Tokushima University / Educator and Researcher Directory --- Uchida, Takayuki

Field of Study

Subject of Study

Book / Paper

Book:

1.	Takayuki Uchida and Takeshi Nikawa : 微小重力環境における筋萎縮発生メカニズムへの新展開, HOKURYUKAN, Tokyo, Oct. 2018. (Keyword) mitochondria / muscle atrophy
2.	Takayuki Uchida and Takeshi Nikawa : サルコペニア発症におけるメカニカルストレスの関与, Apr. 2016. (Keyword) muscle / oxidative stress

Academic Paper (Judged Full Paper):

1.	Takayuki Uchida, Kohno Madoka, Chinami Itoh, Erika Yamano, Hiroki Matsuki, MIZANUR MD Rahman, ANAYT ULLA, Minori Suzuki, Takahiro Ishiguro and Takeshi Nikawa : Inhibitory Effect of Kori-tofu Protein on Denervation-Induced Atrogene Expression in Mouse Skeletal Muscle, Biological Sciences in Space, Vol.38, 1-7, 2024.
2.	Keisuke Ozaki, Tomoya Fukawa, Kei Daizumoto, Yutaro Sasaki, Yoshiteru Ueno, Megumi Tsuda, Takayuki Uchida, Yoshito Kusuhara, Yasuyo Yamamoto, Kunihisa Yamaguchi, Masayuki Takahashi and Hiro-omi Kanayama : The impact of nutritional status and changes of body composition on the prognosis of metastatic renal cell carcinoma patients., The Journal of Medical Investigation : JMI, Vol.70, No.1.2, 80-87, 2023. (Summary) Nutritional status of mRCC patients may predict changes in body composition and be associated with their prognosis. J. Med. Invest. 70 : 80-87, February, 2023. (Keyword) Humans / Carcinoma, Renal Cell / Kidney Neoplasms / Nutritional Status / Prognosis / Body Composition / Retrospective Studies / Protein Kinase Inhibitors (Tokushima University Institutional Repository) ● Metadata: 118311 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.70.80 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37164748 ● Search Scopus @ Elsevier (PMID): 37164748 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.70.80 (Tokushima University Institutional Repository: 118311, DOI: 10.2152/jmi.70.80, PubMed: 37164748)
3.	ANAYT ULLA, Kanae Osaki, Mizanur Md Rahman, Reiko Nakao, Takayuki Uchida, Isafumi Maru, Kazuaki Mawatari, Tomoya Fukawa, Hiro-omi Kanayama, Iori Sakakibara, Katsuya Hirasaka and Takeshi Nikawa : Morin improves dexamethasone-induced muscle atrophy by modulating atrophy-related genes and oxidative stress in female mice., Bioscience, Biotechnology, and Biochemistry, Vol.86, No.10, 1448-1458, 2022. (Summary) This study investigated the effect of morin, a flavonoid, on dexamethasone-induced muscle atrophy in C57BL/6J female mice. Dexamethasone (10 mg/kg body weight) for 10 days significantly reduced body weight, gastrocnemius and tibialis anterior muscle mass, and muscle protein in mice. Dexamethasone significantly upregulated muscle atrophy-associated ubiquitin ligases, including atrogin-1 and MuRF-1, and the upstream transcription factors FoxO3a and Klf15. Additionally, dexamethasone significantly induced the expression of oxidative stress-sensitive ubiquitin ligase Cbl-b and the accumulation of the oxidative stress markers malondialdehyde and advanced protein oxidation products in both the plasma and skeletal muscle samples. Intriguingly, morin treatment (20 mg/kg body weight) for 17 days effectively attenuated the loss of muscle mass and muscle protein and suppressed the expression of ubiquitin ligases while reducing the expression of upstream transcriptional factors. Therefore, morin might act as a potential therapeutic agent to attenuate muscle atrophy by modulating atrophy-inducing genes and preventing oxidative stress. (Keyword) Animals / Body Weight / Dexamethasone / Female / Flavones / Malondialdehyde / Mice / Mice, Inbred C57BL / Muscle Proteins / Muscle, Skeletal / Muscular Atrophy / Oxidative Stress / Tripartite Motif Proteins / Ubiquitin-Protein Ligases (Link to Publication Site) ● Publication site (DOI): 10.1093/bbb/zbac140 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35977398 ● Search Scopus @ Elsevier (PMID): 35977398 ● Search Scopus @ Elsevier (DOI): 10.1093/bbb/zbac140 (DOI: 10.1093/bbb/zbac140, PubMed: 35977398)
4.	Yuichiro Adachi, Masashi Masuda, Iori Sakakibara, Takayuki Uchida, Yuki Niida, Yuki Mori, Yuki Kamei, Yosuke Okumura, Hirokazu Ohminami, Kohta Ohnishi, Hisami Okumura, Takeshi Nikawa and Yutaka Taketani : All-trans retinoic acid changes muscle fiber type via increasing GADD34 dependent on MAPK signal., Life Science Alliance, Vol.5, No.7, 2022. (Summary) All-trans retinoic acid (ATRA) increases the sensitivity to unfolded protein response in differentiating leukemic blasts. The downstream transcriptional factor of PERK, a major arm of unfolded protein response, regulates muscle differentiation. However, the role of growth arrest and DNA damage-inducible protein 34 (GADD34), one of the downstream factors of PERK, and the effects of ATRA on GADD34 expression in muscle remain unclear. In this study, we identified ATRA increased the GADD34 expression independent of the PERK signal in the gastrocnemius muscle of mice. ATRA up-regulated GADD34 expression through the transcriptional activation of gene via inhibiting the interaction of homeobox Six1 and transcription co-repressor TLE3 with the MEF3-binding site on the gene promoter in skeletal muscle. ATRA also inhibited the interaction of TTP, which induces mRNA degradation, with AU-rich element on mRNA via p-38 MAPK, resulting in the instability of mRNA. Overexpressed GADD34 in C2C12 cells changes the type of myosin heavy chain in myotubes. These results suggest ATRA increases GADD34 expression via transcriptional and post-transcriptional regulation, which changes muscle fiber type. (Keyword) Animals / Gene Expression Regulation / MAP Kinase Signaling System / Mice / Muscle Fibers, Skeletal / Protein Phosphatase 1 / RNA, Messenger / Transcription Factors / Tretinoin (Tokushima University Institutional Repository) ● Metadata: 117429 (Link to Publication Site) ● Publication site (DOI): 10.26508/lsa.202101345 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35318262 ● Search Scopus @ Elsevier (PMID): 35318262 ● Search Scopus @ Elsevier (DOI): 10.26508/lsa.202101345 (Tokushima University Institutional Repository: 117429, DOI: 10.26508/lsa.202101345, PubMed: 35318262)
5.	Kitahata Kanako, Takayuki Uchida, Taniguchi Runa, Kato Ayano, Kosuke Sugiura, Iori Sakakibara, Oarada Motoko, Tomoya Fukawa, Junsoo Park, Inho Choi and Takeshi Nikawa : Additional effects of simultaneous treatment with C14-Cblin and celastrol on the clinorotation-induced rat L6 myotube atrophy, The Journal of Medical Investigation : JMI, Vol.69, No.1,2, 127-134, 2022. (Summary) Two novel reagents, N-myristoylated Cbl-b inhibitory peptide (C14-Cblin) and celastrol, a quinone methide triterpene, are reported to be effective in preventing myotube atrophy. The combined effects of C14-Cblin and celastrol on rat L6 myotubes atrophy induced by 3D-clinorotation, a simulated microgravity model, was investigated in the present study. We first examined their effects on expression in atrogenes. Increase in MAFbx1/atrogin-1 and MuRF-1 by 3D-clinorotation was significantly suppressed by treatment with C14-Cblin or celastrol, but there was no additive effect of simultaneous treatment. However, celastrol significantly suppressed the upregulation of Cbl-b and HSP70 by 3D-clinorotation. Whereas 3D-clinorotation decreased the protein level of IRS-1 in L6 myotubes, C14-Cblin and celastrol inhibited the degradation of IRS-1. C14-Cblin and celastrol promoted the phosphorylation of FOXO3a even in microgravity condition. Simultaneous administration of C14-Cblin and celastrol had shown little additive effect in reversing the impairment of IGF-1 signaling by 3D-clinorotation. While 3D-clinorotation-induced marked oxidative stress in L6 myotubes, celastrol suppressed 3D-clinorotation-induced ROS production. Finally, the C14-Cblin and celastrol-treated groups were inhibited decrease in L6 myotube diameter and increased the protein content of slow-twitch MyHC cultured under 3D-clinorotation. The simultaneous treatment of C14-Cblin and celastrol additively prevented 3D-clinorotation-induced myotube atrophy than single treatment. J. Med. Invest. 69 : 127-134, February, 2022. (Keyword) Animals / Atrophy / Humans / Muscle Fibers, Skeletal / Pentacyclic Triterpenes / Rats / Rotation (Tokushima University Institutional Repository) ● Metadata: 116937 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.69.127 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35466134 ● Search Scopus @ Elsevier (PMID): 35466134 ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.69.127 (Tokushima University Institutional Repository: 116937, DOI: 10.2152/jmi.69.127, PubMed: 35466134)
