavior for the epileptic family of Mongolian gerbil. (Preliminary report), 第26回日本神経科学大会, Jul. 2003.
45.	Tetsuya Akamatsu, Most. Nahid Parvin, 小杉-田中知里, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : ラット顎下腺発生過程でのAQPsの発現と局在, 第75回日本生化学会大会, Oct. 2002.
46.	Kawartarini Murdiastuti, 三木修, Chenjuan Yao, Most. Nahid Parvin, 小杉-田中知里, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Divergent gene expression and localization of aquaporin 5 in the submandibular gland of Sprague-Dawley rats, 第44回歯科基礎医学会, Oct. 2002.
47.	Tetsuya Akamatsu, Most. Nahid Parvin, 小杉-田中知里, Chenjuan Yao, Norio Kanamori and Kazuo Hosoi : ラット顎下腺発生過程でのAQPsの発現と局在, 第44回歯科基礎医学会, Oct. 2002.
48.	Norio Kanamori, Tetsuya Akamatsu, 小杉-田中知里, Parvin Nahid Most., Chenjuan Yao and Kazuo Hosoi : 病態モデルスナネズミ近交化の試み(中間報告), 第25回日本神経科学大会, Jul. 2002.
49.	Most. Parvin Nahid, 小杉-田中知里, Tetsuya Akamatsu, 倉淵真悟, Norio Kanamori and Kazuo Hosoi : AQP5 in the rat duodenum-expression, localization, and effect of VIP, 第79回日本生理学会学術大会, Mar. 2002.
50.	津村恵子, Most. Parvin Nahid, Kawartarini Murdiastuti, Tetsuya Akamatsu, Norio Kanamori, 稲永清敏 and Kazuo Hosoi : 水代謝異常多飲多渇マウス(STR/N)の唾液腺および腎におけるアクアポリン(AQP)の発現, 第43回歯科基礎医学会学術大会, Sep. 2001.
51.	Tetsuya Akamatsu, Most Parvin Nahid, Kawartarini Murdiastuti, Norio Kanamori and Kazuo Hosoi : ラット唾液線発生過程でのAQPsの発現, 第43回歯科基礎医学会学術大会, Sep. 2001.
52.	Most Parvin Nahid, Kawartarini Murdiastuti, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Expression of AQP5 in the duodenum Brunner's gland and effects of VIP, 第43回歯科基礎医学会学術大会, Sep. 2001.
53.	Tetsuya Akamatsu, 津村恵子, 多田淳, Most. Nahid Parvin, Norio Kanamori and Kazuo Hosoi : 口腔組織発生におけるプロセシング酵素PACE4の役割, 日本生化学会第73回大会, Oct. 2000.
54.	Wei Wei, Most. Nahid Parvin, 津村恵子, 松浦幸子, Tetsuya Akamatsu, 多田淳, Norio Kanamori and Kazuo Hosoi : Induction of acute phase proteins in the salivary gland of rats, 第42回歯科基礎医学会学術大会, Sep. 2000.
55.	多田淳, 津村恵子, Tetsuya Akamatsu, Most. Nahid Parvin, Norio Kanamori and Kazuo Hosoi : 唾液腺培養細胞でのAQP5のトラフィッキング機構, 第42回歯科基礎医学会学術大会, Sep. 2000.
56.	Most. Nahid Parvin, Wei Wei, 津村恵子, 多田淳, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi : Aquaporin-5 water channel expression and localization in the rat salivary gland and gastrointestinal tract, 第42回歯科基礎医学会学術大会, Sep. 2000.
57.	Tetsuya Akamatsu, 松田佳子, 多田淳, 津村恵子, Most. Nahid Parvin, Norio Kanamori and Kazuo Hosoi : 歯牙形成における前駆体蛋白質活性化酵素SPCsの役割, 日本生化学会第72回大会, Oct. 1999.
58.	松浦幸子, 鈴木和夫, Tetsuya Akamatsu, 津村恵子, 多田淳 and Kazuo Hosoi : 口腔粘膜・肥満細胞でのキニノーゲンの発現, 第41回歯科基礎医学会学術大会, Sep. 1999.
59.	Tetsuya Akamatsu, 津村恵子, Norio Kanamori, 多田淳, Most. Nahid Parvin and Kazuo Hosoi : 前駆体蛋白質活性化酵素SPCのラット唾液腺発生過程での発現, 第41回歯科基礎医学会学術大会, Sep. 1999.
60.	Norio Kanamori, Kazuhito Satomura, Tetsuya Akamatsu and Kazuo Hosoi : スナネズミ総頚動脈結紮時の脳血流動態, 第22回日本神経科学大会, Jul. 1999.
61.	Tetsuya Akamatsu, 松田佳子, 辻明彦, 津村恵子, Norio Kanamori and Kazuo Hosoi : Subtilisin-like proprotein convertase PACE4 is a candidate processing protease of bone morphogenetic proteins during tooth formation, 6th CGGH Symposium, May 1999.
62.	Kazuo Hosoi, 津村恵子, 多田淳, Tetsuya Akamatsu, Norio Kanamori and 松浦幸子 : 浸潤唾液腺肥満細胞におけるキニノーゲンの発現, 第40回歯科基礎医学会学術大会, Oct. 1998.
63.	Norio Kanamori, Tetsuya Akamatsu and Kazuo Hosoi : 新たに開発した血管染色法と, それによって判定したスナネズミ大脳動脈輪欠損出現率の系統差, 第21回日本神経科学・第41回日本神経化学合同大会, Sep. 1998.

