Tokushima University / Educator and Researcher Directory --- Matsushita, Yosuke

Field of Study

Subject of Study

Book / Paper

Academic Paper (Judged Full Paper):

1.	Atsushi Saito, Yasunao Kamikawa, Taichi Ito, Koji Matsuhisa, Masayuki Kaneko, Takumi Okamoto, Tetsuro Yoshimaru, Yosuke Matsushita, Toyomasa Katagiri and Kazunori Imaizumi : p53-independent tumor suppression by cell-cycle arrest via CREB/ATF transcription factor OASIS, Cell Reports, Vol.42, No.5, 112479, 2023. (Summary) CREB/ATF transcription factor OASIS/CREB3L1 is upregulated in long-term-cultured astrocytes undergoing cell-cycle arrest due to loss of DNA integrity by repeated replication. However, the roles of OASIS in the cell cycle remain unexplored. We find that OASIS arrests the cell cycle at G/M phase after DNA damage via direct induction of p21. Cell-cycle arrest by OASIS is dominant in astrocytes and osteoblasts, but not in fibroblasts, which are dependent on p53. In a brain injury model, Oasis reactive astrocytes surrounding the lesion core show sustained growth and inhibition of cell-cycle arrest, resulting in prolonged gliosis. We find that some glioma patients exhibit low expression of OASIS due to high methylation of its promoter. Specific removal of this hypermethylation in glioblastomas transplanted into nude mice by epigenomic engineering suppresses the tumorigenesis. These findings suggest OASIS as a critical cell-cycle inhibitor with potential to act as a tumor suppressor. (Keyword) Mice / Animals / Tumor Suppressor Protein p53 / Cyclic AMP Response Element-Binding Protein / Mice, Nude / Cell Cycle Checkpoints / Activating Transcription Factors / Cyclin-Dependent Kinase Inhibitor p21 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.celrep.2023.112479 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37178686 ● Summary page in Scopus @ Elsevier: 2-s2.0-85160076948 (DOI: 10.1016/j.celrep.2023.112479, PubMed: 37178686, Elsevier: Scopus)
2.	Kosaku Okuda, Kengo Nakahara, Akihiro Ito, Yuta Iijima, Ryosuke Nomura, Ashutosh Kumar, Kana Fujikawa, Kazuya Adachi, Yuki Shimada, Satoshi Fujio, Reina Yamamoto, Nobumasa Takasugi, Kunishige Onuma, Mitsuhiko Osaki, Futoshi Okada, Taichi Ukegawa, Yasuo Takeuchi, Norihisa Yasui, Atsuko Yamashita, Hiroyuki Marusawa, Yosuke Matsushita, Toyomasa Katagiri, Takahiro Shibata, Koji Uchida, Sheng-Yong Niu, B Nhi Lang, Tomohiro Nakamura, J Kam Y Zhang, A Stuart Lipton and Takashi Uehara : Pivotal role for S-nitrosylation of DNA methyltransferase 3B in epigenetic regulation of tumorigenesis., Nature Communications, Vol.14, No.1, 2023. (Summary) DNA methyltransferases (DNMTs) catalyze methylation at the C5 position of cytosine with S-adenosyl-L-methionine. Methylation regulates gene expression, serving a variety of physiological and pathophysiological roles. The chemical mechanisms regulating DNMT enzymatic activity, however, are not fully elucidated. Here, we show that protein S-nitrosylation of a cysteine residue in DNMT3B attenuates DNMT3B enzymatic activity and consequent aberrant upregulation of gene expression. These genes include Cyclin D2 (Ccnd2), which is required for neoplastic cell proliferation in some tumor types. In cell-based and in vivo cancer models, only DNMT3B enzymatic activity, and not DNMT1 or DNMT3A, affects Ccnd2 expression. Using structure-based virtual screening, we discovered chemical compounds that specifically inhibit S-nitrosylation without directly affecting DNMT3B enzymatic activity. The lead compound, designated DBIC, inhibits S-nitrosylation of DNMT3B at low concentrations (IC (Keyword) Animals / Humans / Mice / Cell Transformation, Neoplastic / DNA (Cytosine-5-)-Methyltransferase 1 / DNA (Cytosine-5-)-Methyltransferases / DNA Methylation / DNA Modification Methylases / Epigenesis, Genetic (Tokushima University Institutional Repository) ● Metadata: 118929 (Link to Publication Site) ● Publication site (DOI): 10.1038/s41467-023-36232-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36739439 ● Search Scopus @ Elsevier (PMID): 36739439 ● Search Scopus @ Elsevier (DOI): 10.1038/s41467-023-36232-6 (Tokushima University Institutional Repository: 118929, DOI: 10.1038/s41467-023-36232-6, PubMed: 36739439)
3.	Hidetoshi Satoh, Shintaroh Ochi, Kosuke Mizuno, Yutaka Saga, Shohei Ujita, Mihiro Toyoda, Yuichi Nishiyama, Kasumi Tada, Yosuke Matsushita, Yuichi Deguchi, Keiji Suzuki, Yoshimasa Tanaka, Hiroshi Ueda, Toshiya Inaba, Yoshio Hosoi, Akinori Morita and Shin Aoki : Design, synthesis and biological evaluation of 2-pyrrolone derivatives as radioprotectors., Bioorganic & Medicinal Chemistry, Vol.67, 2022. (Summary) It is known that p53 is an important transcription factor and plays a central role in ionizing radiation (IR)-induced DNA damage responses such as cell cycle arrest, DNA repair and apoptosis. We previously reported that regulating p53 protein is an effective strategy for modulating cell fate by reducing the acute side effects of radiation therapy. Herein, we report on the discovery of STK160830 as a new radioprotector from a chemical library at The University of Tokyo and the design, synthesis and biological evaluation of its derivatives. The radioprotective activity of STK160830 itself and its derivatives that were synthesized in this work was evaluated using a leukemia cell line, MOLT-4 cells as a model of normal cells that express the p53 protein in a structure-activity relationships (SAR) study. The experimental results suggest that a direct relationship exists between the inhibitory effect of these STK160830 derivatives on the expression level of p53 and their radioprotective activity and that the suppression of p53 by STK160830 derivatives contribute to protecting MOLT-4 cells from apoptosis that is induced by exposure to radiation. (Keyword) Apoptosis / DNA Damage / DNA Repair / Tumor Suppressor Protein p53 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bmc.2022.116764 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35635928 ● Search Scopus @ Elsevier (PMID): 35635928 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bmc.2022.116764 (DOI: 10.1016/j.bmc.2022.116764, PubMed: 35635928)
4.	Sayumi Fujimori, Izumi Ohigashi, Hayato Abe, Yosuke Matsushita, Toyomasa Katagiri, Taketo M. Makoto, Takahama Yousuke and Takada Shinji : Fine-tuning of β-catenin in mouse thymic epithelial cells is required for postnatal T-cell development, eLife, Vol.11, e69088, 2022. (Summary) In the thymus, the thymic epithelium provides a microenvironment essential for the development of functionally competent and self-tolerant T cells. Previous findings showed that modulation of Wnt/β-catenin signaling in mouse thymic epithelial cells (TECs) disrupts embryonic thymus organogenesis. However, the role of β-catenin in TECs for postnatal T-cell development remains to be elucidated. Here, we analyzed gain-of-function (GOF) and loss-of-function (LOF) of β-catenin highly specific in mouse TECs. We found that GOF of β-catenin in TECs results in severe thymic dysplasia and T-cell deficiency beginning from the embryonic period. By contrast, LOF of β-catenin in TECs reduces the number of cortical TECs and thymocytes modestly and only postnatally. These results indicate that fine-tuning of β-catenin expression within a permissive range is required for TECs to generate an optimal microenvironment to support postnatal T-cell development. (Keyword) Animals / Epithelial Cells / Female / Mice / T-Lymphocytes / Thymus Gland / beta Catenin (Tokushima University Institutional Repository) ● Metadata: 116664 (Link to Publication Site) ● Publication site (DOI): 10.7554/eLife.69088 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35042581 ● Search Scopus @ Elsevier (PMID): 35042581 ● Search Scopus @ Elsevier (DOI): 10.7554/eLife.69088 (Tokushima University Institutional Repository: 116664, DOI: 10.7554/eLife.69088, PubMed: 35042581)
