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209 results on '"Ohkoshi, Norio"'

2. The CHC22 clathrin-GLUT4 transport pathway contributes to skeletal muscle regeneration.

Author

Hoshino, Sachiko, Sakamoto, Kazuho, Vassilopoulos, Stéphane, Camus, Stéphane, Griffin, Christine, Esk, Christopher, Torres, Jorge, Ohkoshi, Norio, Ishii, Akiko, Tamaoka, Akira, Funke, Birgit, Kucherlapati, Raju, Brodsky, Frances, Margeta, Marta, and Rando, Thomas

Subjects
Animals, Case-Control Studies, Cell Differentiation, Cells, Cultured, Clathrin, Clathrin Heavy Chains, Glucose, Glucose Transporter Type 4, Humans, Immunoblotting, Mice, Mice, Transgenic, Muscle Fibers, Skeletal, Muscle, Skeletal, Muscular Diseases, Myoblasts, Protein Transport, Rats, Regeneration
Abstract

Mobilization of the GLUT4 glucose transporter from intracellular storage vesicles provides a mechanism for insulin-responsive glucose import into skeletal muscle. In humans, clathrin isoform CHC22 participates in formation of the GLUT4 storage compartment in skeletal muscle and fat. CHC22 function is limited to retrograde endosomal sorting and is restricted in its tissue expression and species distribution compared to the conserved CHC17 isoform that mediates endocytosis and several other membrane traffic pathways. Previously, we noted that CHC22 was expressed at elevated levels in regenerating rat muscle. Here we investigate whether the GLUT4 pathway in which CHC22 participates could play a role in muscle regeneration in humans and we test this possibility using CHC22-transgenic mice, which do not normally express CHC22. We observed that GLUT4 expression is elevated in parallel with that of CHC22 in regenerating skeletal muscle fibers from patients with inflammatory and other myopathies. Regenerating human myofibers displayed concurrent increases in expression of VAMP2, another regulator of GLUT4 transport. Regenerating fibers from wild-type mouse skeletal muscle injected with cardiotoxin also showed increased levels of GLUT4 and VAMP2. We previously demonstrated that transgenic mice expressing CHC22 in their muscle over-sequester GLUT4 and VAMP2 and have defective GLUT4 trafficking leading to diabetic symptoms. In this study, we find that muscle regeneration rates in CHC22 mice were delayed compared to wild-type mice, and myoblasts isolated from these mice did not proliferate in response to glucose. Additionally, CHC22-expressing mouse muscle displayed a fiber type switch from oxidative to glycolytic, similar to that observed in type 2 diabetic patients. These observations implicate the pathway for GLUT4 transport in regeneration of both human and mouse skeletal muscle, and demonstrate a role for this pathway in maintenance of muscle fiber type. Extrapolating these findings, CHC22 and GLUT4 can be considered markers of muscle regeneration in humans.

Published
2013

6. An autosomal dominant cerebellar ataxia linked to chromosome 16q22.1 is associated with a single-nucleotide substitution in the 5' untranslated region of the gene encoding a protein with spectrin repeat and rho guanine-nucleotide exchange-factor domains

Author

Ishikawa, Kinya, Toru, Shuta, Tsunemi, Taiji, Li, Mingshun, Kobayashi, Kazuhiro, Yokota, Takanori, Amino, Takeshi, Owada, Kiyoshi, Fujigasaki, Hiroto, Sakamoto, Masaki, Tomimitsu, Hiroyuki, Takashima, Minoru, Kumagai, Jiro, Noguchi, Yoshihiro, Kawashima, Yoshiyuki, Ohkoshi, Norio, Ishida, Gen, Gomyoda, Manabu, Yoshida, Mari, Hashizume, Yoshio, Saito, Yuko, Murayama, Shigeo, Yamanouchi, Hiroshi, Mizutani, Toshio, Kondo, Ikuko, Toda, Tatsushi, and Mizusawa, Hidehiro

Subjects
Human genetics -- Research, Nervous system -- Degeneration, Genetic disorders, Cerebellar ataxia, Central nervous system diseases, Biological sciences
Published
2005

21. Beta-synemin expression in cardiotoxin-injected rat skeletal muscle

Author

Okamoto Koichi, Tamaoka Akira, Ohkoshi Norio, Hoshino Sachiko, Ishii Akiko, Guyon Jeffrey R, Mizuno Yuji, and Kunkel Louis M

