Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading.

Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Research Abstract Details 

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Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Abstract Text:

Zhi Bin Yu,Fang Gao,Han Zhong Feng,Jian-Ping Jin,

Weight-bearing skeletal muscles change phenotype in response to unloading. Using the hindlimb suspension rat model, we investigated the regulation of myofilament protein isoforms in correlation to contractility. Four weeks of continuous hindlimb unloading produced progressive atrophy and contractility changes in soleus but not extensor digitorum longus muscle. The unloaded soleus muscle also had decreased fatigue resistance. Along with the decrease of myosin heavy chain isoform I and IIa and increase of IIb and IIx, coordinated regulation of thin filament regulatory protein isoforms were observed: gamma- and beta-tropomyosin decreased and alpha-tropomyosin increased, resulting in an alpha/beta ratio similar to that in normal fast twitch skeletal muscle; troponin I and troponin T (TnT) both showed decrease in the slow isoform and increases in the fast isoform. The TnT isoform switching began after 7 days of unloading and TnI isoform showed detectable changes at 14 days while other protein isoform changes were not significant until 28 days of treatment. Correlating to the early changes in contractility, especially the resistance to fatigue, the early response of TnT isoform regulation may play a unique role in the adaptation of skeletal muscle to unloading. When the fast TnT gene expression was upregulated in the unloaded soleus muscle, alternative RNA splicing switched to produce more high molecular weight acidic isoforms, reflecting a potential compensation for the decrease of slow TnT that is critical to skeletal muscle function. The results demonstrate that differential regulation of TnT isoforms is a sensitive mechanism in muscle adaptation to functional demands.

Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Publishing Authors By Initials

ZB Yu,F Gao,HZ Feng,JP Jin,

For similar animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats: rats, sprague-dawley research abstracts see: animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats: rats, sprague-dawley research

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Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: American journal of physiology. Cell physiology

VOLUME: 292

Page Numbers: C1192-203

Journal Abbreviation: Am. J. Physiol., Cell Physiol.

ISSN: 0363-6143

DAY: 15

MONTH: 11

YEAR: 2006

Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 100901225

Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Keywords Mesh Terms:

KEYWORDS: Rats, Sprague-Dawley

MESH TERMS: metabolism

Chemical & Substance for Abstract: Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading. Information

Substance Name: Protein Isoforms

Registry Number: 0

Grant and Affiliation Information for Differential regulation of myofilament protein isoforms underlying the contractility changes in skeletal muscle unloading.

AFFILIATION: Section of Molecular Cardiology, Evanston Northwestern Healthcare, Northwestern University Feinberg School of Medicine, Evanston, IL 60201, USA.

Country: United States

AGENCY: United States NICHD

GRANT: R21 HD044824-03

ACRONYM: HD

MEDLINETA: Am J Physiol Cell Physiol

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