5.	Akinori Morita, Shintaro Ochi, Hidetoshi Satoh, Shohei Ujita, Yosuke Matsushita, Kasumi Tada, Mihiro Toyoda, Yuichi Nishiyama, Kosuke Mizuno, Yuichi Deguchi, Keiji Suzuki, Yoshimasa Tanaka, Hiroshi Ueda, Toshiya Inaba, Yoshio Hosoi and Shin Aoki : A Novel RNA Synthesis Inhibitor, STK160830, Has Negligible DNA-Intercalating Activity for Triggering A p53 Response, and Can Inhibit p53-Dependent Apoptosis., Life, Vol.11, No.10, 2021. (Summary) RNA synthesis inhibitors and protein synthesis inhibitors are useful for investigating whether biological events with unknown mechanisms require transcription or translation; however, the dependence of RNA synthesis has been difficult to verify because many RNA synthesis inhibitors cause adverse events that trigger a p53 response. In this study, we screened a library containing 9600 core compounds and obtained STK160830 that shows anti-apoptotic effects in irradiated wild-type-p53-bearing human T-cell leukemia MOLT-4 cells and murine thymocytes. In many of the p53-impaired cells and p53-knockdown cells tested, STK160830 did not show a remarkable anti-apoptotic effect, suggesting that the anti-apoptotic activity is p53-dependent. In the expression analysis of p53, p53-target gene products, and reference proteins by immunoblotting, STK160830 down-regulated the expression of many of the proteins examined, and the downregulation correlated strongly with its inhibitory effect on cell death. mRNA expression analyses by qPCR and nascent RNA capture kit revealed that STK160830 showed a decreased mRNA expression, which was similar to that induced by the RNA synthesis inhibitor actinomycin D but differed to some extent. Furthermore, unlike other RNA synthesis inhibitors such as actinomycin D, p53 accumulation by STK160830 alone was negligible, and a DNA melting-curve analysis showed very weak DNA-intercalating activity, indicating that STK160830 is a useful inhibitor for RNA synthesis without triggering p53-mediated damage responses. (Tokushima University Institutional Repository) ● Metadata: 116405 (Link to Publication Site) ● Publication site (DOI): 10.3390/life11101087 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34685458 ● Search Scopus @ Elsevier (PMID): 34685458 ● Search Scopus @ Elsevier (DOI): 10.3390/life11101087 (Tokushima University Institutional Repository: 116405, DOI: 10.3390/life11101087, PubMed: 34685458)
6.	Shun-ichi Toki, Tetsuro Yoshimaru, Yosuke Matsushita, Hitoshi Aibara, Masaya Ono, Koichi Tsuneyama, Koichi Sairyo and Toyomasa Katagiri : The survival and proliferation of osteosarcoma cells are dependent on the mitochondrial BIG3-PHB2 complex formation., Cancer Science, Vol.112, No.10, 4208-4219, 2021. (Summary) Previous studies reported the critical role of the brefeldin A-inhibited guanine nucleotide exchange protein 3-prohibitin 2 (BIG3-PHB2) complex in modulating estrogen signaling activation in breast cancer cells, yet its pathophysiological roles in osteosarcoma (OS) cells remain elusive. Here, we report a novel function of BIG3-PHB2 in OS malignancy. BIG3-PHB2 complexes were localized mainly in mitochondria in OS cells, unlike in estrogen-dependent breast cancer cells. Depletion of endogenous BIG3 expression by small interfering RNA (siRNA) treatment led to significant inhibition of OS cell growth. Disruption of BIG3-PHB2 complex formation by treatment with specific peptide inhibitor also resulted in significant dose-dependent suppression of OS cell growth, migration, and invasion resulting from G2/M-phase arrest and in PARP cleavage, ultimately leading to PARP-1/apoptosis-inducing factor (AIF) pathway activation-dependent apoptosis in OS cells. Subsequent proteomic and bioinformatic pathway analyses revealed that disruption of the BIG3-PHB2 complex might lead to downregulation of inner mitochondrial membrane protein complex activity. Our findings indicate that the mitochondrial BIG3-PHB2 complex might regulate PARP-1/AIF pathway-dependent apoptosis during OS cell proliferation and progression and that disruption of this complex may be a promising therapeutic strategy for OS. (Keyword) Animals / apoptosis / Apoptosis Inducing Factor / Bone Neoplasms / Cell Line, Tumor / Cell Movement / Cell Proliferation / Cell Survival / Cell-Penetrating Peptides / Databases, Factual / Down-Regulation / G2 Phase Cell Cycle Checkpoints / Gene Silencing / Guanine Nucleotide Exchange Factors / Humans / M Phase Cell Cycle Checkpoints / Membrane Proteins / Mice / Mice, Nude / mitochondria / Mitochondrial Membranes / Neoplasm Invasiveness / Neoplasm Transplantation / Osteosarcoma / Poly (ADP-Ribose) Polymerase-1 / Prohibitins / RNA, Small Interfering / Repressor Proteins (Tokushima University Institutional Repository) ● Metadata: 116580 (Link to Publication Site) ● Publication site (DOI): 10.1111/cas.15099 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34363714 ● Search Scopus @ Elsevier (PMID): 34363714 ● Search Scopus @ Elsevier (DOI): 10.1111/cas.15099 (Tokushima University Institutional Repository: 116580, DOI: 10.1111/cas.15099, PubMed: 34363714)
7.	Takashi Sugiyama, Naoya Murao, Hisae Kadowaki, Keizo Takao, Tsuyoshi Miyakawa, Yosuke Matsushita, Toyomasa Katagiri, Akira Futatsugi, Yohei Shinmyo, Hiroshi Kawasaki, Juro Sakai, Kazutaka Shiomi, Masamitsu Nakazato, Kohsuke Takeda, Katsuhiko Mikoshiba, L Hidde Ploegh, Hidenori Ichijo and Hideki Nishitoh : ERAD components Derlin-1 and Derlin-2 are essential for postnatal brain development and motor function., iScience, Vol.24, No.7, 2021. (Summary) and surprisingly also inhibited sterol regulatory element binding protein 2 (SREBP-2)-mediated brain cholesterol biosynthesis. In addition, reduced neurite outgrowth due to Derlin-1 deficiency was rescued by SREBP-2 pathway activation. Overall, our findings demonstrate that Derlins sustain brain cholesterol biosynthesis, which is essential for appropriate postnatal brain development and function. (Tokushima University Institutional Repository) ● Metadata: 117222 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.isci.2021.102758 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34355142 ● Search Scopus @ Elsevier (PMID): 34355142 ● Search Scopus @ Elsevier (DOI): 10.1016/j.isci.2021.102758 (Tokushima University Institutional Repository: 117222, DOI: 10.1016/j.isci.2021.102758, PubMed: 34355142)
8.	Hiroshi Ueda, Hiroyuki Neyama and Yosuke Matsushita : Lysophosphatidic Acid Receptor 1- and 3-Mediated Hyperalgesia and Hypoalgesia in Diabetic Neuropathic Pain Models in Mice., Cells, Vol.9, No.8, 2020. (Keyword) Animals / Blood Glucose / Body Weight / Carbamates / Diabetes Mellitus, Experimental / Diet, High-Fat / Hyperalgesia / Isoxazoles / Lysophospholipids / Male / Mice / Mice, Inbred C57BL / Mice, Knockout / Neuralgia / Phenylacetates / Propionates / Receptors, Lysophosphatidic Acid / Signal Transduction / Streptozocin (Tokushima University Institutional Repository) ● Metadata: 116514 (Link to Publication Site) ● Publication site (DOI): 10.3390/cells9081906 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32824296 ● Search Scopus @ Elsevier (PMID): 32824296 ● Search Scopus @ Elsevier (DOI): 10.3390/cells9081906 (Tokushima University Institutional Repository: 116514, DOI: 10.3390/cells9081906, PubMed: 32824296)