Et cetera, Workshop:

1.	Kazuo Hosoi : 「巻頭言」および「総括」, 徳島大学サマープログラム2015 報告書, Mar. 2016.
2.	Kazuo Hosoi : 巻頭言, 2015 年度徳島大学国際センター紀要・年報, Mar. 2016.
3.	Kazuo Hosoi : 対日理解促進交流プログラムKAKEHASHI project, 徳島大学国際センターニュース, No.24, Jan. 2016.
4.	Kazuo Hosoi : 「はじめに」, 徳島大学国際センター外部評価報告書, Mar. 2015.
5.	Kazuo Hosoi : 「巻頭言」および「総括」, 徳島大学サマープログラム2014 報告書, Mar. 2015.
6.	Kazuo Hosoi : 巻頭言, 2014 年度徳島大学国際センター紀要・年報, Mar. 2015.
7.	Kazuo Hosoi : 渡目前入学許可, 徳島大学国際センターニュース, No.23, Feb. 2015.
8.	Kazuo Hosoi : 留学生受入の意義, 徳島大学国際センターニュース, No.22, Aug. 2014.
9.	Kazuo Hosoi : 第4章寄稿「徳島大学に期待すること」, 徳島大学60周年史, 174, Jun. 2010.
10.	Kazuo Hosoi : 図書館と国際化事業に携わって，第3章寄稿「徳島大学の思い出」, 徳島大学60周年史, 149-150, Jun. 2010.
11.	Kazuo Hosoi : 2．4国際交流，2.4.2国際連携推進室, 徳島大学60周年史, 99-101, Jun. 2010.
12.	Yasuko OISHI and Kazuo Hosoi : 2．4国際交流，2.4.1国際センター, 徳島大学60周年史, 97-99, Jun. 2010.
13.	Kazuo Hosoi : 1．4留学生センターと国際センターの設置，3.国際センターの設置, 徳島大学60周年史, 14, Jun. 2010.
14.	Kazuo Hosoi : 巻頭言, 徳島大学国際センター紀要第5号・年報第6号 2009年度, No.5/6, Mar. 2010.
15.	Kazuo Hosoi : 寄稿法人化第1期終了によせて「国際化事業に携わって」, 躍進する徳島大学法人化第1期の歩み(2004-2010), Mar. 2010.
16.	Kazuo Hosoi : 国際センター長からのご挨拶―この1年を振り返ってー, 徳島大学国際センターニュース, No.13, Mar. 2010.
17.	Kazuo Hosoi : 第11回外分泌腺機能国際シンポジウム開催報告, HBS研究部だより, Vol.11, Nov. 2009.
18.	Kazuo Hosoi : 国際センター長からのご挨拶, 徳島大学国際センターニュース, No.12, Nov. 2009.
19.	Kazuo Hosoi : 巻頭言, 徳島大学国際センター紀要第4号・年報第5号 2008年度, No.4/5, Mar. 2009.
20.	Kazuo Hosoi : Greeting from the director, Facilitating academic partnership with other universities around the world, The University of Tokushima International Center pamphlet, 2009.
21.	Kazuo Hosoi : 国際センターへの改組に向けて⋯, 徳島大学国際センターパンフレット, Dec. 2008.
22.	Kazuo Hosoi : 大学教育の国際化加速プログラム-サマープログラム2008-, HBS研究部だより, Vol.9, Oct. 2008.
23.	Kazuo Hosoi : 巻頭言, 徳島大学留学生センター紀要第3号・年報第4号 2007年度, No.3/4, Mar. 2008.
24.	Kazuo Hosoi : 地域に根ざした国際化の推進, 徳島大学留学生センターニュース, No.10, Mar. 2008.
25.	Kazuo Hosoi : 留学生交流の意義, 徳島大学留学生センターニュース, No.9, Nov. 2007.
26.	Kazuo Hosoi : 口の中は唾液腺によって守られている, とくtalk 徳大広報, No.129, 5-6, Oct. 2007.
27.	Kazuo Hosoi : 徳島大学附属図書館の課題と今後について, メールマガジン，「すだち」, 2007.
28.	Kazuo Hosoi : 学術情報基盤と図書館, 高度情報基盤センター広報, No.13, Dec. 2006.
29.	Kazuo Hosoi : 徳島大学附属図書館の現状と課題, メールマガジン，「すだち」, No.4, May 2005.
30.	Tetsuya Akamatsu and Kazuo Hosoi : 顎下腺の発生・分化・成熟と機能発現, 生理学研究所研究会:唾液分泌機構解明に向けての戦略的展開, Feb. 2005.
31.	Tetsuya Akamatsu and Kazuo Hosoi : ラット顎下腺の発生・分化・成熟と機能発現, Strategy of infomatics, genomics and proteomics for salivary secretion research, Feb. 2004.
32.	Kazuo Hosoi : 蔵本分館の現状と課題, 徳島大学附属図書館報，「すだち」, No.64, 1-3, Dec. 2001.
33.	Kazuo Hosoi : Johns Hopkins大学で学んで, 城西歯科大学学生会, No.15, 19-23, Apr. 1986.