6.	Madoka Kohno, ANAYT ULLA, Rina Taniguchi, Akane Ohishi, Kako Hirayama, Yuma Takemura, Shoichiro Takao, Yuki Kanazawa, Yuki Matsumoto, Masafumi Harada, Tomoya Fukawa, Hiro-omi Kanayama, Takayuki Uchida, Toshio Suzuki and Takeshi Nikawa : Daily Dietary Supplementation with Steamed Soybean Improves Muscle Volume and Strength in Healthy People Lacking Exercise., Journal of Nutritional Science and Vitaminology, Vol.68, No.6, 521-526, 2022. (Summary) Various dietary protein supplements are used by the elderly and bedridden to maintain their skeletal muscle mass and functions. High-quality proteins act as an anabolic driver and help to improve muscle strength and performance. Previously, we reported that soy protein significantly attenuates denervation-induced loss of muscle mass and myofiber cross sectional area in mice with inhibition of ubiquitination and degradation of IRS-1 in tibialis anterior muscle. It also increased muscle volume and strength in bedridden patients. In the present study, we investigated the effects of dietary soybean supplementation on muscle functions in taxi drivers lacking vigorous physical exercise. We conducted a case-control study on 25 healthy, male taxi drivers between the ages of 36 and 71 y performing minimal physical exercise. They were divided into two dietary groups: the soybean diet group (n=13) who ate daily meals (dinner) supplemented with 50 g of steamed soybean for 30 d and the control diet group (n=12) who received no soybean supplement. Next, we measured the muscle cross-sectional area (CSA) and muscle strength and function in both the groups before and after 30 d of soybean intake. The body weights of both diet groups did not differ significantly over time. However, after 30 d of soybean supplementation, the soybean-fed group developed significantly higher muscle CSA and grip strength compared to the control groups. In conclusion, dietary soybean supplementation improved muscle function in taxi drivers who lacked exercise. (Keyword) Male / Animals / Mice / Soybeans / Case-Control Studies / Muscle, Skeletal / Dietary Supplements / Muscle Strength / Dietary Proteins (Link to Publication Site) ● Publication site (DOI): 10.3177/jnsv.68.521 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36596550 ● Search Scopus @ Elsevier (PMID): 36596550 ● Search Scopus @ Elsevier (DOI): 10.3177/jnsv.68.521 (DOI: 10.3177/jnsv.68.521, PubMed: 36596550)
7.	Taku Fukushima, Miho Takata, Ayano Kato, Takayuki Uchida, Takeshi Nikawa and Iori Sakakibara : Transcriptome Analyses of In Vitro Exercise Models by Clenbuterol Supplementation or Electrical Pulse Stimulation, Applied Sciences, Vol.11, No.21, 10436, 2021. (Tokushima University Institutional Repository) ● Metadata: 117280 (Link to Publication Site) ● Publication site (DOI): 10.3390/app112110436 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.3390/app112110436 (Tokushima University Institutional Repository: 117280, DOI: 10.3390/app112110436)
8.	Reiko Nakao, Shen Weilin, Shimajiri Yasuka, Kainou Kumiko, Sato Yuki, Ulla Anayt, Kohta Ohnishi, Ninomiya Miyuki, Ohno Ayako, Takayuki Uchida, Tanaka Mitsuru, Akama Kazuhito, Matsui Toshiro and Takeshi Nikawa : Oral intake of rice overexpressing ubiquitin ligase inhibitory pentapeptide prevents atrophy in denervated skeletal muscle, NPJ Science of Food, Vol.5, No.1, 25, 2021. (Summary) We previously reported that intramuscular injections of ubiquitin ligase CBLB inhibitory pentapeptide (Cblin; Asp-Gly-pTyr-Met-Pro) restored lost muscle mass caused by sciatic denervation. Here, we detected Cblin on the basolateral side of Caco-2 cells after being placed on the apical side, and found that cytochalasin D, a tight junction opener, enhanced Cblin transport. Orally administered Cblin was found in rat plasma, indicating that intact Cblin was absorbed in vitro and in vivo. Furthermore, transgenic Cblin peptide-enriched rice (CbR) prevented the denervation-induced loss of muscle mass and the upregulation of muscle atrophy-related ubiquitin ligases in mice. These findings indicated that CbR could serve as an alternative treatment for muscle atrophy. (Tokushima University Institutional Repository) ● Metadata: 117588 (Link to Publication Site) ● Publication site (DOI): 10.1038/s41538-021-00108-0 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34504092 ● Search Scopus @ Elsevier (PMID): 34504092 ● Search Scopus @ Elsevier (DOI): 10.1038/s41538-021-00108-0 (Tokushima University Institutional Repository: 117588, DOI: 10.1038/s41538-021-00108-0, PubMed: 34504092)
9.	Kosuke Sugiura, Katsuya Hirasaka, Tasuku Maeda, Takayuki Uchida, Koji Kishimoto, Motoko Oarada, Siegfried Labeit, Anayt Ulla, Iori Sakakibara, Reiko Nakao, Koichi Sairyo and Takeshi Nikawa : MuRF1 deficiency prevents age-related fat weight gain, possibly through accumulation of PDK4 in skeletal muscle mitochondria in older mice, Journal of Orthopaedic Research, Vol.40, No.5, 1026-1038, 2021. (Tokushima University Institutional Repository) ● Metadata: 116581 (Link to Publication Site) ● Publication site (DOI): 10.1002/jor.25131 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34185335 ● Summary page in Scopus @ Elsevier: 2-s2.0-85109422486 (Tokushima University Institutional Repository: 116581, DOI: 10.1002/jor.25131, PubMed: 34185335, Elsevier: Scopus)
10.	Ulla Anayt, Takayuki Uchida, Miki Yukari, Kosuke Sugiura, Higashitani Atsushi, Kobayashi Takeshi, Ohno Ayako, Reiko Nakao, Katsuya Hirasaka, Iori Sakakibara and Takeshi Nikawa : Morin attenuates dexamethasone-mediated oxidative stress and atrophy in mouse C2C12 skeletal myotubes, Archives of Biochemistry and Biophysics, Vol.704, 108873, 2021. (Summary) Glucocorticoids are the drugs most commonly used to manage inflammatory diseases. However, they are prone to inducing muscle atrophy by increasing muscle proteolysis and decreasing protein synthesis. Various studies have demonstrated that antioxidants can mitigate glucocorticoid-induced skeletal muscle atrophy. Here, we investigated the effect of a potent antioxidative natural flavonoid, morin, on the muscle atrophy and oxidative stress induced by dexamethasone (Dex) using mouse C2C12 skeletal myotubes. Dex (10 μM) enhanced the production of reactive oxygen species (ROS) in C2C12 myotubes via glucocorticoid receptor. Moreover, Dex administration reduced the diameter and expression levels of the myosin heavy chain protein in C2C12 myotubes, together with the upregulation of muscle atrophy-associated ubiquitin ligases, such as muscle atrophy F-box protein 1/atrogin-1, muscle ring finger protein-1, and casitas B-lineage lymphoma proto-oncogene-b. Dex also significantly decreased phosphorylated Foxo3a and increased total Foxo3a expression. Interestingly, Dex-induced ROS accumulation and Foxo3a expression were inhibited by morin (10 μM) pretreatment. Morin also prevented the Dex-induced reduction of myotube thickness, together with muscle protein degradation and suppression of the upregulation of atrophy-associated ubiquitin ligases. In conclusion, our results suggest that morin effectively prevents glucocorticoid-induced muscle atrophy by reducing oxidative stress. (Keyword) Animals / Cell Line / Dexamethasone / Dose-Response Relationship, Drug / Flavonoids / Mice / Muscle Fibers, Skeletal / Muscle Proteins / Muscular Atrophy / Oxidative Stress (Tokushima University Institutional Repository) ● Metadata: 116344 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.abb.2021.108873 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33848514 ● Search Scopus @ Elsevier (PMID): 33848514 ● Search Scopus @ Elsevier (DOI): 10.1016/j.abb.2021.108873 (Tokushima University Institutional Repository: 116344, DOI: 10.1016/j.abb.2021.108873, PubMed: 33848514)
11.	Sun Luchuanyang, Miyaji Nobuyuki, Yang Min, Mills M Edward, Taniyama Shigeto, Takayuki Uchida, Takeshi Nikawa, Li Jifeng, Shi Jie, Tachibana Katsuyasu and Katsuya Hirasaka : Astaxanthin Prevents Atrophy in Slow Muscle Fibers by Inhibiting Mitochondrial Reactive Oxygen Species via a Mitochondria-Mediated Apoptosis Pathway, Nutrients, Vol.13, No.379, 2021. (Summary) Astaxanthin (AX) is a carotenoid that exerts potent antioxidant activity and acts in the lipid bilayer. This study aimed to investigate the effects of AX on muscle-atrophy-mediated disturbance of mitochondria, which have a lipid bilayer. Tail suspension was used to establish a muscle-atrophied mouse model. AX diet fed to tail-suspension mice prevented loss of muscle weight, inhibited the decrease of myofiber size, and restrained the increase of hydrogen peroxide (HO) production in the soleus muscle. Additionally, AX improved downregulation of mitochondrial respiratory chain complexes I and III in the soleus muscle after tail suspension. Meanwhile, AX promoted mitochondrial biogenesis by upregulating the expressions of , , in the soleus muscle of tail-suspension mice. To confirm the AX phenotype in the soleus muscle, we examined its effects on mitochondria using Sol8 myotubes derived from the soleus muscle. We found that AX was preferentially detected in the mitochondrial fraction; it significantly suppressed mitochondrial reactive oxygen species (ROS) production in Sol8 myotubes. Moreover, AX inhibited the activation of caspase 3 via inhibiting the release of cytochrome c into the cytosol in antimycin A-treated Sol8 myotubes. These results suggested that AX protected the functional stability of mitochondria, alleviated mitochondrial oxidative stress and mitochondria-mediated apoptosis, and thus, prevented muscle atrophy. (Keyword) astaxanthin / mitochondria / muscle atrophy / oxidative stress (Tokushima University Institutional Repository) ● Metadata: 116285 (Link to Publication Site) ● Publication site (DOI): 10.3390/nu13020379 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33530505 ● Summary page in Scopus @ Elsevier: 2-s2.0-85099928726 (Tokushima University Institutional Repository: 116285, DOI: 10.3390/nu13020379, PubMed: 33530505, Elsevier: Scopus)