9.	Yukie Fujimoto, Natsuko Inoue, Koji Morimoto, Takahiro Watanabe, Seiichi Hirota, Michiko Imamura, Yosuke Matsushita, Toyomasa Katagiri, Haruki Okamura and Yasuo Miyoshi : Significant association between high serum CCL5 levels and better disease-free survival of patients with early breast cancer., Cancer Science, Vol.111, No.1, 209-218, 2019. (Summary) Analysis of anticancer immunity aids in assessing the prognosis of patients with breast cancer. From 250 operated breast cancers, we focused on serum levels of C-C motif chemokine ligand 5 (CCL5), which is involved in cancer immune reactions. Serum levels of CCL5 were measured using a cytometric bead-based immunoassay kit and CCL5 expression in cancer cells was determined using immunohistochemical staining. In addition, mRNA in cancer and stromal cells was analyzed by microdissection and comparison with the public dataset. Disease-free survival (DFS) of patients with high CCL5 levels (cut-off, 13.87 ng/mL; n = 192) was significantly better than those with low CCL5 levels (n = 58; hazard ratio, 0.20; 95% confidence interval, 0.10-0.39; P < .0001). An improved overall survival was observed in patients with high CCL5 levels compared to those with low CCL5 levels (P = .024). On the contrary, high immunohistochemical expression of CCL5 in cancer cells was significantly associated with decreased DFS. As serum CCL5 levels did not correlate with CCL5 expression in cancer cells and the relative expression of mRNA CCL5 was elevated in stromal cells in relation to cancer cells, serum CCL5 might be derived not from cancer cells, but from stromal cells. Expression of CCL5 in serum, but not in cancer cells, might contribute to improved patient prognosis mediating through not only immune reaction, but through other mechanisms. Determination of circulating CCL5 levels could be useful for predicting patient prognosis. (Keyword) Adult / Aged / Aged, 80 and over / Biomarkers, Tumor / Breast Neoplasms / Chemokine CCL5 / Disease-Free Survival / female / Humans / Middle Aged / Prognosis / RNA, Messenger (Tokushima University Institutional Repository) ● Metadata: 114897 (Link to Publication Site) ● Publication site (DOI): 10.1111/cas.14234 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31724785 ● Search Scopus @ Elsevier (PMID): 31724785 ● Search Scopus @ Elsevier (DOI): 10.1111/cas.14234 (Tokushima University Institutional Repository: 114897, DOI: 10.1111/cas.14234, PubMed: 31724785)
10.	Ryuichiro Kimura, Tetsuro Yoshimaru, Yosuke Matsushita, Taisuke Matsuo, Masaya Ono, Jae-Hyun Park, Mitsunori Sasa, Yasuo Miyoshi, Yusuke Nakamura and Toyomasa Katagiri : The GALNT6‑LGALS3BP axis promotes breast cancer cell growth., International Journal of Oncology, Vol.56, No.2, 581-595, 2019. (Summary) Polypeptide N‑acetylgalactosaminyltransferase 6 (GALNT6), which is involved in the initiation of O‑glycosylation, has been reported to play crucial roles in mammary carcinogenesis through binding to several substrates; however, its biological roles in mediating growth‑promoting effects remain unknown. The present study demonstrated a crucial pathophysiological role of GALNT6 through its O‑glycosylation of lectin galactoside‑binding soluble 3 binding protein (LGALS3BP), a secreted growth‑promoting glycoprotein, in breast cancer growth. The Cancer Genome Atlas data analysis revealed that high expression levels of GALNT6 were significantly associated with poor prognosis of breast cancer. GALNT6 O‑glycosylated LGALS3BP in breast cancer cells, whereas knockdown of GALNT6 by siRNA led to the inhibition of both the O‑glycosylation and secretion of LGALS3BP, resulting in the suppression of breast cancer cell growth. Notably, LGALS3BP is potentially O‑glycosylated at three sites (T556, T571 and S582) by GALNT6, thereby promoting autocrine cell growth, whereas the expression of LGALS3BP with three Ala substitutions (T556A, T571A and S582A) in cells drastically reduced GALNT6‑dependent LGALS3BP O‑glycosylation and secretion, resulting in suppression of autocrine growth‑promoting effect. The findings of the present study suggest that the GALNT6‑LGALS3BP axis is crucial for breast cancer cell proliferation and may be a therapeutic target and biomarker for mammary tumors. (Link to Publication Site) ● Publication site (DOI): 10.3892/ijo.2019.4941 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31894262 ● Search Scopus @ Elsevier (PMID): 31894262 ● Search Scopus @ Elsevier (DOI): 10.3892/ijo.2019.4941 (DOI: 10.3892/ijo.2019.4941, PubMed: 31894262)
11.	Izumi Ohigashi, Yu Tanaka, Kenta Kondou, Sayumi Fujimori, Hiroyuki Kondo, Amy Palin, Victoria Hoffmann, Mina Kozai, Yosuke Matsushita, Shinsuke Uda, Ryo Motosugi, Jun Hamazaki, Hiroyuki Kubota, Shigeo Murata, Keiji Tanaka, Toyomasa Katagiri, Hidetaka Kosako and Yousuke Takahama : Trans-omics Impact of Thymoproteasome in Cortical Thymic Epithelial Cells., Cell Reports, Vol.29, No.9, 2901-2916.e6, 2019. (Tokushima University Institutional Repository) ● Metadata: 115049 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.celrep.2019.10.079 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31775054 ● Search Scopus @ Elsevier (PMID): 31775054 ● Search Scopus @ Elsevier (DOI): 10.1016/j.celrep.2019.10.079 (Tokushima University Institutional Repository: 115049, DOI: 10.1016/j.celrep.2019.10.079, PubMed: 31775054)
12.	Natsuko Inoue, Wen Li, Yukie Fujimoto, Yosuke Matsushita, Toyomasa Katagiri, Haruki Okamura and Yasuo Miyoshi : High Serum Levels of Interleukin-18 Are Associated With Worse Outcomes in Patients With Breast Cancer., Anticancer Research, Vol.39, No.9, 5009-5018, 2019. (Summary) IL-18 levels may be useful for predicting the prognosis of patients who have received surgical treatment for breast cancer. (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.13691 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31519608 ● Search Scopus @ Elsevier (PMID): 31519608 ● Search Scopus @ Elsevier (DOI): 10.21873/anticanres.13691 (DOI: 10.21873/anticanres.13691, PubMed: 31519608)