Subjects
Diseases of the musculoskeletal system, RC925-935
Abstract

Abstract Background β-synemin was originally identified in humans as an α-dystrobrevin-binding protein through a yeast two-hybrid screen using an amino acid sequence derived from exons 1 through 16 of α-dystrobrevin, a region common to both α-dystrobrevin-1 and -2. α-Dystrobrevin-1 and -2 are both expressed in muscle and co-localization experiments have determined which isoform preferentially functions with β-synemin in vivo. The aim of our study is to show whether each α-dystrobrevin isoform has the same affinity for β-synemin or whether one of the isoforms preferentially functions with β-synemin in muscle. Methods The two α-dystrobrevin isoforms (-1 and -2) and β-synemin were localized in regenerating rat tibialis anterior muscle using immunoprecipitation, immunohistochemical and immunoblot analyses. Immunoprecipitation and co-localization studies for α-dystrobrevin and β-synemin were performed in regenerating muscle following cardiotoxin injection. Protein expression was then compared to that of developing rat muscle using immunoblot analysis. Results With an anti-α-dystrobrevin antibody, β-synemin co-immunoprecipitated with α-dystrobrevin whereas with an anti-β-synemin antibody, α-dystrobrevin-1 (rather than the -2 isoform) preferentially co-immunoprecipitated with β-synemin. Immunohistochemical experiments show that β-synemin and α-dystrobrevin co-localize in rat skeletal muscle. In regenerating muscle, β-synemin is first expressed at the sarcolemma and in the cytoplasm at day 5 following cardiotoxin injection. Similarly, β-synemin and α-dystrobrevin-1 are detected by immunoblot analysis as weak bands by day 7. In contrast, immunoblot analysis shows that α-dystrobrevin-2 is expressed as early as 1 day post-injection in regenerating muscle. These results are similar to that of developing muscle. For example, in embryonic rats, immunoblot analysis shows that β-synemin and α-dystrobevin-1 are weakly expressed in developing lower limb muscle at 5 days post-birth, while α-dystrobrevin-2 is detectable before birth in 20-day post-fertilization embryos. Conclusion Our results clearly show that β-synemin expression correlates with that of α-dystrobrevin-1, suggesting that β-synemin preferentially functions with α-dystrobrevin-1 in vivo and that these proteins are likely to function coordinately to play a vital role in developing and regenerating muscle.

Published
2007
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25. Miller Fisher syndrome with sinus arrest

Author

Shiraiwa, Nobuko, primary, Umesawa, Mitsumasa, additional, Hoshino, Sachiko, additional, Enomoto, Tsuyoshi, additional, Kusunoki, Susumu, additional, Tamaoka, Akira, additional, and Ohkoshi, Norio, additional

Published
2017
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28. Functional Limitations in Thiamine Deficiency Neuropathy: FIM Score Improvement With Treatment

Author

Fujita Tsuneo, Ohkoshi Norio, and Hayashi Akito

Subjects
Vitamin, medicine.medical_specialty, Activities of daily living, Bathing, business.industry, General Medicine, Functional Independence Measure, chemistry.chemical_compound, Neurology, Biochemistry, chemistry, Toileting, Physical therapy, Medicine, Daily living, Neurology (clinical), business, human activities, Motor ability, Thiamine deficiency neuropathy
Abstract

We studied the functional limitations of the activities of daily living and the effect of treatment on 8 patients with thiamine deficiency neuropathy. Functional activities of daily living were evaluated using the functional independence measure whose scores were obtained before and after high-dose vitamin B1 therapy. In the pretreatment evaluation, the lowest mean score was that of in locomotion (stairs), followed by locomotion (walk-wheelchair), transfers (tub-shower), bathing, dressing the lower body, toileting, transfers (bed-chair-wheelchair), and transfers (toilet), in that order. This tendency was also observed after treatment. The most remarkable therapeutic efficacy was observed in locomotion (walk-wheelchair), followed by transfers (tub-shower), locomotion (stairs), dressing the lower body, and toileting, in that order. Every action reflects the motor ability of the lower extremities. Thiamine deficiency neuropathy should be assessed routinely not only by medical evaluation of clinical symptoms or laboratory studies but also by functional evaluation that reflects each patient's disability.

Published
2008

47. Autoimmunity to Gephyrin in Stiff-Man Syndrome

Author

Butler, Margaret Husta, primary, Hayashi, Akito, additional, Ohkoshi, Norio, additional, Villmann, Carmen, additional, Becker, Cord-Michael, additional, Feng, Guoping, additional, De Camilli, Pietro, additional, and Solimena, Michele, additional

Published
2000
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