Abstract:
:Full muscle relaxation happens when [Ca2+] falls below the threshold for force activation. Several experimental models, from whole muscle organs and intact muscle down to skinned fibers, have been used to explore the cascade of kinetic events leading to mechanical relaxation. The use of single myofibrils together with fast solution switching techniques, has provided new information about the role of cross-bridge (CB) dissociation in the time course of isometric force decay. Myofibril's relaxation is biphasic starting with a slow seemingly linear phase, with a rate constant, slow kREL, followed by a fast mono-exponential phase. Sarcomeres remain isometric during the slow force decay that reflects CB detachment under isometric conditions while the final fast relaxation phase begins with a sudden give of few sarcomeres and is then dominated by intersarcomere dynamics. Based on a simple two-state model of the CB cycle, myofibril slow kREL represents the apparent forward rate with which CBs leave force generating states (gapp) under isometric conditions and correlates with the energy cost of tension generation (ATPase/tension ratio); in short slow kREL ~ gapp ~ tension cost. The validation of this relationship is obtained by simultaneously measuring maximal isometric force and ATP consumption in skinned myocardial strips that provide an unambiguous determination of the relation between contractile and energetic properties of the sarcomere. Thus, combining kinetic experiments in isolated myofibrils and mechanical and energetic measurements in multicellular cardiac strips, we are able to provide direct evidence for a positive linear correlation between myofibril isometric relaxation kinetics (slow kREL) and the energy cost of force production both measured in preparations from the same cardiac sample. This correlation remains true among different types of muscles with different ATPase activities and also when CB kinetics are altered by cardiomyopathy-related mutations. Sarcomeric mutations associated to hypertrophic cardiomyopathy (HCM), a primary cardiac disorder caused by mutations in genes encoding sarcomeric proteins, have been often found to accelerate CB turnover rate and increase the energy cost of myocardial contraction. Here we review data showing that faster CB detachment results in a proportional increase in the energetic cost of tension generation in heart samples from both HCM patients and mouse models of the disease.
journal_name
J Muscle Res Cell Motiljournal_title
Journal of muscle research and cell motilityauthors
Vitale G,Ferrantini C,Piroddi N,Scellini B,Pioner JM,Colombini B,Tesi C,Poggesi Cdoi
10.1007/s10974-019-09566-2subject
Has Abstractpub_date
2019-11-19 00:00:00eissn
0142-4319issn
1573-2657pii
10.1007/s10974-019-09566-2pub_type
杂志文章abstract::The hypothesis that calmodulin (CaM) may act as a positive modulator of junctional SR Ca2+-release channel/ ryanodine receptor (RyRl) rests largerly on the demonstrated capacity of CaM to interact structurally and functionally with RyRl at pCa > 8 (Tripathy et al., 1995). The goal of the present [3H]-ryanodine binding...
journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章,评审
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
doi:10.1007/BF01739856
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
doi:10.1023/a:1019988815436
更新日期:2002-01-01 00:00:00
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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更新日期:2004-01-01 00:00:00
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
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journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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abstract::The kinetics of smooth muscle are thought to be partially determined by the level of the expression of the 7 amino acid insert, SMB, in the myosin heavy chain, as SMB is generally expressed at higher levels in faster smooth muscle. In this study, we determined the role of this insert on shortening velocity and force r...
journal_title:Journal of muscle research and cell motility
pub_type: 杂志文章
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