13.	Kei Daizumoto, Tetsuro Yoshimaru, Yosuke Matsushita, Tomoya Fukawa, Hisanori Uehara, Masaya Ono, Masato Komatsu, Hiro-omi Kanayama and Toyomasa Katagiri : A DDX31/mutant-p53/EGFR axis promotes multistep progression of muscle invasive bladder cancer, Cancer Research, Vol.78, No.9, 2233-2247, 2018. (Summary) The p53 and EGFR pathways are frequently altered in bladder cancer, yet their contributions to its progression remain elusive. Here we report that DEAD box polypeptide 31 (DDX31) plays a critical role in the multistep progression of muscle-invasive bladder cancer (MIBC) through its sequential interactions with mutant p53 (mutp53) and EGFR. In early MIBC cells, nuclear DDX31-bound mutp53/SP1 enhanced mutp53 transcriptional activation, leading to migration and invasion of MIBC. Cytoplasmic DDX31 also bound EGFR and phospho-nucleolin in advanced MIBC, leading to EGFR-Akt signaling activation. High expression of both cytoplasmic DDX31 and p53 proteins correlated with poor prognosis in patients with MIBC, and blocking the DDX31/NCL interaction resulted in downregulation of EGFR/Akt signaling, eliciting an antitumor effect against bladder cancer. These findings reveal that DDX31 cooperates with mutp53 and EGFR to promote progression of MIBC, and inhibition of DDX31/NCL formation may lead to potential treatment strategies for advanced MIBC. DDX31 cooperates with mutp53 and EGFR to promote progression of muscle invasive bladder cancer. . (Tokushima University Institutional Repository) ● Metadata: 111804 (Link to Publication Site) ● Publication site (DOI): 10.1158/0008-5472.CAN-17-2528 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29440146 ● Search Scopus @ Elsevier (PMID): 29440146 ● Search Scopus @ Elsevier (DOI): 10.1158/0008-5472.CAN-17-2528 (Tokushima University Institutional Repository: 111804, DOI: 10.1158/0008-5472.CAN-17-2528, PubMed: 29440146)
14.	Yoshimasa Miyagawa, Yosuke Matsushita, Hiromu Suzuki, Masato Komatsu, Tetsuro Yoshimaru, Ryuichiro Kimura, Ayako Yanai, Junko Honda, Akira Tangoku, Mitsunori Sasa, Yasuo Miyoshi and Toyomasa Katagiri : Frequent downregulation of LRRC26 by epigenetic alterations is involved in the malignant progression of triple-negative breast cancer., International Journal of Oncology, 2018. (Summary) Triple-negative breast cancer (TNBC), defined as breast cancer lacking estrogen- and progesterone‑receptor expression and human epidermal growth factor receptor 2 (HER2) amplification, is a heterogeneous disease. RNA-sequencing analysis of 15 TNBC specimens and The Cancer Genome Atlas-TNBC dataset analysis identified the frequent downregulation of leucine-rich repeat-containing 26 (LRRC26), which negatively regulates nuclear factor-κB (NF-κB) signaling, in TNBC tissues. Quantitative polymerase chain reaction and bisulfite pyrosequencing analyses revealed that LRRC26 was frequently silenced in TNBC tissues and cell lines as a result of promoter methylation. LRRC26 expression was restored by 5-aza-2'-deoxycytidine (5'-aza-dC) treatment in HCC1937 TNBC cells, which lack LRRC26 expression. Notably, small interfering RNA-mediated knockdown of LRRC26 expression significantly enhanced the anchorage-independent growth, invasion and migration of HCC70 cells, whereas ectopic overexpression of LRRC26 in BT20 cells suppressed their invasion and migration. Conversely, neither knockdown nor overexpression of LRRC26 had an effect on cell viability in the absence of tumor necrosis factor-α (TNF-α) stimulation. Meanwhile, overexpression of LRRC26 caused the reduction of TNF-α-mediated NF-κB luciferase reporter activity, whereas depleting LRRC26 expression resulted in the upregulation of TNF-α-mediated NF-κB downstream genes [interleukin-6 (IL-6), IL-8 and C-X-C motif chemokine ligand-1]. Taken together, these findings demonstrate that LRRC26 is frequently downregulated in TNBC due to DNA methylation and that it suppresses the TNF-α-independent anchorage-independent growth, invasion and migration of TNBC cells. Loss of LRRC26 function may be a critical event in the aggressiveness of TNBC cells through a TNF-α/NF-κB-independent mechanism. (Link to Publication Site) ● Publication site (DOI): 10.3892/ijo.2018.4301 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29512727 ● Search Scopus @ Elsevier (PMID): 29512727 ● Search Scopus @ Elsevier (DOI): 10.3892/ijo.2018.4301 (DOI: 10.3892/ijo.2018.4301, PubMed: 29512727)
15.	Tetsuro Yoshimaru, Keisuke Aihara, Masato Komatsu, Yosuke Matsushita, Yasumasa Okazaki, Shinya Toyokuni, Junko Honda, Mitsunori Sasa, Yasuo Miyoshi, Akira Otaka and Toyomasa Katagiri : Stapled BIG3 helical peptide ERAP potentiates anti-tumour activity for breast cancer therapeutics., Scientific Reports, Vol.7, No.1, 1821, 2017. (Summary) Estradiol (E2) and the oestrogen receptor-alpha (ER) signalling pathway play pivotal roles in the proliferative activity of breast cancer cells. Recent findings show that the brefeldin A-inhibited guanine nucleotide-exchange protein 3-prohibitin 2 (BIG3-PHB2) complex plays a crucial role in E2/ER signalling modulation in breast cancer cells. Moreover, specific inhibition of the BIG3-PHB2 interaction using the ER activity-regulator synthetic peptide (ERAP: 165-177 amino acids), derived from -helical BIG3 sequence, resulted in a significant anti-tumour effect. However, the duration of this effect was very short for viable clinical application. We developed the chemically modified ERAP using stapling methods (stapledERAP) to improve the duration of its antitumour effects. The stapledERAP specifically inhibited the BIG3-PHB2 interaction and exhibited long-lasting suppressive activity. Its intracellular localization without the membrane-permeable polyarginine sequence was possible via the formation of a stable -helix structure by stapling. Tumour bearing-mice treated daily or weekly with stapledERAP effectively prevented the BIG3-PHB2 interaction, leading to complete regression of E2-dependent tumours in vivo. Most importantly, combination of stapledERAP with tamoxifen, fulvestrant, and everolimus caused synergistic inhibitory effects on growth of breast cancer cells. Our findings suggested that the stapled ERAP may be a promising anti-tumour drug to suppress luminal-type breast cancer growth. (Tokushima University Institutional Repository) ● Metadata: 112387 (Link to Publication Site) ● Publication site (DOI): 10.1038/s41598-017-01951-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28500289 ● Search Scopus @ Elsevier (PMID): 28500289 ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-017-01951-6 (Tokushima University Institutional Repository: 112387, DOI: 10.1038/s41598-017-01951-6, PubMed: 28500289)
16.	Uchida Hitoshi, Yosuke Matsushita, Araki Kohei, Mukae Takehiro and Ueda Hiroshi : Histone deacetylase inhibitors relieve morphine resistance in neuropathic pain after peripheral nerve injury., Journal of Pharmacological Sciences, Vol.128, No.4, 208-211, 2015. (Summary) Neuropathic pain is often insensitive to morphine. Our previous study has demonstrated that neuron-restrictive silencer factor represses mu opioid receptor (MOP) gene expression in the dorsal root ganglion (DRG) via histone hypoacetylation-mediated mechanisms after peripheral nerve injury, thereby causing loss of peripheral morphine analgesia. Here, we showed that histone deacetylase (HDAC) inhibitors, such as trichostatin A and valproic acid, restored peripheral and systemic morphine analgesia in neuropathic pain. Also, these agents blocked nerve injury-induced MOP down-regulation in the DRG. These results suggest that HDAC inhibitors could serve as adjuvant analgesics to morphine for the management of neuropathic pain. (Keyword) Acetylation / Analgesia / Analgesics / Animals / Down-Regulation / Drug Resistance / Ganglia, Spinal / gene expression / Histone Deacetylase Inhibitors / Histone Deacetylases / Histones / Hydroxamic Acids / Male / Mice, Inbred C57BL / Morphine / Neuralgia / Peripheral Nerve Injuries / Receptors, Opioid, mu / Valproic Acid (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jphs.2015.07.040 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26318673 ● Summary page in Scopus @ Elsevier: 2-s2.0-84940788267 (DOI: 10.1016/j.jphs.2015.07.040, PubMed: 26318673, Elsevier: Scopus)