12.	Ohno Ayako, Nobuo Maita, Tabata Takanori, Nagano Hikaru, Arita Kyohei, Ariyoshi Mariko, Takayuki Uchida, Reiko Nakao, Ulla Anayt, Kosuke Sugiura, Koji Kishimoto, Teshima-Kondo Shigetada, Okumura Yuushi and Takeshi Nikawa : Crystal structure of inhibitor-bound human MSPL that can activate high pathogenic avian influenza., Life Science Alliance, Vol.4, No.6, e202000849, 2021. (Summary) Infection of certain influenza viruses is triggered when its HA is cleaved by host cell proteases such as proprotein convertases and type II transmembrane serine proteases (TTSP). HA with a monobasic motif is cleaved by trypsin-like proteases, including TMPRSS2 and HAT, whereas the multibasic motif found in high pathogenicity avian influenza HA is cleaved by furin, PC5/6, or MSPL. MSPL belongs to the TMPRSS family and preferentially cleaves [R/K]-K-K-R sequences. Here, we solved the crystal structure of the extracellular region of human MSPL in complex with an irreversible substrate-analog inhibitor. The structure revealed three domains clustered around the C-terminal α-helix of the SPD. The inhibitor structure and its putative model show that the P1-Arg inserts into the S1 pocket, whereas the P2-Lys and P4-Arg interacts with the Asp/Glu-rich 99-loop that is unique to MSPL. Based on the structure of MSPL, we also constructed a homology model of TMPRSS2, which is essential for the activation of the SARS-CoV-2 spike protein and infection. The model may provide the structural insight for the drug development for COVID-19. (Keyword) Animals / Birds / Crystallography, X-Ray / Humans / Influenza in Birds / Membrane Proteins / Orthomyxoviridae / Protein Conformation / Serine Endopeptidases (Tokushima University Institutional Repository) ● Metadata: 116821 (Link to Publication Site) ● Publication site (DOI): 10.26508/LSA.202000849 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33820827 ● Summary page in Scopus @ Elsevier: 2-s2.0-85103997820 (Tokushima University Institutional Repository: 116821, DOI: 10.26508/LSA.202000849, PubMed: 33820827, Elsevier: Scopus)
13.	Yuki Niida, Masashi Masuda, Yuichiro Adachi, Aika Yoshizawa, Hirokazu Ohminami, Yuki Mori, Kohta Ohnishi, Hisami Okumura, Takayuki Uchida, Takeshi Nikawa, Hironori Yamamoto, Makoto Miyazaki and Yutaka Taketani : Reduction of stearoyl-CoA desaturase (SCD) contributes muscle atrophy through the excess endoplasmic reticulum stress in chronic kidney disease, Journal of Clinical Biochemistry and Nutrition, Vol.67, No.2, 179-187, 2020. (Summary) <p>Skeletal muscle atrophy is associated with mortality and poor prognosis in patients with chronic kidney disease (CKD). However, underlying mechanism by which CKD causes muscle atrophy has not been completely understood. The quality of lipids (lipoquality), which is defined as the functional features of diverse lipid species, has recently been recognized as the pathology of various diseases. In this study, we investigated the roles of the stearoyl-CoA desaturase (SCD), which catalyzes the conversion of saturated fatty acids into monounsaturated fatty acids, in skeletal muscle on muscle atrophy in CKD model animals. In comparison to control rats, CKD rats decreased the SCD activity and its gene expression in atrophic gastrocnemius muscle. Next, oleic acid blocked the reduction of the thickness of C2C12 myotubes and the increase of the endoplasmic reticulum stress induced by SCD inhibitor. Furthermore, endoplasmic reticulum stress inhibitor ameliorated CKD-induced muscle atrophy (the weakness of grip strength and the decrease of muscle fiber size of gastrocnemius muscle) in mice and the reduction of the thickness of C2C12 myotubes by SCD inhibitor. These results suggest that the repression of SCD activity causes muscle atrophy through excessive endoplasmic reticulum stress in CKD.</p> (Keyword) skeletal muscle atrophy / endoplasmic reticulum stress / chronic kidney disease / stearoyl-CoA desaturase / saturated fatty acid (Tokushima University Institutional Repository) ● Metadata: 114720 (Link to Publication Site) ● Publication site (DOI): 10.3164/jcbn.20-24 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33041516 ● CiNii @ National Institute of Informatics (CRID): 1390566775163696384 ● Search Scopus @ Elsevier (PMID): 33041516 ● Search Scopus @ Elsevier (DOI): 10.3164/jcbn.20-24 (Tokushima University Institutional Repository: 114720, DOI: 10.3164/jcbn.20-24, PubMed: 33041516, CiNii: 1390566775163696384)
14.	Tomohiro Yoshimura, Kanae Saitoh, Luchuanyang Sun, Yao Wang, Shigeto Taniyama, Kenichi Yamaguchi, Takayuki Uchida, Tsutomu Ohkubo, Atsushi Higashitani, Takeshi Nikawa, Katsuyasu Tachibana and Katsuya Hirasaka : Morin suppresses cachexia-induced muscle wasting by binding to ribosomal protein S10 in carcinoma cells., Biochemical and Biophysical Research Communications, Vol.506, No.4, 773-779, 2018. (Summary) Cachexia, observed in most cancer patients, is a syndrome that includes wasting of bodily energy reserves and is characterized by muscle atrophy and fat loss. We have previously demonstrated that isoflavones, such as genistein and daidzein, prevent muscle wasting in tumor-bearing mice. In this study, we examined the effect of morin, a flavonoid, on cachexia. The wet weight and myofiber size of muscles in Lewis lung carcinoma (LLC) cell-bearing mice fed a normal diet were decreased, compared with those in control mice fed a normal diet. In contrast, intake of morin prevented the reduction of muscle wet weight and myofiber size. Moreover, the tumor weight in mice fed the morin diet was lower than that in mice fed the normal diet. Both cell viability and protein synthetic ability of LLC cells were reduced by treatment with morin, but C2C12 myotubes were not affected. Binding assay using morin-conjugated magnetic beads identified ribosomal protein S10 (RPS10) as a target protein of morin. Consistent with the result of morin treatment, knockdown of RPS10 suppressed LLC cell viability. These results suggest that morin indirectly prevents muscle wasting induced by cancer cachexia by suppressing cancer growth via binding to RPS10. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2018.10.184 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30389140 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056802520 (DOI: 10.1016/j.bbrc.2018.10.184, PubMed: 30389140, Elsevier: Scopus)
15.	Chisato Tomida, Naoko Yakagishi, Hikaru Nagano, Takayuki Uchida, Ayako Maita, Katsuya Hirasaka, Takeshi Nikawa and Shigetada Kondo : VEGF pathway-targeting drugs induce evasive adaptation by activation of neuropilin-1/cMet in colon cancer cells., International Journal of Oncology, Vol.52, No.4, 1350-1362, 2018. (Summary) Anti-angiogenic therapies targeting vascular endothelial growth factor (VEGF) and its receptor (VEGF-R) are important treatments for a number of human malignancies, including colorectal cancers. However, there is increasing evidence that VEGF/VEGF-R inhibitors promote the adaptive and evasive resistance of tumor cells to the therapies. The mechanism by which the cancer cells become resistant remains unclear. One potential mechanism is that VEGF/VEGF-R blockers directly act on tumor cells independently of anti-angiogenic effects. In this study, the direct effects of an anti-VEGF antibody (bevacizumab) and a VEGF-R tyrosine kinase inhibitor (sunitinib) on the evasive adaptation of colon cancer cells were compared. HCT116 and RKO human colon cancer cell lines were chronically exposed (3 months) to bevacizumab or sunitinib in vitro to establish bevacizumab- and sunitinib-adapted cells, respectively. Transwell migration and invasion assays, western blotting, reverse transcription-quantitative polymerase chain reaction, co-immunoprecipitation analysis, cell survival assays and ELISAs were conducted to analyze the adapted cells. Compared with the control vehicle-treated cells, the two cell models exhibited increased migration and invasion activities to different degrees and through different mechanisms. The bevacizumab-adapted cells, but not in the sunitinib-adapted cells, exhibited redundantly increased expression levels of VEGF/VEGF-R family members, including VEGF-A, placental growth factor, VEGF-C, VEGF-R1 and VEGF-R3. In addition, the phosphorylation levels of VEGF-R1 and VEGF-R3 were increased in the bevacizumab-adapted cells compared with the control cells. Thus, the inhibition of VEGF-R1 and VEGF-R3 decreased the evasive activities of the cells, suggesting that they remained dependent on redundant VEGF/VEGF-R signaling. By contrast, the sunitinib-adapted cells exhibited increased neuropilin-1 (NRP1) expression levels compared with the control cells. In the sunitinib-adapted cells, NRP1 interacted with phosphorylated cMet, and the cMet activation was dependent on NRP1. Thus, NRP1 or cMet blockade suppressed the evasive activation of the sunitinib-adapted cells. These results suggest that the sunitinib-adapted cells switched from a VEGF-R-dependent pathway to an alternative NRP1/cMet-dependent one. The findings of the present study indicate that VEGF/VEGF-R inhibitors directly act on colon cancer cells and activate their evasive adaptation via different mechanisms. (Tokushima University Institutional Repository) ● Metadata: 111606 (Link to Publication Site) ● Publication site (DOI): 10.3892/ijo.2018.4291 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29532881 ● Summary page in Scopus @ Elsevier: 2-s2.0-85042801496 (Tokushima University Institutional Repository: 111606, DOI: 10.3892/ijo.2018.4291, PubMed: 29532881, Elsevier: Scopus)