Report:

1.	Kazuo Hosoi, Norio Kanamori, Tetsuya Akamatsu and Chenjuan Yao : Molecular mechanism of expression and regulation of water channel, esp. aquaporins in the exocrine gland, , Report of research project, grant in-aid for scientific research (B), Tokushima, Mar. 2009.
2.	Kazuo Hosoi, Norio Kanamori, Tetsuya Akamatsu and Chisato Kosugi : Induction of inflammation cytokine and defense system of oral cavity: a trial in regeneration medicine, Report of research project, Grant-in-Aid for Exploratory Research, Tokushima, Mar. 2006, Tokushima, Mar. 2006.
3.	Kazuo Hosoi, Nobuyoshi Nakajo, Tatsuji Haneji and Tetsuya Akamatsu : Inflammation by mast cell kininogen and its suppression Development of a new drug, , Report of research project, grant in-aid for scientific research (B)(2), Tokushima, Mar. 2004.
4.	Keiko Tsumura and Kazuo Hosoi : Production of a salivary gland cell line expressing an aquaporin 5 mutant protein and approach to explore the mechanism for water secretion, Report of research project, grant in-aid for scientific research (C)(2), Tokushima, Mar. 2003.
5.	Kazuo Hosoi, Norio Kanamori, Tetsuya Akamatsu, Jun Tada and Keiko Tsumura : : Expression and regulation of a water channel, aquaporin, in the exocrine gland, Report of research project, grant in-aid for scientific research (C)(2), Tokushima, Mar. 2003.
6.	Kazuo Hosoi, Norio Kanamori, Sachiko Matsuura, Tetsuya Akamatsu and Takamasa Sawa : Molecular mechanism of expression and regulation of water channel proteins aquaporins in the salivary gland cells, Report of research project, grant in-aid for scientific research (C)(2), Tokushima, Mar. 2001.
7.	Kazuo Hosoi, Norio Kanamori and Yamato Kikkawa : A new physiologic function of tissue kallikrein family enzymes and processing of growth factor precursors,, Report of research project, grant in-aid for scientific research (C)(2), 1998 March), Tokushima, Mar. 1998.
8.	Kazuo Hosoi, Norio Kanamori and Yamato Kikkawa : Analysis of genes for tissue kallikrein family enzymes and processing of growth factor precursors, Report of research by special budget for education and research (Tokushima University), Tokushima, Dec. 1997. (Summary) マウス顎下腺に存在する4種の主要な組織カリクレイン(mK22，mK9，mK1，mK13)によるキニン遊離活性，並びにプロレニン変換活性を調べた．mK1は最も強いキニン遊離活性を示し，唾液腺以外にも尿，膵臓，消化管に局在した．この事からmK1はマウスの真性組織カリクレインであることが証明された．またキニノーゲナーゼ活性の弱いmK13は最も強いプロレニン変換活性を示した．
9.	Kazuo Hosoi, Kinji Kurihara and Kenji Sugita : : Regulation mechanism of EGF receptor functions via P2-purinergic receptors and related signal transduction system, , Report of research project, grant in-aid for scientific research (C), Tokushima, Mar. 1995.
10.	Kazuo Hosoi, Kinji Kurihara and Kenji Sugita : : Effects of extracellular ATP on Ca²⁺ and phosphatidylinositol metabolism and modulation of EGF receptor function, Report of research project, grant in-aid for scientific research (C), Sakado, Mar. 1990.
11.	Kazuo Hosoi : Development and differentiation of salivary gland -The hormonal regulation, Report of research project, grant in-aid for scientific research Collaborated research (A), Sakado, Mar. 1981.