Review, Commentary:

1.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : Elucidating Molecular-mechanism of Triple-negative Breast Cancer Through Comprehensive Genome Analysis, Japanese Journal of Breast Cancer, Vol.31, No.5, 377-385, Oct. 2016.

Proceeding of International Conference:

1.	Takeshi Harada, Asuka Oda, Yosuke Matsushita, Ryohei Sumitani, Yusuke Inoue, Tomoyo Hara, Masahiro Oura, Kimiko Sogabe, Tomoko Maruhashi, Mamiko Takahashi, Kiyoe Kurahashi, Shiroh Fujii, Shingen Nakamura, Hirokazu Miki, Masahiro Hiasa, Jumpei Teramachi, Toyomasa Katagiri and Masahiro Abe : ADAR1-dsRNA metabolism in myeloma cells with 1q amplification: a novel therapeutic target, 19th International Myeloma Society Annual Meeting, Aug. 2022.
2.	Toyomasa Katagiri and Yosuke Matsushita : Genetic and epigenetic alterations of SALL3 contributes to chemoresistance in triple-negative breast cancer, the 5th Annual Meeting of the International Society of Precision Cancer Medicine (ISPCM), virtual meeting, Online, Sep. 2021.
3.	Tetsuro Yoshimaru, Yosuke Matsushita, Sasa Mitsunori, Miyoshi Yasuo and Toyomasa Katagiri : BIG3 phosphatase inactivates tumor suppressor PHB2 via tis dephosphorylation to contribute to the breast carcinogenesis, The 14th International Conference on Protein Phosphatase, Online, Dec. 2020.
4.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, Suzuki Hiromu, Miyoshi Yasuo, Sasa Mitsunori and Toyomasa Katagiri : Frequent downregulation of SALL3 by genetic and epigenetic alterations is involved in progression and chemoresistance of triple negative breast cancers, American Association for Cancer Research ANNUAL MEETING 2019, Atlanta, Apr. 2019.
5.	Tetsuro Yoshimaru, Yosuke Matsushita, Sasa Mitsunori, Miyoshi Yasuo and Toyomasa Katagiri : PHB2 inactivation by AKAP-BIG3 is required for progression of HER2-overexpressing breast cancer, American Association for Cancer Research ANNUAL MEETING 2019, Atlanta, Apr. 2019.
6.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, Suzuki Hiromu, Miyoshi Yasuo, Sasa Mitsunori and Toyomasa Katagiri : Frequent downregulation of SALL3 by recurrent genetic and epigenetic alterations is involved in triple-negative breast cancers, American Association for Cancer Research ANNUAL MEETING 2018, Vol.78, No.13, Chicago, Apr. 2018. (Link to Publication Site) ● Publication site (DOI): 10.1158/1538-7445.AM2018-5315 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1158/1538-7445.AM2018-5315 (DOI: 10.1158/1538-7445.AM2018-5315)
7.	Tetsuro Yoshimaru, Yosuke Matsushita, Sasa Mitsunori, Miyoshi Yasuo and Toyomasa Katagiri : Overcoming trastuzumab resistance in HER2-overexpressing breast cancer by utilizing PHB2, a tumor suppressor of multiple resistance pathways, American Association for Cancer Research ANNUAL MEETING 2018, Chicago, Apr. 2018.
8.	Toyomasa Katagiri, Kei Daizumoto, Tetsuro Yoshimaru, Yosuke Matsushita, Tomoya Fukawa, Ono Masaya and Hiro-omi Kanayama : DDX31 cooperates with mutant p53 and EGFR to promote the multistep progression of invasive bladder cancer, American Association For Cancer Research ANNUAL MEETING 2018, Chicago, Apr. 2018.

Proceeding of Domestic Conference:

1.	齋藤敦, 上川泰直, 伊藤泰智, Tetsuro Yoshimaru, Yosuke Matsushita, Toyomasa Katagiri and 今泉和則 : Downregulation of transcription factor OASIS that induces p21 expression is involved in glioblastoma development, 第82回日本癌学会学術総会, Sep. 2023.
2.	Yosuke Matsushita, 奥村和正, 小松正人, Tetsuro Yoshimaru, 尾野雅哉, 笹三徳, 三好康雄 and Toyomasa Katagiri : RHBDL2-ASCT2 axis have critical roles for modulating glutaminolysis in triple negative breast cancer, 第82回日本癌学会学術総会, Sep. 2023.
3.	Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, 笹三徳, 三好康雄 and Toyomasa Katagiri : Tumor microenvironmental control via persistent ER stress response by Golgi-ER collaboration and new therapeutics, 第82回日本癌学会学術総会, Sep. 2023.
4.	Tetsuro Yoshimaru, Yosuke Matsushita, Mitsunori Sasa, Yasuo Miyoshi and Toyomasa Katagiri : Targeting BIG3-PHB2 interaction overcomes trastuzumab-resistance in patients with HER2-positive breast cancer, 第82回日本癌学会学術総会, Sep. 2023.
5.	加藤廉平, 前川滋克, 加藤陽一郎, 兼平貢, 高田亮, Yosuke Matsushita, Tetsuro Yoshimaru, Tomoya Fukawa and Toyomasa Katagiri : Critical involvement of PRELID2 in regulating mitochondrial homeostasis for renal carcinogenesis, 第82回日本癌学会学術総会, Sep. 2023.
6.	Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 6. 乳がん細胞の持続的小胞体ストレスの適応に必須な小胞体ストレス依存的なIRE1の小胞体‐ゴルジ体間輸送機構と新規治療戦略, 第27回日本がん分子標的治療学会学術集会, Jun. 2023.
7.	Yosuke Matsushita, Tetsuro Yoshimaru and Toyomasa Katagiri : 5. トリプルネガティブ乳癌におけるグルタミン代謝のマスターレギュレーターであるRHBDL2の役割解明, 第27回日本がん分子標的治療学会学術集会, Jun. 2023.
8.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 4. BIG3-PHB2複合体を標的としたHER2陽性乳がんの薬剤耐性を克服する分子内架橋型阻害ペプチドstERAPの開発, 第27回日本がん分子標的治療学会学術集会, Jun. 2023.
9.	Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, 三好康雄, 笹三徳 and Toyomasa Katagiri : 乳がん細胞における O型糖鎖修飾を介した IRE1の恒常的活性化機構, 第95回日本生化学会大会, Nov. 2022.
10.	Yosuke Matsushita, Kazumasa Okumura, Masato Komatsu, Tetsuro Yoshimaru, Ono Masaya, Akira Tangoku, Miyoshi Yasuo, Sasa Mitsunori and Toyomasa Katagiri : RHBDL2 has essential roles for glutaminolysis and chemoresistance in triple negative breast cancer, The 17th International Symposium of the Institute Network for Biomedical Sciences International Symposium on Tumor Biology in Kanazawa 2022, Oct. 2022.
11.	Tetsuro Yoshimaru, Yosuke Matsushita, Hidetaka Kosako, Sasa Mitsunorii, Miyoshi Yasuo and Toyomasa Katagiri : The plasma membrane BIG3-PHB2 complex contributes to the acquisition of trastuzumab-resistance in HER2-positive breast cancer, The 17th International Symposium of the Institute Network for Biomedical Sciences International Symposium on Tumor Biology in Kanazawa 2022, Oct. 2022.
12.	HAGIWARA Kosei, Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita, 三好康雄, 笹三徳 and Toyomasa Katagiri : 乳がん細胞におけるO 結合型糖鎖修飾GRP78/Bip の役割解明と創薬研究, 第81回日本癌学会学術総会, Oct. 2022.
13.	Abdullah S. Ili, Tetsuro Yoshimaru, Yosuke Matsushita, Masato Komatsu, Miyoshi Yasuo, Honda Junko, Ohsumi Shozo, Sasa Mitsunori and Toyomasa Katagiri : Whole-exome sequencing for the identification of Japanese familial breast cancer susceptibility genes, The 81st Annual Meeting of the Japanese Cancer Association, Oct. 2022.
14.	Yosuke Matsushita, Kazumasa Okumura, Masato Komatsu, Tetsuro Yoshimaru, 尾野雅哉, 三好康雄, 笹三徳 and Toyomasa Katagiri : トリプルネガティブ乳癌におけるRHBDL2 のグルタミン代謝調節機構, 第81回日本癌学会学術総会, Oct. 2022.
15.	Tetsuro Yoshimaru, Yosuke Matsushita, 笹三徳, 三好康雄 and Toyomasa Katagiri : 細胞膜BIG3-PHB2 複合体がHER2 陽性乳癌のトラスツズマブ耐性獲得に必須である, 第81回日本癌学会学術総会, Oct. 2022.
16.	加藤廉平, 前川滋克, 加藤陽一郎, 兼平貢, 高田亮, Yosuke Matsushita, Tetsuro Yoshimaru, Tomoya Fukawa, Toyomasa Katagiri and 小原航 : 3 次元培養下における新規の癌特異分子PRELID2 の分子機能の解明, 第81回日本癌学会学術総会, Oct. 2022.
17.	Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, 笹三徳, 三好康雄 and Toyomasa Katagiri : 乳がん細胞におけるO 結合型糖転移酵素の発現亢進はIRE1 の恒常的活性化を惹起する, 第81回日本癌学会学術総会, Sep. 2022.
18.	Yosuke Matsushita, Tetsuro Yoshimaru and Toyomasa Katagiri : トリプルネガティブ乳癌におけるRHBDL2のグルタミン代謝調節機構の解明, 第26回日本がん分子標的治療学会学術集会, Jul. 2022.
19.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : トラスツズマブ耐性HER2陽性乳がんの克服に向けたBIG3-PHB2相互作用を標的とした持続型阻害ペプチドの開発, 第26回日本がん分子標的治療学会学術集会, Jul. 2022.
20.	HAGIWARA Kosei, Keiji Uchiyama, Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 乳がん細胞におけるO結合型糖鎖修飾GRP78/Bipの役割解明と創薬研究, 第26回日本がん分子標的治療学会学術集会, Jun. 2022.
21.	Keiji Uchiyama, Yosuke Matsushita, Tetsuro Yoshimaru, HAGIWARA Kosei and Toyomasa Katagiri : 乳がん細胞におけるO型糖鎖修飾IRE1経路の恒常的活性化を標的とした新規治療戦略の可能性, 第26回日本がん分子標的治療学会学術集会, Jun. 2022.
22.	Yosuke Matsushita, 高橋定子, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 三好康雄, 本田純子, 紺谷桂一, 大住省三, 笹三徳 and Toyomasa Katagiri : 日本人家族性乳癌家系の新規感受性遺伝子の解析, 日本人類遺伝学会第66回大会第28回日本遺伝子診断学会大会合同開催, Oct. 2021.
23.	Tetsuro Yoshimaru, Yosuke Matsushita, 笹三徳, 三好康雄 and Toyomasa Katagiri : HER2陽性乳癌のトラスツズマブ耐性獲得に対するBIG3-PHB2複合体の病態生理学的役割, 第80回日本癌学会学術総会, Oct. 2021.
24.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, 新沼猛, 鈴木拓, Tetsuro Yoshimaru, 田嶋敦, Issei Imoto, 本田純子, 古川洋一, 中村祐輔, 三好康雄, 笹三徳 and Toyomasa Katagiri : SALL3のエピゲノム異常はトリプルネガティブ乳癌の薬剤抵抗性の一因となる, 第80回日本癌学会学術総会, Oct. 2021.
25.	Abdullah S. Ili, Yosuke Matsushita, Yasuko Takahashi, Masato Komatsu, Kazuma Kiyotani, Yasuo Miyoshi, Junko Honda, Shozo Ohsumi, Mitsunori Sasa and Toyomasa Katagiri : Identification and characterization of novel susceptibility genes in hereditary Japanese familial breast cancer, 第80回日本癌学会学術総会, Sep. 2021.
26.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : トラスツズマブ耐性HER2陽性乳がんに対するBIG3-PHB2相互作用の標的治療薬としての可能性, 第25回日本がん分子標的治療学会学術集会, May 2021.
27.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, 鈴木拓, Tetsuro Yoshimaru, Issei Imoto and Toyomasa Katagiri : 新規がん抑制因子SALL3不活化はトリプルネガティブ乳癌の化学療法抵抗性に関与する, 第25回日本がん分子標的治療学会学術集会, May 2021.
28.	Shun-ichi Toki, Tetsuro Yoshimaru, Hitoshi Aibara, Yosuke Matsushita and Toyomasa Katagiri : ミトコンドリア局在BIG3-PHB2複合体の抑制は骨肉腫細胞の悪性化を阻害する, 第24回日本がん分子標的治療学会学術集会, Oct. 2020.
29.	Yosuke Matsushita, Tetsuro Yoshimaru and Toyomasa Katagiri : トリプルネガティブ乳癌におけるRHBDL2のグルタミン代謝制御の役割解明, 第24回日本がん分子標的治療学会学術集会, Oct. 2020.
30.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : BIG3-PHB2標的治療薬によるトラスツズマブ耐性HER2陽性乳がんの克服, 第24回日本がん分子標的治療学会学術集会, Oct. 2020.
31.	Toyomasa Katagiri, Tetsuro Yoshimaru and Yosuke Matsushita : 乳がん治療耐性克服を目指した抑制因子活性化誘導PPI阻害ペプチドの開発, 第24回日本がん分子標的治療学会学術集会, Oct. 2020.
32.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 新沼猛, 鈴木拓, 本田純子, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : 新規癌抑制遺伝子SALL3はトリプルネガティブ乳癌の薬剤抵抗性に関与する, 第79回日本癌学会学術総会, Oct. 2020.
33.	Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, 笹三徳, 三好康雄 and Toyomasa Katagiri : BIG3-PHB2複合体の形成が，HER2陽性乳癌のトラスツズマブ耐性獲得を誘導する, 第79回日本癌学会学術総会, Oct. 2020.
34.	Shun-ichi Toki, Tetsuro Yoshimaru, Hitoshi Aibara, Yosuke Matsushita, 尾野雅哉 and Toyomasa Katagiri : ミトコンドリアBIG3-PHB2複合体阻害は骨肉腫の悪性化を抑制する, 第79回日本癌学会学術総会, Oct. 2020.
35.	Shun-ichi Toki, Tetsuro Yoshimaru, Hitoshi Aibara, Yosuke Matsushita and Toyomasa Katagiri : ミトコンドリア局在BIG3-PHB2複合体の機能抑制は骨肉腫細胞の悪性化を阻害する, 第35回日本整形外科学会基礎学術集会, Oct. 2020.
