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Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse
Myosin in adult murine skeletal muscle is composed primarily of three adult fast myosin heavy chain (MyHC) isoforms. These isoforms, MyHC-IIa, -IId, and -IIb, are >93% identical at the amino acid level and are broadly expressed in numerous muscles, and their genes are tightly linked. Mice with a...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1998
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132782/ https://www.ncbi.nlm.nih.gov/pubmed/9585413 |
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author | Sartorius, Carol A. Lu, Brian D. Acakpo-Satchivi, Leslie Jacobsen, Renee P. Byrnes, William C. Leinwand, Leslie A. |
author_facet | Sartorius, Carol A. Lu, Brian D. Acakpo-Satchivi, Leslie Jacobsen, Renee P. Byrnes, William C. Leinwand, Leslie A. |
author_sort | Sartorius, Carol A. |
collection | PubMed |
description | Myosin in adult murine skeletal muscle is composed primarily of three adult fast myosin heavy chain (MyHC) isoforms. These isoforms, MyHC-IIa, -IId, and -IIb, are >93% identical at the amino acid level and are broadly expressed in numerous muscles, and their genes are tightly linked. Mice with a null mutation in the MyHC-IId gene have phenotypes that include growth inhibition, muscle weakness, histological abnormalities, kyphosis (spinal curvature), and aberrant kinetics of muscle contraction and relaxation. Despite the lack of MyHC-IId, IId null mice have normal amounts of myosin in their muscles because of compensation by the MyHC-IIa gene. In each muscle examined from IId null mice, there was an increase in MyHC-IIa– containing fibers. MyHC-IIb content was unaffected in all muscles except the masseter, where its expression was extinguished in the IId null mice. Cross-sectional fiber areas, total muscle cross-sectional area, and total fiber number were affected in ways particular to each muscle. Developmental expression of adult MyHC genes remained unchanged in IId null mice. Despite this universal compensation of MyHC-IIa expression, IId null mice have severe phenotypes. We conclude that despite the similarity in sequence, MyHC-IIa and -IId have unique roles in the development and function of skeletal muscle. |
format | Text |
id | pubmed-2132782 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1998 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21327822008-05-01 Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse Sartorius, Carol A. Lu, Brian D. Acakpo-Satchivi, Leslie Jacobsen, Renee P. Byrnes, William C. Leinwand, Leslie A. J Cell Biol Articles Myosin in adult murine skeletal muscle is composed primarily of three adult fast myosin heavy chain (MyHC) isoforms. These isoforms, MyHC-IIa, -IId, and -IIb, are >93% identical at the amino acid level and are broadly expressed in numerous muscles, and their genes are tightly linked. Mice with a null mutation in the MyHC-IId gene have phenotypes that include growth inhibition, muscle weakness, histological abnormalities, kyphosis (spinal curvature), and aberrant kinetics of muscle contraction and relaxation. Despite the lack of MyHC-IId, IId null mice have normal amounts of myosin in their muscles because of compensation by the MyHC-IIa gene. In each muscle examined from IId null mice, there was an increase in MyHC-IIa– containing fibers. MyHC-IIb content was unaffected in all muscles except the masseter, where its expression was extinguished in the IId null mice. Cross-sectional fiber areas, total muscle cross-sectional area, and total fiber number were affected in ways particular to each muscle. Developmental expression of adult MyHC genes remained unchanged in IId null mice. Despite this universal compensation of MyHC-IIa expression, IId null mice have severe phenotypes. We conclude that despite the similarity in sequence, MyHC-IIa and -IId have unique roles in the development and function of skeletal muscle. The Rockefeller University Press 1998-05-18 /pmc/articles/PMC2132782/ /pubmed/9585413 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Sartorius, Carol A. Lu, Brian D. Acakpo-Satchivi, Leslie Jacobsen, Renee P. Byrnes, William C. Leinwand, Leslie A. Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title | Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title_full | Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title_fullStr | Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title_full_unstemmed | Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title_short | Myosin Heavy Chains IIa and IId Are Functionally Distinct in the Mouse |
title_sort | myosin heavy chains iia and iid are functionally distinct in the mouse |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132782/ https://www.ncbi.nlm.nih.gov/pubmed/9585413 |
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