Document Detail


Chronic contractile activity upregulates the proteasome system in rabbit skeletal muscle.
MedLine Citation:
PMID:  10710413     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Remodeling of skeletal muscle in response to altered patterns of contractile activity is achieved, in part, by the regulated degradation of cellular proteins. The ubiquitin-proteasome system is a dominant pathway for protein degradation in eukaryotic cells. To test the role of this pathway in contraction-induced remodeling of skeletal muscle, we used a well-established model of continuous motor nerve stimulation to activate tibialis anterior (TA) muscles of New Zealand White rabbits for periods up to 28 days. Western blot analysis revealed marked and coordinated increases in protein levels of the 20S proteasome and two of its regulatory proteins, PA700 and PA28. mRNA of a representative proteasome subunit also increased coordinately in contracting muscles. Chronic contractile activity of TA also increased total proteasome activity in extracts, as measured by the hydrolysis of a proteasome-specific peptide substrate, and the total capacity of the ubiquitin-proteasome pathway, as measured by the ATP-dependent hydrolysis of an exogenous protein substrate. These results support the potential role of the ubiquitin-proteasome pathway of protein degradation in the contraction-induced remodeling of skeletal muscle.
Authors:
G A Ordway; P D Neufer; E R Chin; G N DeMartino
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  88     ISSN:  8750-7587     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-04-24     Completed Date:  2000-04-24     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1134-41     Citation Subset:  IM; S    
Affiliation:
Department of Physiology, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9040, USA. gordwa@mednet.swmed.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Cysteine Endopeptidases / genetics,  metabolism*
Electric Stimulation
Multienzyme Complexes / genetics,  metabolism*
Muscle Contraction / physiology*
Muscle Proteins / metabolism
Muscle, Skeletal / enzymology*,  physiology
Proteasome Endopeptidase Complex
RNA, Messenger / genetics,  metabolism
Rabbits
Ubiquitins / metabolism
Up-Regulation
Grant Support
ID/Acronym/Agency:
DK-46181/DK/NIDDK NIH HHS; HL-06296/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; 0/Muscle Proteins; 0/RNA, Messenger; 0/Ubiquitins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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