16.	Takayuki Uchida, Yoshihiro Sakashita, Kanako Kitahata, Yui Yamashita, Chisato Tomida, Yuki Kimori, Akio Komatsu, Katsuya Hirasaka, Ayako Maita, Reiko Nakao, Atsushi Higashitani, Akira Higashibata, Noriaki Ishioka, Toru Shimazu, Takeshi Kobayashi, Yuushi Okumura, Inho Choi, Motoko Oarada, M Edward Mills, Shigetada Kondo, Shin'ichi Takeda, Eiji Tanaka, Keiji Tanaka, Masahiro Sokabe and Takeshi Nikawa : Reactive oxygen species up-regulate expression of muscle atrophy-associated ubiquitin ligase Cbl-b in rat L6 skeletal muscle cells., American Journal of Physiology, Cell Physiology, Vol.314, No.6, C721-C731, 2018. (Summary) Unloading-mediated muscle atrophy is associated with increased reactive oxygen species (ROS) production. We previously demonstrated that elevated ubiquitin ligase casitas B-lineage lymphoma-b (Cbl-b) resulted in the loss of muscle volume [Nakao R. et al. Mol Cell Biol, 29: 4798-4811, 2009]. However, the pathological role of ROS production associated with unloading-mediated muscle atrophy still remains unknown. Here, we showed the ROS-mediated signal transduction caused by microgravity or its simulation contributes to Cbl-b expression. In L6 myotubes, the assessment of redox status revealed that oxidized glutathione was increased under microgravity conditions, and simulated microgravity caused a burst of ROS, implicating ROS as a critical upstream mediator linking to downstream atrophic signaling. ROS generation activated the ERK1/2-early growth response protein (Egr) 1/2-Cbl-b signaling pathway, an established contributing pathway to muscle volume loss. Interestingly, antioxidant treatment, such as N-acetylcysteine and TEMPOL, but not catalase, blocked the clinorotation-mediated activation of ERK1/2. The increased ROS induced transcriptional activity of Egr 1 and/or Egr 2 to stimulate Cbl-b expression through the ERK 1/2 pathway in L6 myoblasts, since treatment with Egr 1/2 siRNA and an ERK 1/2 inhibitor significantly suppressed clinorotation-induced Cbl-b and Egr expression, respectively. Promoter and gel mobility shift assays revealed that Cbl-b was upregulated via an Egr consensus oxidative responsive element at -110 to -60 bp of the Cbl-b promoter. Together this indicates that under microgravity conditions, elevated ROS may be a crucial mechanotransducer in skeletal muscle cells, regulating muscle mass, through Cbl-b expression activated by the ERK-Egr signaling pathway. (Tokushima University Institutional Repository) ● Metadata: 111610 (Link to Publication Site) ● Publication site (DOI): 10.1152/ajpcell.00184.2017 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29513566 ● Search Scopus @ Elsevier (PMID): 29513566 ● Search Scopus @ Elsevier (DOI): 10.1152/ajpcell.00184.2017 (Tokushima University Institutional Repository: 111610, DOI: 10.1152/ajpcell.00184.2017, PubMed: 29513566)
17.	Manami Abe, Yuki Matsuo, Akiko Harada, Takayuki Uchida, Kanako Kitahata, Chisato Tomida, Katsuya Hirasaka, Shigetada Kondo, Nagakatsu Harada, Yutaka Nakaya, Hiroshi Sakaue, Reiko Nakao and Takeshi Nikawa : Distinct Gene Expression Profile Distinguishes Increased Metabolic Activity in Spontaneously Hyperactive Rats While Sedentary from That Induced by Exercise, Advances in Biological Chemistry, Vol.8, No.01, 1-14, 2018. (Tokushima University Institutional Repository) ● Metadata: 111609 (Link to Publication Site) ● Publication site (DOI): 10.4236/abc.2018.81001 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.4236/abc.2018.81001 (Tokushima University Institutional Repository: 111609, DOI: 10.4236/abc.2018.81001)
18.	Chisato Tomida, Hikaru Nagano, Naoko Yamagishi, Takayuki Uchida, Ayako Maita, Katsuya Hirasaka, Takeshi Nikawa and Shigetada Kondo : Regorafenib induces adaptive resistance of colorectal cancer cells via inhibition of vascular endothelial growth factor receptor., The Journal of Medical Investigation : JMI, Vol.64, No.3-4, 262-265, 2017. (Summary) Recently, inhibition of tumor angiogenesis has become an important anti-cancer therapy. Tumor angiogenesis is regulated by multiple signaling pathways, including VEGF and VEGF receptor (VEGF-R), FGF and FGF receptor (FGF-R), and PDGF and PDGF receptor (PDGF-R) pathways. Thus, the antiangiogenic agents, such as regorafenib, simultaneously target those receptors on vascular endothelial cells. In addition to endothelial cells, cancer cells express the three receptors, suggesting that the antiangiogenic inhibitors affect tumor cells. In fact, we previously demonstrated that regorafenib directly acted on human colorectal cancer cells and accelerated their apoptosis resistance and migration capability. Thus, we here elucidated how regorafenib induced the malignant phenotypes in colorectal cancer cells. To identify the responsible receptor among the regorafenib-targeting proangiogenic receptors, we examined the effects of a potent selective inhibitor for VEGF-R, FGF-R or PDGF-R on apoptosis resistance and migration capability. We clarified that blockade of VEGF-R, but not FGF-R and PDGF-R, induced the malignant phenotypes. We confirmed that blocking of VEGF ligands derived from colorectal cancer cells also induced the phenotypes. These results suggest that regorafenib progressed the malignancy via prevention of autocrine and paracrine VEGF signaling in colorectal cancer cells. J. Med. Invest. 64: 262-265, August, 2017. (Keyword) Angiogenesis Inhibitors / Apoptosis / Cell Movement / Colorectal Neoplasms / Drug Resistance, Neoplasm / HCT116 Cells / Humans / Phenylurea Compounds / Protein-Tyrosine Kinases / Pyridines / Receptors, Vascular Endothelial Growth Factor (Tokushima University Institutional Repository) ● Metadata: 111128 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.64.262 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28954993 ● CiNii @ National Institute of Informatics (CRID): 1390282679224220288 ● Summary page in Scopus @ Elsevier: 2-s2.0-85030250811 (Tokushima University Institutional Repository: 111128, DOI: 10.2152/jmi.64.262, PubMed: 28954993, CiNii: 1390282679224220288, Elsevier: Scopus)
19.	Chisato Tomida, Naoko Yamagishi, Hikaru Nagano, Takayuki Uchida, Ayako Maita, Katsuya Hirasaka, Takeshi Nikawa and Shigetada Kondo : Antiangiogenic agent sunitinib induces epithelial to mesenchymal transition and accelerates motility of colorectal cancer cells., The Journal of Medical Investigation : JMI, Vol.64, No.3-4, 250-254, 2017. (Summary) Although vascular endothelial growth factor receptor (VEGF-R)-targeted antiangiogenic agents are important treatment for a number of human malignancies, there is accumulating evidence that the therapies may promote disease progression, such as invasion and metastasis. How tumors become to promote their evasiveness remains fully uncertain. One of possible mechanisms for the adaptation may be a direct effect of VEGF-R inhibitors on tumor cells expressing VEGF-R. To elucidate a direct effect of VEGF-R-targeting drug (sunitinib), we established a human colorectal cancer cell model adapted to sunitinib. The sunitinib-conditioned cells showed a significant increase in cellular motility and migration activities, compared to the vehicle-treated control cells. Consistent with the phenotype, the sunitinib-conditioned cells decreased the expression levels of E-cadherin (an epithelial marker), while significantly increased the levels of Slug and Zeb1 (mesenchymal markers). Expression profiles of VEGF-R in the sunitinib-conditioned cells showed that only neuropilin-1 (NRP1) expression was significantly increased among all VEGF-R tested. Blockade of NRP1 using its antagonist clearly repressed the migration activation in sunitinib-conditioned cells, but not in the control cells. These results suggest that inhibition of VEGF-R on colorectal cancer cells can drive the epithelial-mesenchymal transition, leading to activation of cell motility in an NRP1-dependent manner. J. Med. Invest. 64: 250-254, August, 2017. (Keyword) Angiogenesis Inhibitors / Cell Movement / Colorectal Neoplasms / Epithelial-Mesenchymal Transition / HCT116 Cells / Humans / Indoles / Neuropilin-1 / Pyrroles / Receptors, Vascular Endothelial Growth Factor / Transcriptome (Tokushima University Institutional Repository) ● Metadata: 111126 (Link to Publication Site) ● Publication site (DOI): 10.2152/jmi.64.250 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28954991 ● CiNii @ National Institute of Informatics (CRID): 1390001204247522048 ● Summary page in Scopus @ Elsevier: 2-s2.0-85030217718 (Tokushima University Institutional Repository: 111126, DOI: 10.2152/jmi.64.250, PubMed: 28954991, CiNii: 1390001204247522048, Elsevier: Scopus)

