Document Detail


Residual force enhancement in myofibrils and sarcomeres.
MedLine Citation:
PMID:  18348966     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Residual force enhancement has been observed following active stretch of skeletal muscles and single fibres. However, there has been intense debate whether force enhancement is a sarcomeric property, or is associated with sarcomere length instability and the associated development of non-uniformities. Here, we studied force enhancement for the first time in isolated myofibrils (n=18) that, owing to the strict in series arrangement, allowed for evaluation of this property in individual sarcomeres (n=79). We found consistent force enhancement following stretch in all myofibrils and each sarcomere, and forces in the enhanced state typically exceeded the isometric forces on the plateau of the force-length relationship. Measurements were made on the plateau and the descending limb of the force-length relationship and revealed gross sarcomere length non-uniformities prior to and following active myofibril stretching, but in contrast to previous accounts, revealed that sarcomere lengths were perfectly stable under these experimental conditions. We conclude that force enhancement is a sarcomeric property that does not depend on sarcomere length instability, that force enhancement varies greatly for different sarcomeres within the same myofibril and that sarcomeres with vastly different amounts of actin-myosin overlap produce the same isometric steady-state forces. This last finding was not explained by differences in the amount of contractile proteins within sarcomeres, vastly different passive properties of individual sarcomeres or (half-) sarcomere length instabilities, suggesting that the basic mechanical properties of muscles, such as force enhancement, force depression and creep, which have traditionally been associated with sarcomere instabilities and the corresponding dynamic redistribution of sarcomere lengths, are not caused by such instabilities, but rather seem to be inherent properties of the mechanisms of contraction.
Authors:
V Joumaa; T R Leonard; W Herzog
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proceedings. Biological sciences / The Royal Society     Volume:  275     ISSN:  0962-8452     ISO Abbreviation:  Proc. Biol. Sci.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-05-05     Completed Date:  2008-08-21     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  101245157     Medline TA:  Proc Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1411-9     Citation Subset:  IM    
Affiliation:
University of Calgary, 2500 University Drive NW, Calgary, Alberta, Canada T2N 1N4.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biomechanics
Isometric Contraction / physiology
Muscle Contraction / physiology
Muscle, Skeletal / physiology*
Myofibrils / physiology*
Rabbits
Sarcomeres / physiology*
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