36.	Shun-ichi Toki, Tetsuro Yoshimaru, Hitoshi Aibara, Yosuke Matsushita, Koichi Sairyo and Toyomasa Katagiri : 骨肉腫細胞悪性化におけるBIG3の役割解明と分子間相互作用阻害ペプチド薬による抗腫瘍効果, 第93回日本整形外科学会学術総会, Jun. 2020.
37.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 新沼猛, 鈴木拓, Junko Honda, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : トリプルネガティブ乳癌の薬剤抵抗性に関与する新規癌抑制遺伝子SALL3の分子機構解明, 第1回日本癌学会若手の会, Feb. 2020.
38.	Ochi Shintaro, Satoh Hidetoshi, Ujita Shohei, Tada kasumi, Yosuke Matsushita, MiIzuno Kosuke, Deguchi Yuichi, Suzuki Keiji, Tanaka Yoshimasa, Ueda Hiroshi, Inaba Toshiya, Hosoi Yoshio, Aoki Shin and Akinori Morita : Mechanism of action of p53-regulating anti-cell death compound discovered by chemical library screening., The 62th Annual Meeting of the Japan Radiation Research Society, Nov. 2019.
39.	Yosuke Matsushita, 高橋定子, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 三好康雄, Junko Honda, 粕谷桂一, 大住省三, 笹三徳 and Toyomasa Katagiri : 全エキソーム解析による日本人家族性乳がん家系の新規感受性遺伝子の探索, 日本人類遺伝学会第64回大会, Nov. 2019.
40.	Tetsuro Yoshimaru, Yosuke Matsushita, 笹三徳, 三好康雄 and Toyomasa Katagiri : トラスツズマブ耐性乳がんに関連したBIG3-PHB2相互作用標的治療薬の開発, 第78回日本癌学会学術総会, Sep. 2019.
41.	加藤廉平, Tomoya Fukawa, Yosuke Matsushita, Tetsuro Yoshimaru, 尾野雅哉, Kei Daizumoto, 加藤陽一郎, 小原航 and Toyomasa Katagiri : 腎癌の癌化におけるPRELID2によるミトコンドリアROS制御機構の解明, 第78回日本癌学会学術総会, Sep. 2019.
42.	Shun-ichi Toki, Tetsuro Yoshimaru, Yosuke Matsushita, Hitoshi Aibara and Toyomasa Katagiri : 骨肉腫細胞悪性化におけるBIG3の役割解明と分子間相互作用阻害ペプチド薬による抗腫瘍効果, 第78回日本癌学会学術総会, Sep. 2019.
43.	Yosuke Matsushita, Kazumasa Okumura, Masato Komatsu, Ryuichiro Kimura, Tetsuro Yoshimaru, 尾野雅哉, Junko Honda, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : RHBDL2によるグルタミノリシスの制御はTNBCの悪性化や抗癌剤抵抗性に関連する, 第78回日本癌学会学術総会, Sep. 2019.
44.	Yosuke Matsushita, Masato Komatsu, Tetsuro Yoshimaru, 井本逸成, 鈴木拓 and Toyomasa Katagiri : トリプルネガティブ乳癌におけるがん抑制因子SALL3の不活化機構の解明, 第23回日本がん分子標的治療学会学術集会, Jun. 2019.
45.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : BIG3複合体によるがん抑制因子PHB2の不活制化を介したトラスツズマブ耐性乳がんの増殖機構と新規治療法, 第23回日本がん分子標的治療学会学術集会, Jun. 2019.
46.	Shun-ichi Toki, Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 骨肉腫細胞悪性化におけるBIG3の役割解明と分子間相互作用阻害ペプチド薬による抗腫瘍効果の検討, 第23回日本がん分子標的治療学会学術集会, Jun. 2019.
47.	佐藤秀哉, Shintaroh Ochi, 水野皓介, Yosuke Matsushita, 出口雄一, 鈴木啓司, 田中義正, 植田弘師, 稲葉俊哉, 細井義夫, Akinori Morita and 青木伸 : 放射線防護活性を有する 2-Oxopyrrole 類の設計・合成及び活性評価, 日本薬学会第139年回, Mar. 2019.
48.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 新規Aキナーゼアンカータンパク質BIG3による抑制因子PHB2の制御はHER2乳癌細胞増殖に必須である, 第41回日本分子生物学会年会, Nov. 2018.
49.	Shintaroh Ochi, 佐藤秀哉, Shohei Ujita, Kasumi Tada, Yosuke Matsushita, 水野皓介, 出口雄一, 鈴木啓司, 田中義正, 植田弘師, 稲葉俊哉, 細井義夫, 青木伸 and Akinori Morita : 化合物ライブラリーから選抜されたp53依存性細胞死抑制剤の作用機構解析, 日本放射線影響学会第61回大会, Nov. 2018.
50.	高橋定子, Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 本田純子, 大住省三, 笹三徳 and Toyomasa Katagiri : Identification and evaluation of novel susceptibility genes in Japanese familial breast cancer by whole exome sequencing, 第77回日本癌学会学術総会, Sep. 2018.
51.	加藤廉平, Tomoya Fukawa, Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, Kei Daizumoto, 加藤陽一郎, 小原航 and Toyomasa Katagiri : Critical roles of mitochondrial PRELID2 for renal carcinogenesis, 第77回日本癌学会学術総会, Sep. 2018.
52.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 新沼猛, 鈴木拓, 本田純子, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : Downregulation of SALL3 by recurrent genetic and epigenetic alterations is involved in triple negative breast cancers, 第77回日本癌学会学術総会, Sep. 2018.
53.	Kei Daizumoto, Tetsuro Yoshimaru, Yosuke Matsushita, Tomoya Fukawa, Hisanori Uehara, 尾野雅哉, Masato Komatsu, Hiro-omi Kanayama and Toyomasa Katagiri : Crucial roles of DDX31 as related to the status of TP53 in bladder cancer progression, 第77回日本癌学会学術総会, Sep. 2018.
54.	Tetsuro Yoshimaru, Yosuke Matsushita, 笹三徳, 三好康雄 and Toyomasa Katagiri : BIG3-PKA-PP1Cα複合体による癌抑制因子PHB2不活性化を介したトラスツズマブ耐性乳癌増殖機構と新規治療法開発, 第77回日本癌学会学術総会, Sep. 2018.
55.	Kazumasa Okumura, Yosuke Matsushita, Masato Komatsu, Ryuichiro Kimura, Tetsuro Yoshimaru, 尾野雅哉, 三好康雄, Junko Honda, 笹三徳, Akira Tangoku and Toyomasa Katagiri : Ritical pathophysiological roles of a potential therapeutic target RHBDL2 in triple negative breast cancer, 第77回日本癌学会学術総会, Sep. 2018.
56.	佐藤秀哉, Shintaroh Ochi, 水野皓介, Yosuke Matsushita, 出口雄一, 鈴木啓司, 田中義正, 植田弘師, 稲葉俊哉, 細井義夫, Akinori Morita and 青木伸 : 2—oxopyrrole 骨格を有する放射線防護剤の設計・合成及び活性評, 第62回日本薬学会関東支部大会, Sep. 2018.
57.	Yosuke Matsushita, Masato Komatsu, Tetsuro Yoshimaru and Toyomasa Katagiri : トリプルネガティブ乳がんの悪性化におけるRHBDL2の役割解明と創薬開発, 第22回日本がん分子標的治療学会学術集会, May 2018.
58.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 宮川義仁, 本田純子, Issei Imoto, Akira Tangoku, 鈴木拓, 三好康雄, 笹三徳 and Toyomasa Katagiri : Identification of recurrent genetic and epigenetic alterations in triple negative breast, 日本人類遺伝学会第62回大会, Nov. 2017.
59.	Shintaroh Ochi, Shohei Ujita, Kasumi Tada, Yosuke Matsushita, 水野皓介, 佐藤秀哉, 青木伸, 出口雄一, 鈴木啓司, 田中義正, 植田弘師, 稲葉俊哉, 細井義夫 and Akinori Morita : ケミカルライブラリーから選抜されたp53制御性放射線防護剤の作用機構解析, 日本放射線影響学会第60回大会, Oct. 2017.
60.	Tetsuro Yoshimaru, 尾野雅哉, Yosuke Matsushita, Masato Komatsu, 笹三徳, 三好康雄 and Toyomasa Katagiri : BIG3-PKA-PP1Cα複合体による癌抑制因子PHB2不活性化を介したエストロゲン依存性乳癌増殖機構と新規治療法開発, 第76回日本癌学会学術総会, Sep. 2017.
61.	高橋定子, Yosuke Matsushita, Masato Komatsu, Tetsuro Yoshimaru, 本田純子, 大住省三, 三木義男, Issei Imoto, 三好康雄, 笹三徳 and Toyomasa Katagiri : 日本人家族性乳がん家系の全エキソーム解析による新規家族性乳がん感受性遺伝子の同定, 第76回日本癌学会学術総会, Sep. 2017.
62.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 宮川義仁, 本田純子, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : TNBCにおける包括的なゲノム解析によるZNFタンパク質のジェネティックかつエピジェネティックな変化の同定, 第76回日本癌学会学術総会, Sep. 2017.
63.	Kazumasa Okumura, Yosuke Matsushita, Masato Komatsu, Ryuichiro Kimura, Tetsuro Yoshimaru, 尾野雅哉, 三好康雄, Junko Honda, 笹三徳, Akira Tangoku and Toyomasa Katagiri : 《Japanese Oral Sessions》トリプルネガティブ乳がんの悪性化におけるRHBDL2の役割解明, 第76回日本癌学会学術総会, Sep. 2017.
64.	加藤廉平, Tomoya Fukawa, Tetsuro Yoshimaru, Yosuke Matsushita, 尾野雅哉, 小原航 and Toyomasa Katagiri : 腎癌の癌化におけるPRELID2の重要な役割, 第76回日本癌学会学術総会, Sep. 2017.
65.	Tetsuro Yoshimaru, Yosuke Matsushita and Toyomasa Katagiri : 分子内架橋型BIG3-PHB2相互作用阻害ペプチドERAPによるホルモン依存性乳がん新規治療法の開発, 第21回日本がん分子標的治療学会学術集会, Jun. 2017.
66.	Yosuke Matsushita, Masato Komatsu, Tetsuro Yoshimaru, 鈴木拓, Issei Imoto and Toyomasa Katagiri : 全エクソームシーケンス解析によるトリプルネガティブ乳癌の分子特性の解明, 第21回日本がん分子標的治療学会学術集会, Jun. 2017.
67.	Tetsuro Yoshimaru, Yosuke Matsushita, Masato Komatsu, 岡崎泰昌, 豊國伸哉, 笹三徳, 三好康雄 and Toyomasa Katagiri : 内分泌療法耐性乳がんに対するBIG3-PHB2相互作用阻害ペプチドの開発, 第75回日本癌学会学術総会, Oct. 2016.
68.	瀧亮祐, Tetsuro Yoshimaru, 大豆本圭, Yosuke Matsushita, Ryuichiro Kimura, 尾野雅哉 and Toyomasa Katagiri : BIG3-PHB2相互作用を標的とした前立腺がん治療法の開発の可能性, 第75回日本癌学会学術総会, Oct. 2016.
69.	Kazumasa Okumura, Masato Komatsu, Ryuichiro Kimura, 尾野雅哉, Tetsuro Yoshimaru, Yosuke Matsushita, 三好康雄, 本田純子, 笹三徳, Akira Tangoku and Toyomasa Katagiri : トリプルネガティブ乳癌で高発現が認められるTNRHP1の発現亢進は癌の悪性度と相関する, 第75回日本癌学会学術総会, Oct. 2016.
70.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 宮川義仁, 本田純子, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : 全エキソーム解析によるトリプルネガティブ乳癌の分子特性の解明, 第75回日本癌学会学術総会, Oct. 2016.