12.	Kazuo Hosoi : : Study on hormone action in the salivary gland, Report of research project, grant in-aid for scientific research (D), Sakado, Mar. 1980.
13.	Kazuo Hosoi : Development and differentiation of salivary gland -The hormonal regulation, Report of research project, grant in-aid for scientific research Collaborated research (A), Sakado, Mar. 1980.
14.	Kazuo Hosoi : Study on hormone action in the salivary gland, Report of research project, grant in-aid for scientific research (C), 1979 March), Sakado, Mar. 1979.
15.	Masayoshi Kumegawa and Kazuo Hosoi : Research in molecular biology of development and differentiation of the salivary gland, 1979-80 Grant-in-Aid for Co-operative Research (A) Development and differentiation of the salivary gland, esp., hormonal regulation, Sakado, Mar. 1977.
16.	Kazuo Hosoi : Study on the mechanism of synthesis of androgen-dependent granules in the mouse submandibular gland, Report of research project, grant in-aid for scientific research, -Encouragement of Young Scientists (A) -, 1977 March), Sakado, Mar. 1977.

Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)

Elucidation of the molecular mechanism on the differentiation/maturation and functional expression of salivary acinar cell toward conquest of xerostomia. (Project/Area Number: 23592737 )
病態時における外分泌腺型水チャネル、AQP5の発現と機能調節の分子機構 (Project/Area Number: 23592736 )
Immunolocalization of hormone receptors and their regulatory system in the hormonally responsive ducts of the mouse salivary glands (Project/Area Number: 20592158 )
Moecular meohanism of expression and regulation of the water channe1, aquapor in 5 in the exocrine gland (Project/Area Number: 18390493 )
唾液腺における炎症性サイトカインの誘導と口腔の防御システム:再生医療への試み (Project/Area Number: 16659513 )
Molecular mechanisms of expression and regulation of water channel proteins aquaporins in the exocrine gland cells (Project/Area Number: 13671941 )
Molecular mechanisms of expression and regulation of water channel proteins aquaporins in the exocrine gland cells (Project/Area Number: 13671940 )
Inflammation by mast cell kininogen and its suppression -Development of a new drug (Project/Area Number: 13557154 )
Molecular mechanisms of expression and regulation of function of water channel proteins aquaporins in the salivary gland cells (Project/Area Number: 11671844 )
A new physiologic function of tissue kallikrein family enzymes and processing of growth factor precursors (Project/Area Number: 08672129 )
Regulation of the function of EGF receptors via P_2 purinergic receptors and related cell signaling systems (Project/Area Number: 04807133 )
Effects of extracellular ATP on Ca^<2+> movement, and phosphoinositide metabolism, leading to a functional change of EGF receptor (Project/Area Number: 62570840 )
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Professor Emeritus : Hosoi, Kazuo

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Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)