Review, Commentary:

1.	Takayuki Uchida, Ayako Maita and Takeshi Nikawa : 微小重力環境を利用した筋萎縮機構の研究, 実験医学増刊号, Vol.38, No.7, 82-87, Apr. 2020.
2.	Takayuki Uchida, Takeshi Nikawa and Reiko Nakao : Mitochondria-mediated mechanosensing mechanism in skeletal muscle, Science of the Living Body, Vol.70, No.4, 301-305, May 2019. (Keyword) ミトコンドリア / 筋肉 / IGF-1 / メカノセンシング (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1521980704885620096 (CiNii: 1521980704885620096)
3.	Takayuki Uchida and Takeshi Nikawa : 微小重力環境における筋萎縮発生メカニズムへの新展開, 月刊細胞, Vol.50, No.12, 618-621, Oct. 2018.
4.	Reiko Nakao, Takayuki Uchida and Takeshi Nikawa : サルコペニアとメカニカルストレス, 診断と治療, Vol.106, No.6, 701-704, Jun. 2018. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520573329924547328 (CiNii: 1520573329924547328)
5.	Yoshihiro Sakashita, Takayuki Uchida and Takeshi Nikawa : [Impacts of physical exercise on remodeling and hypertrophy of skeletal muscle.], Clinical Calcium, Vol.27, No.1, 79-85, 2017. (Summary) The skeletal muscle has high sensitivity for the mechanical stress. Because it is enlarged by training, whereas it is easily withered by lack of exercise. When we exercise, skeletal muscle cells per se sense mechanical loading, and muscular remodeling and the muscular hypertrophy occur. It has been revealed that the intracellular signaling through PGC-1 participates in the remodeling of the skeletal muscle, while PGC-14, an isoform of PGC-1, and the dystrophin-glycoprotein complex play important roles in muscular hypertrophy. This review describes the impact of physical exercise gives on the remodeling and hypertrophy of muscle through the signaling. (Keyword) Animals / Exercise / Humans / Hypertrophy / Insulin-Like Growth Factor I / Muscle, Skeletal / Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha / signal transduction (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28017949 ● Search Scopus @ Elsevier (PMID): 28017949 (PubMed: 28017949)
6.	Hikaru Kishimoto, Takayuki Uchida, Kanako Kitahata and Takeshi Nikawa : [Plasticity of skeletal muscle against unloading stress.], Clinical Calcium, Vol.27, No.3, 351-356, 2017. (Summary) Recently, muscle atrophy caused by unloading, such as spaceflight and bed rest has been becoming a social problem in Japan. However, the effective countermeasures against these disuse atrophy have not been developed. We have reviewed the mechanisms of disuse atrophy and its possible countermeasures. (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28232649 ● Search Scopus @ Elsevier (PMID): 28232649 (PubMed: 28232649)