Et cetera, Workshop:

1.	Yosuke Matsushita and Toyomasa Katagiri : --, キアゲンバイオインフォマティクスユーザーグループミーティング, May 2016.
2.	Yosuke Matsushita, Masato Komatsu, Kazuma Kiyotani, Tetsuro Yoshimaru, 宮川義仁, 本田純子, Issei Imoto, Akira Tangoku, 三好康雄, 笹三徳 and Toyomasa Katagiri : --, 第75回徳島乳腺研究会, Apr. 2016.

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

乳癌患者由来オルガノイド・動物モデルの臨床的有用性の検証と新規治療開発への応用 (Project/Area Number: 24K11755 )
Development of biomarkers and new treatments for metastatic breast cancer by eribulin (Project/Area Number: 22K08764 )
新規家族性乳がん感受性遺伝子の同定と既知原因遺伝子のVUSリスク評価法の確立 (Project/Area Number: 21K07125 )
Identification of recurrent genetic and epigenetic alterations of SALL3 in TNBC by comprehensive genomic analysis (Project/Area Number: 18K07200 )
Drug discovery in breast cancer utilizing reactivation of tumor suppressors (Project/Area Number: 17K19601 )
Clarification of novel pathophysiological roles of BIG3 in breast cancer cells (Project/Area Number: 16H05153 )
Screening of small molecule compounds that inhibits interaction between PD-1 and PD-L1 (Project/Area Number: 15K21235 )
Search by Researcher Number (70634450)