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1. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration

Author

Towler, MC, Gleeson, PA, Hoshino, S, Rahkila, P, Ohkoshi, N, Ordahl, CP, Parton, RG, and Brodsky, FM

Subjects
Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle, Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins, Biological Sciences, Medical and Health Sciences, Developmental Biology, Biochemistry and cell biology
Abstract

The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.

Published
2023

2. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration

Author

Towler, MC, Gleeson, PA, Hoshino, S, Rahkila, P, Ohkoshi, N, Ordahl, CP, Parton, RG, and Brodsky, FM

Subjects
Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle, Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins, Biological Sciences, Medical and Health Sciences, Developmental Biology
Abstract

The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.

Published
2021

3. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration

Author

Towler, MC, Towler, MC, Gleeson, PA, Hoshino, S, Rahkila, P, Ohkoshi, N, Ordahl, CP, Parton, RG, Brodsky, FM, Towler, MC, Towler, MC, Gleeson, PA, Hoshino, S, Rahkila, P, Ohkoshi, N, Ordahl, CP, Parton, RG, and Brodsky, FM

Abstract

The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.

Published
2022

11. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration

Author

Towler, MC, Gleeson, PA, Hoshino, S, Rahkila, P, Ohkoshi, N, Ordahl, CP, Parton, RG, and Brodsky, FM

Subjects
Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle, Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins, Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle, Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins, Biological Sciences, Medical and Health Sciences, Developmental Biology
Abstract

The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin and then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light-chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair, and at neuromuscular and myotendinous junctions.

Published
2017

17. G.P.204

Author

Ishii, A., primary, Yoshida, M., additional, Ohkoshi, N., additional, Ueno, H., additional, Kokubo, K., additional, and Tamaoka, A., additional

Published
2014
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27. Does K-11706 Enhance Performance and Why?

Author

Imagawa, S., primary, Matsumoto, K., additional, Horie, M., additional, Ohkoshi, N., additional, Nagasawa, T., additional, Doi, T., additional, Suzuki, N., additional, and Yamamoto, M., additional

Published
2007
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36. Cytoplasmic and nuclear polyglutamine aggregates in SCA6 Purkinje cells

Author

Ishikawa, K., primary, Owada, K., additional, Ishida, K., additional, Fujigasaki, H., additional, Shun Li, M., additional, Tsunemi, T., additional, Ohkoshi, N., additional, Toru, S., additional, Mizutani, T., additional, Hayashi, M., additional, Arai, N., additional, Hasegawa, K., additional, Kawanami, T., additional, Kato, T., additional, Makifuchi, T., additional, Shoji, S., additional, Tanabe, T., additional, and Mizusawa, H., additional

Published
2001
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43. Japanese Families with Autosomal Dominant Pure Cerebellar Ataxia Map to Chromosome 19p13.1-p13.2 and Are Strongly Associated with Mild CAG Expansions in the Spinocerebellar Ataxia Type 6 Gene in Chromosome 19p13.1

Author

Ishikawa, K., primary, Tanaka, H., additional, Saito, M., additional, Ohkoshi, N., additional, Fujita, T., additional, Yoshizawa, K., additional, Ikeuchi, T., additional, Watanabe, M., additional, Hayashi, A., additional, Takiyama, Y., additional, Nishizawa, M., additional, Nakano, I., additional, Matsubayashi, K., additional, Miwa, M., additional, Shoji, S., additional, Kanazawa, I., additional, Tsuji, S., additional, and Mizusawa, H., additional

Published
1997
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47. Association between Catechol-O -Methyltransferase Gene Polymorphisms and Wearing-Off and Dyskinesia in Parkinson’s Disease.

Author

Harada, S., Nakamura, T., Ohkoshi, N., Yoshizawa, K., Hayashi, A., Shoji, S., and Watanabe, M.

Subjects
CATECHOLAMINES, DOPA, GENETIC polymorphisms, PARKINSON'S disease patients, MOVEMENT disorders, DOPAMINE, THERAPEUTICS
Abstract

Catechol-O -methyltransferase (COMT) is an enzyme that inactivates catecholamines, including levodopa. An amino acid change (Val-108-Met) in the COMT protein has been found to result in a change from high to low enzyme activity. In the present study, we genotyped 121 Japanese patients with Parkinson’s disease (PD) and 100 controls. Comparison of the allele frequencies revealed that homozygosity for the low-activity allele was significantly more common among PD patients than the controls (p = 0.047, odds ratio = 3.23). In addition, homozygosity for the low-activity allele was overrepresented in PD patients that exhibited the ‘wearing-off’ phenomenon (p = 0.045, odds ratio = 3.82) or dyskinesia (p = 0.030, odds ratio = 4.80) compared with controls, although these differences were not significant after Bonferroni’s correction. Our results may help understand the mechanism that cause complications of levodopa therapy in PD patients. Copyright © 2003 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Published
2003

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