Proceeding of International Conference:

1.	Takayuki Uchida, Miki Yukari, Katsuya Hirasaka, Sato Takahiko, Teranishi Mika, Ishihara Naotada, Kobayashi Takeshi, Higashitani Atsushi, Sokabe Masahiro and Takeshi Nikawa : The elucidation of mechanism by MFN2-mediated induction of disuse muscle atrophy, International Symposium on Mechanobiology for Human Health:8 years progress in The AMED-CREST/PRIME project on mechanobiplogy, Mar. 2023.
2.	Takeshi Nikawa, Takata Miho, Kosuke Sugiura, Takayuki Uchida, Iori Sakakibara, Madoka Uezumi and Akiyoshi Uezumi : Functional analysis of Aconitase2 in fetal skeletal muscle, International Symposium on Mechanobiology for Human Health:8 years progress in The AMED-CREST/PRIME project on mechanobiplogy, Mar. 2023.
3.	(名) Anaytulla, Takayuki Uchida, Miki Yukari, Sugiura Kohsuke, Ohno Ayako, Reiko Nakao and Takeshi Nikawa : Supplementation of Morin attenuates oxidative stress and muscle wasting in mouse C2C12 skeletal myotubes treated with dexamethasone, The 7th International Conference on Food Factors(ICoFF2019)/The 12th International Conference and Exhibition on Nutraceuticals and Functional Foods (ISNFF2019), Kobe, Dec. 2019.
4.	Takayuki Uchida, Sakashita Yoshihiro, Katsuya Hirasaka, Ohno Ayako, Reiko Nakao, Akira Higashibata, Kobayashi Takeshi, Sokabe Masahiro and Takeshi Nikawa : The influence of skeletal muscle thermogenesis on the regulation of body temperature during ketogenic diet-induced hypothermia, ADVANCED BIOMEDICAL ENGINEERING AND INSTRUMENTATION SUMMIT, San Francisco, Jun. 2019.
5.	Takeshi Nikawa, Takayuki Uchida, Ayako Maita and Reiko Nakao : Molecular mechanism and nutritional approach for unloading-mediated muscle atrophy, 2018 International Conference on Functional Food for improving Sarcopenia, Cachexia and Frailty, Mar. 2018.
6.	Takeshi Nikawa, Hashimoto Rie, Katsuya Hirasaka, Yano Chiaki, Aibara Kana, Takayuki Uchida, Tomoki Abe, Ayako Maita and Akama Kazuhito : Effects of dietary soy protein on unloading mediated muscle atrophy, 11th Asian Microgravity Symposium, Oct. 2016.
7.	Takayuki Uchida, Tomoki Abe, Ayako Maita, Reiko Nakao, Higashitani Atsushi, Kobayashi Takeshi, Sokabe Masahiro, Akira Higashibata and Takeshi Nikawa : Microgravity-induced signal transduction in skeletal muscle cells, 11th Asian Microgravity Symposium, Oct. 2016.

Proceeding of Domestic Conference:

1.	Chinami Itoh, MINORI Suzuki, HIROKI Matsuki, ANAYT ULLA, Takayuki Uchida, 中森俊宏, 松井利郎 and Takeshi Nikawa : 大豆タンパク質の抗筋萎縮活性, 第56回日本栄養・食糧学会中国・四国支部大会, Oct. 2023.
2.	Haruka Tsuda, Kanako Kitahata, Takayuki Uchida, 橋爪藤子, Akira Higashibata, Junsoo Park, Inho Choi and Takeshi Nikawa : 3D-clinorotation によるラットL6 筋管萎縮に対するC14-Cblin とセラストロールの同時投与による相加効果, 日本宇宙生物科学会第37回大会, Sep. 2023.
3.	ANAYT ULLA, Mizanur Md Rahman, Takayuki Uchida, Hiroyuki Kayaki, Yosuke Nishitani, Susumu Yoshino, Hiroshige Kuwahara and Takeshi Nikawa : 3-(4-hydroxy-3-methoxyphenyl) propionic acid attenuates dexamethasone-induced muscle atrophy by suppressing Atrogin-1 and MuRF-1, 日本食品科学工学会第70回記念大会, Aug. 2023.
4.	Chinami Itoh, HIROKI Matsuki, MINORI Suzuki, KONO Madoka, ANAYT ULLA, Takayuki Uchida, 石黒貴寛 and Takeshi Nikawa : 高野豆腐タンパク質の抗筋萎縮活性の解析, 第77回日本栄養・食糧学会大会, May 2023.
5.	Takayuki Uchida, ARAKAKI Tsubasa, Haruka Tsuda, TANIGUCHI Runa, 山本綾乃 and Takeshi Nikawa : 筋ミトコンドリアタンパク質Mitofusin2(Mfn2)による脂質代謝制御機構の解明, 第77回日本栄養・食糧学会大会, May 2023.
6.	Haruka Tsuda, Takayuki Uchida, Izumi Kawabata, ANAYT ULLA, TANIGUCHI Runa and Takeshi Nikawa : 筋肉へのピセアタンノール作用の検討, 第77回日本栄養・食糧学会大会, May 2023.
7.	Erika Yamano, Chinami Itoh, HIROKI Matsuki, KONO Madoka, ANAYT ULLA, Takayuki Uchida, Takashi Uebanso, Hitoshi Takagi and Takeshi Nikawa : セルロースナノファイバーの栄養学的機能性の検討, 第77回日本栄養・食糧学会大会, May 2023.
8.	Haruka Tsuda, Takayuki Uchida, Izumi Kawabata, (名) ANAYTULLA, TANIGUCHI Runa, 内田裕子, 森貞夫, 守田稔 and Takeshi Nikawa : C2C12 筋管細胞へのピセアタンノールの影響, 第55回日本栄養・食糧学会中国・四国支部大会, Oct. 2022.
9.	TANIGUCHI Runa, Kanako Kitahata, Takayuki Uchida, Ayano Katoh, KISHIDA Kohta, TANAKA Yukako, Junsoo Park, Choi Inho and Takeshi Nikawa : 3D-clinorotation によるラット L6 筋管萎縮に対する C14-Cblin とセラストロールの同時投与による相加効果, 第55回日本栄養・食糧学会中国・四国支部大会, Oct. 2022.
10.	KISHIDA Kohta, TAKATA Miho, Kosuke Sugiura, Takayuki Uchida, Iori Sakakibara, Madoka Uezumi, Akiyoshi Uezumi and Takeshi Nikawa : Aconitase2, 第55回日本栄養・食糧学会中国・四国支部大会, Oct. 2022.
11.	TAKATA Miho, KISHIDA Kohta, Kosuke Sugiura, Takayuki Uchida, 榊原伊織, Madoka Uezumi, Akiyoshi Uezumi and Takeshi Nikawa : 胎生期骨格筋における Aconitase2 の機能解析, 日本宇宙生物科学会第36回大会, Sep. 2022.
12.	TAKATA Miho, Iori Sakakibara, KISHIDA Kohta, FUKUSHIMA Taku, ARAKAKI Tsubasa, Takayuki Uchida, Tomoya Fukawa and Takeshi Nikawa : 骨格筋におけるAconitase2の機能解明, 第76回日本栄養・食糧学会大会, Jun. 2022.
13.	Minori Yamasaki, HIROKI Matsuki, NAKANO Wataru, Kosuke Sugiura, Tomoya Fukawa, Takayuki Uchida, Iori Sakakibara and Takeshi Nikawa : 廃用性筋萎縮におけるアコニターゼ活性の低下とその栄養学的保護, 第76回日本栄養・食糧学会大会, Jun. 2022.
14.	ARAKAKI Tsubasa, TANIGUCHI Runa, Erika Aoki, Ayaka Satoh, TAKATA Miho, Takayuki Uchida and Takeshi Nikawa : 高脂肪負荷食によるMfn2と骨格筋エネルギー代謝の関連解明, 第76回日本栄養・食糧学会大会, Jun. 2022.
15.	NAKANO Wataru, Kosuke Sugiura, Takayuki Uchida, Iori Sakakibara, Koichi Sairyo and Takeshi Nikawa : 廃用性萎縮筋におけるアコニターゼ活性とその保護, 第 54 回日本栄養•食糧学会中国•四国支部大会第7 回日本栄養改善学会四国支部学術総会合同大会, Oct. 2021.
16.	ADACHI Yuichiroh, Masashi Masuda, Iori Sakakibara, Takayuki Uchida, Hirokazu Ohminami, Hisami Okumura, Takeshi Nikawa and Yutaka Taketani : all trans レチノイン酸は小胞体ストレス応答関連因子 GADD34 の転写・転写後制御を介して筋繊維タイプ変化を引き起こす, 第 62 回日本生化学会中国・四国支部例会, Sep. 2021.
17.	KONO Madoka, Takayuki Uchida, Akane Ohishi, HIRAYAMA Kako, TAKEMURA Yuma, Shoichiro Takao, Yuki Kanazawa, Yuki Matsumoto, Masafumi Harada, Iori Sakakibara, 鈴木利雄 and Takeshi Nikawa : 蒸し大豆食品の継続摂取が運動不足の健常人の筋量や筋力に及ぼす影響, 第75回日本栄養・食糧学会大会, Jul. 2021.
18.	TANIGUCHI Runa, Izumi Kawabata, Takayuki Uchida, (名) ANAYTULLA, Iori Sakakibara and Takeshi Nikawa : パッションフルーツ種子由来成分ピセアタンノールはデキサメタゾン誘導性筋萎縮を抑制する, 第75回日本栄養・食糧学会大会, Jul. 2021.
19.	ADACHI Yuichiroh, Masashi Masuda, Iori Sakakibara, Takayuki Uchida, SASAKI Kohei, NOBE Yutaro, Hirokazu Ohminami, Kohta Ohnishi, Hisami Okumura, Hironori Yamamoto, Takeshi Nikawa and Yutaka Taketani : all trans レチノイン酸は小胞体ストレス応答関連因子 GADD34 の発現制御を介して筋繊維タイプ変化を誘導する, 第 75 回日本栄養・食糧学会大会, Jul. 2021.
20.	Iori Sakakibara, Kosuke Sugiura, Takayuki Uchida, Higashitani Atsushi, Kobayashi Takeshi, Sokabe Masahiro and Takeshi Nikawa : Mechano-signals regulate mitochondria-associated membrane, 第43回日本分子生物学会年会, Dec. 2020.
21.	Ayano Katoh, Takayuki Uchida, Iori Sakakibara, 池田泰隆, 濱田広一郎 and Takeshi Nikawa : 細胞内エネルギー代謝が筋細胞に与える影響, 第53回日本栄養食糧学会中国・四国支部大会, Oct. 2020.
22.	NAKANO Wataru, 三木裕可里, Kosuke Sugiura, Iori Sakakibara, Takayuki Uchida and Takeshi Nikawa : ミトコンドリア小胞体接触領域 (MAM) を介した筋量調節メカニズムの解明, 第53回日本栄養食糧学会中国・四国支部大会, Oct. 2020.
23.	Kosuke Sugiura, Takayuki Uchida, Koichi Sairyo and Takeshi Nikawa : (ROS)Mitochondrial Aconitase, 35, Oct. 2020.
24.	Koichi Sairyo, Kosuke Sugiura, Takayuki Uchida and Takeshi Nikawa : ミトコンドリア-小胞体接触領域(MAM)は廃用性筋委縮を制御する(一般演題基礎:筋・腱・滑膜 ), 第93回日本整形外科学会学術総会【WEB】, May 2020.
25.	Takayuki Uchida, Yukari Miki, Kosuke Sugiura, Ayako Maita, Reiko Nakao, 平坂勝也, 東谷篤志, 小林剛, 曽我部正博 and Takeshi Nikawa : 筋肉におけるミトコンドリアタンパク質Mfn2の役割, 第74回日本栄養・食糧学会大会, May 2020.
26.	Taiju Fujioka, Takayuki Uchida, Kosuke Sugiura, 小林剛, 東谷篤志, 曽我部正博 and Takeshi Nikawa : Unloadingによる筋萎縮におけるCa2+-ROSシグナルの変化, 第74回日本栄養・食糧学会大会, May 2020.
27.	Ayano Katoh, Takayuki Uchida, Kosuke Sugiura, 池田泰隆, 濱田広一郎 and Takeshi Nikawa : 細胞内エネルギー代謝経路が筋繊維タイプに与える影響, 第74回日本栄養・食糧学会大会, May 2020.
28.	Izumi Kawabata, Takayuki Uchida, Ayano Katoh, Ulla Anayt, 内田裕子, 森貞夫, 森田稔 and Takeshi Nikawa : ピセアタンノールの筋萎縮抑制効果の検討, 第74回日本栄養・食糧学会大会, May 2020.
29.	Yuuki Niida, Masashi Masuda, Aika Yoshizawa, Yuichiroh Adachi, Kohta Ohnishi, Hirokazu Ohminami, Takayuki Uchida, Hisami Okumura, Takeshi Nikawa, Hironori Yamamoto and Yutaka Taketani : 慢性腎臓病による骨格筋の脂肪酸代謝異常を介した脂肪毒性(Liptoxicity)は筋委縮(サルコペニア) を惹起する, 第23回日本病態栄養学会年次集会, Jan. 2020.
30.	Katsuya Hirasaka, M.Mills Edward, Takayuki Uchida, Ohno Ayako and Takeshi Nikawa : New aspect of mitochondrial uncoupling protein(UCP):Identification of UCP3 interacting proteins, 第42回日本分子生物学会年会, Dec. 2019.
31.	Izumi Kawabata, Takayuki Uchida, Ayano Katoh, (名) Anaytulla, 内田裕子, 森貞夫, 森田稔 and Takeshi Nikawa : ピセアタンノールの筋萎縮抑制効果の検討, 第52回日本栄養・食慮学会中国・四国支部大会, Oct. 2019.
32.	Yuuki Niida, Masashi Masuda, Aika Yoshizawa, Yuichiroh Adachi, Kohta Ohnishi, Hirokazu Ohminami, Takayuki Uchida, Hisami Okumura, Takeshi Nikawa, Hironori Yamamoto and Yutaka Taketani : 慢性腎臓病モデルラットの骨格筋における脂肪酸代謝異常が及ぼす筋萎縮への影響, 第66回日本栄養改善学会学術集会, Sep. 2019.
33.	Kohsuke Sugiura, Takayuki Uchida, Ayako Maita, Reiko Nakao, Katsuya Hirasaka, 東谷篤志, Akira Higashibata, 小林剛, 曽我部正博, Koichi Sairyo and Takeshi Nikawa : 廃用性筋萎縮におけるミトコンドリア形態変化及び酸化ストレス発生による影響, 日本筋学会第5回学術集会, Aug. 2019.
34.	Yuichiroh Adachi, Masashi Masuda, Yuuki Niida, Kohta Ohnishi, Takayuki Uchida, Hisami Okumura, Hironori Yamamoto, Takeshi Nikawa and Yutaka Taketani : レチノイン酸による小胞体ストレス感受性の影響, 日本ビタミン学会第71回大会, Jun. 2019.
35.	Yukari Miki, Akio Komatsu, Takayuki Uchida, Reiko Nakao, Ayako Maita, 曽我部正博 and Takeshi Nikawa : 廃用性筋萎縮進展におけるミトコンドリアタンパク質Mfn2の役割, 第73回日本栄養・食糧学会大会, May 2019.
36.	Takayuki Uchida, Yukari Miki, Yoshihiro Sakashita, 真板綾子, Reiko Nakao, Katsuya Hirasaka, 東谷篤志, Akira Higashibata, 小林剛, 曽我部正博 and Takeshi Nikawa : ミトコンドリアを介した無重力ストレス感知機構の解明, 第73回日本栄養・食糧学会大会, May 2019.
37.	Takayuki Uchida, Ayako Maita, Reiko Nakao and Takeshi Nikawa : 宇宙医学から健康長寿へ, 第221回徳島医学会学術集会, Feb. 2019. (Keyword) muscle atrophy / mitochondria
38.	Takeshi Nikawa, Takayuki Uchida, Reiko Nakao, Katsuya Hirasaka, Nobuo Maita, 東谷篤志, 小林剛, 石原直忠 and 曽我部正博 : Unloadingストレスに対する筋細胞の初期応答:酸化ストレスの重要性, 第41回日本分子生物学会年会, Nov. 2018.
39.	足立雄一郎, Masashi Masuda, 新井田裕樹, Kohta Ohnishi, Takayuki Uchida, Hisami Okumura, Takeshi Nikawa and Yutaka Taketani : 小胞体ストレス誘導下におけるレチノイン酸の影響, 第51回日本栄養・食糧学会中国・四国支部大会, Nov. 2018.
40.	Yukari Miki, Takayuki Uchida, Yuki Kimori, Yoshihiro Sakashita, Akio Komatsu, Ayako Maita, Reiko Nakao, Miyu Uchida, Taiju Fujioka, 小林剛, 東谷篤志, 石原直忠, 東端晃, 石岡憲昭, 武田伸一, 曽我部正博 and Takeshi Nikawa : ユビキチンリガーゼCbl-bは無重力ストレス誘導性の酸化ストレスにより増大する, 第51回日本栄養・食糧学会中国・四国支部大会, Nov. 2018.
41.	Yukari Miki, Takayuki Uchida, Yuki Kimori, Yoshihiro Sakashita, Akio Komatsu, Ayako Maita, Reiko Nakao, Miyu Uchida, Taiju Fujioka, 小林剛, 東谷篤志, 石原直忠, 東端晃, 石岡憲昭, 武田伸一, 曽我部正博 and Takeshi Nikawa : 酸化ストレスはラットL6細胞におけるユビキチンリガーゼCbl-bの発現を増大する, 日本宇宙生物科学会第32回大会, Sep. 2018.
42.	Akio Komatsu, Takayuki Uchida, Kanako Kitahata, Ayako Maita, Reiko Nakao, 瀬川圭 and Takeshi Nikawa : 廃用性筋萎縮を抑制するユビキチンリガーゼCbl-bの低分子阻害剤の開発, 日本筋学会第4回学術集会, Aug. 2018.
43.	Ayako Maita, Nobuo Maita, Yuushi Okumura, Takayuki Uchida, Reiko Nakao, Koji Kishimoto and Takeshi Nikawa : 高病原性インフルエンザ感染に関わる宿主酵素MSPLと阻害剤との複合体構造., 病態プロテアーゼ学会, Aug. 2018.
44.	Yuuki Niida, Masashi Masuda, Aika Yoshizawa, Yuichiroh Adachi, Takayuki Uchida, Kohta Ohnishi, Yoshichika Kawai, Takeshi Nikawa, Hironori Yamamoto and Yutaka Taketani : 慢性腎臓病に伴う骨格筋の飽和脂肪酸蓄積はオートファジー不全を介して筋萎縮を誘発する, 日本ビタミン学会第70回大会(高槻現代劇場), Jun. 2018.
45.	Miyuki Ninomiya, Yuki Kimori, Akio Komatsu, Ayaka Tetsuno, Yukari Miki, Kanako Kitahata, Takayuki Uchida, Ayako Maita, Reiko Nakao, 松井利郎, 赤間一仁 and Takeshi Nikawa : 廃用性筋萎縮を防ぐ高機能米の開発, 第72回日本栄養・食糧学会大会, May 2018.
46.	Risa Yoshida, Yuuki Niida, Yuichiroh Adachi, 酒井晶子, Hisami Okumura, Kohta Ohnishi, Takayuki Uchida, Yoshichika Kawai, Hironori Yamamoto, Takeshi Nikawa, Yutaka Taketani and Masashi Masuda : スルフォラファンのリポファジーを介した脂肪分解効果, 第72回日本栄養・食糧学会大会(岡山県立大学), May 2018.
47.	Yuki Kimori, Miyuki Ninomiya, Yukari Miki, Akio Komatsu, Ayaka Tetsuno, Takayuki Uchida, Reiko Nakao, Ayako Maita, 近藤茂忠, 曽我部正博 and Takeshi Nikawa : 無重力環境におけるミトコンドリアタンパク質Mitofusin2(Mfn2)の役割, 第72回日本栄養・食糧学会大会, May 2018.
48.	Takayuki Uchida, Yuki Kimori, Yoshihiro Sakashita, Ayako Maita, Reiko Nakao, 平坂勝也, 東谷篤志, 東端晃, 小林剛, 曽我部正博, 武田伸一 and Takeshi Nikawa : 無重力による廃用性筋萎縮における酸化ストレスの重要性, 第72回日本栄養・食糧学会大会, May 2018.
49.	Takayuki Uchida : 無重力による酸化ストレスを介した筋細胞内シグナルトランスダクション, Genes to Cells, Dec. 2017.
50.	Yukari Miki, Takayuki Uchida, Yuki Kimori, Yoshihiro Sakashita, Ayako Maita, Reiko Nakao, 小林剛, 東谷篤志, 石原直忠, 武田伸一, 曽我部正博 and Takeshi Nikawa : 無重力ストレスによる筋萎縮における酸化ストレスの重要性, 第50回日本栄養・食糧学会中国・四国支部大会, Nov. 2017.
51.	Takayuki Uchida : 無重力による酸化ストレスを介した筋細胞のシグナルトランスダクション, Biological Sciences in Space, Sep. 2017.
52.	Takayuki Uchida : 無重力ストレスによる筋萎縮における酸化ストレスの重要性, 第3回Neo VitamineD Workshop 学術集会, Aug. 2017.
53.	Takayuki Uchida, Ayako Maita, Reiko Nakao, 小林剛, 東谷篤志, 石原直忠, 武田伸一, 曽我部正博 and Takeshi Nikawa : 無重力ストレスによる筋萎縮における酸化ストレスの重要性, 日本筋学会第3回学術集会, Aug. 2017.
54.	Miyuki Ninomiya, Yuki Kimori, Marina Takagi, Kurumi Ida, Hikaru Kishimoto, Erika Takatsu, 石田祐子, 加藤健, Arisa Ochi, Takayuki Uchida, Ayako Maita, Tomoki Abe, Shigetada Kondo, Reiko Nakao, Katsuya Hirasaka and Takeshi Nikawa : 坐骨神経切除による筋萎縮におけるホエイペプチドと大豆タンパク質の阻害効果, 第71回日本栄養・食糧学会大会, May 2017.
55.	Takayuki Uchida, Yuki Kimori, Miyuki Ninomiya, Yoshihiro Sakashita, Tomoki Abe, Ayako Maita, Reiko Nakao, Katsuya Hirasaka, 東谷篤志, 小林剛, 曽我部正博, 武田伸一 and Takeshi Nikawa : 無重力による酸化ストレス産生を介した筋細胞内シグナル・トランスダクション, 第71回日本栄養・食糧学会大会, May 2017.
56.	Yuki Kimori, Miyuki Ninomiya, Chika Aihara, Yoshihiro Sakashita, Takayuki Uchida, Tomoki Abe, Reiko Nakao, Ayako Maita, Shigetada Kondo and Takeshi Nikawa : Mfn2ノックダウンの筋肉における影響の検討, 第71回日本栄養・食糧学会大会, May 2017.
57.	二宮みゆき, 髙木麻理奈, 井田くるみ, 岸本ひかる, 高津絵梨香, 石田祐子, 加藤健, 越智ありさ, Takayuki Uchida, Ayako Maita, Tomoki Abe, Shigetada Kondo, Reiko Nakao, Katsuya Hirasaka and Takeshi Nikawa : 坐骨神経切除による筋萎縮に対するホエイペプチドと大豆タンパク質の効果, 第49回日本栄養・食糧学会中国・四国支部大会, Nov. 2016.

Et cetera, Workshop:

1.	Takeshi Nikawa, Takayuki Uchida, Ayako Maita, Reiko Nakao, Katsuya Hirasaka, 小林剛, 曽我部正博, 東谷篤志 and 武田伸一 : 廃用性筋萎縮における酸化ストレスの重要性, 国立研究開発法人国立精神・神経医療研究センター精神・神経疾患研究開発費「ジストロフィン欠損モデル動物を基盤とした筋ジストロフィーの新しい治療法開発」平成30年度班会議, Dec. 2018.
2.	Takeshi Nikawa, Takayuki Uchida, Ayako Maita, Reiko Nakao, 小林剛, 曽我部正博 and 武田伸一 : 無重力(Unloading)ストレスによる筋細胞のシグナルトランスダクション, 国立研究開発法人国立精神・神経医療研究センター精神・神経疾患研究開発費「ジストロフィン欠損モデル動物を基盤とした筋ジストロフィーの新しい治療法開発」平成29年度班会議, Dec. 2017.
3.	Takeshi Nikawa, Takayuki Uchida, Ayako Maita and Reiko Nakao : 無重力環境で培養した筋細胞のメタボローム解析, 第2回メタボローム解析シンポジウム, Jun. 2017.

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

廃用性筋萎縮に繋がるミトコンドリア-小胞体連関による新規鉄代謝制御システムの解明 (Project/Area Number: 23K10846 )
Novel anti-muscle atrophy signaling via the stress response molecule HO-1 (Project/Area Number: 20K19639 )
長期間の重力変化に対するマウス骨格筋の適応メカニズム追究 (Project/Area Number: 19KK0253 )
A novel nutritional approach to muscle atrophy: Connecting iron and energy metabolism (Project/Area Number: 18K17968 )
Search by Researcher Number (00803561)

Associate Professor : Uchida, Takayuki

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