Literature DB >> 16205841

Length-dependent Ca(2+) activation in cardiac muscle: some remaining questions.

Franklin Fuchs1, Donald A Martyn.   

Abstract

The steep relationship between systolic force and end diastolic volume in cardiac muscle (Frank-Starling relation) is, to a large extent, based on length-dependent changes in myofilament Ca(2+) sensitivity. How sarcomere length modulates Ca(2+) sensitivity is still a topic of active investigation. Two general themes have emerged in recent years. On the one hand, there is a large body of evidence indicating that length-dependent changes in lattice spacing determine changes in Ca(2+) sensitivity for a given set of conditions. A model has been put forward in which the number of strong-binding cross-bridges that are formed is directly related to the proximity of the myosin heads to binding sites on actin. On the other hand, there is also a body of evidence suggesting that lattice spacing and Ca(2+) sensitivity are not tightly linked and that there is a length-sensing element in the sarcomere, which can modulate actin-myosin interactions independent of changes in lattice spacing. In this review, we examine the evidence that has been cited in support of these viewpoints. Much recent progress has been based on the combination of mechanical measurements with X-ray diffraction analysis of lattice spacing and cross-bridge interaction with actin. Compelling evidence indicates that the relationship between sarcomere length and lattice spacing is influenced by the elastic properties of titin and that changes in lattice spacing directly modulate cross-bridge interactions with thin filaments. However, there is also evidence that the precise relationship between Ca(2+) sensitivity and lattice spacing can be altered by changes in protein isoform expression, protein phosphorylation, modifiers of cross-bridge kinetics, and changes in titin compliance. Hence although there is no unique relationship between Ca(2+) sensitivity and lattice spacing the evidence strongly suggests that under any given set of physiological circumstances variation in lattice spacing is the major determinant of length-dependent changes in Ca(2+) sensitivity.

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Year:  2005        PMID: 16205841     DOI: 10.1007/s10974-005-9011-z

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  91 in total

Review 1.  Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation.

Authors:  John P Konhilas; Thomas C Irving; Pieter P de Tombe
Journal:  Pflugers Arch       Date:  2002-11-01       Impact factor: 3.657

2.  Length dependence of Ca(2+)-tension relationship in aequorin-injected ferret papillary muscles.

Authors:  K Komukai; S Kurihara
Journal:  Am J Physiol       Date:  1997-09

3.  Effects of in vivo-like activation frequency on the length-dependent force generation of skeletal muscle fibre bundles.

Authors:  C J Zuurbier; M B Lee-de Groot; W J Van der Laarse; P A Huijing
Journal:  Eur J Appl Physiol Occup Physiol       Date:  1998-05

4.  Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle.

Authors:  N Fukuda; H Kajiwara; S Ishiwata; S Kurihara
Journal:  Circ Res       Date:  2000-01-07       Impact factor: 17.367

5.  Stretch-induced increase in activation of skinned muscle fibres by calcium.

Authors:  M Endo
Journal:  Nat New Biol       Date:  1972-06-14

6.  The variation in isometric tension with sarcomere length in vertebrate muscle fibres.

Authors:  A M Gordon; A F Huxley; F J Julian
Journal:  J Physiol       Date:  1966-05       Impact factor: 5.182

7.  Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes.

Authors:  J van der Velden; J W de Jong; V J Owen; P B Burton; G J Stienen
Journal:  Cardiovasc Res       Date:  2000-06       Impact factor: 10.787

8.  Effect of length and cross-bridge attachment on Ca2+ binding to cardiac troponin C.

Authors:  P A Hofmann; F Fuchs
Journal:  Am J Physiol       Date:  1987-07

9.  Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins.

Authors:  J van der Velden; Z Papp; R Zaremba; N M Boontje; J W de Jong; V J Owen; P B J Burton; P Goldmann; K Jaquet; G J M Stienen
Journal:  Cardiovasc Res       Date:  2003-01       Impact factor: 10.787

10.  Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner.

Authors:  Norio Fukuda; Yiming Wu; Preetha Nair; Henk L Granzier
Journal:  J Gen Physiol       Date:  2005-03       Impact factor: 4.086

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  50 in total

1.  Length dependence of force generation exhibit similarities between rat cardiac myocytes and skeletal muscle fibres.

Authors:  Laurin M Hanft; Kerry S McDonald
Journal:  J Physiol       Date:  2010-06-07       Impact factor: 5.182

2.  X-ray diffraction studies of the thick filament in permeabilized myocardium from rabbit.

Authors:  Sengen Xu; Donald Martyn; Jessica Zaman; Leepo C Yu
Journal:  Biophys J       Date:  2006-09-01       Impact factor: 4.033

3.  Interfilament spacing is preserved during sarcomere length isometric contractions in rat cardiac trabeculae.

Authors:  Gerrie P Farman; Edward J Allen; David Gore; Thomas C Irving; Pieter P de Tombe
Journal:  Biophys J       Date:  2007-02-09       Impact factor: 4.033

4.  Sarcomere length dependence of rat skinned cardiac myocyte mechanical properties: dependence on myosin heavy chain.

Authors:  F Steven Korte; Kerry S McDonald
Journal:  J Physiol       Date:  2007-03-08       Impact factor: 5.182

5.  Effects of sustained length-dependent activation on in situ cross-bridge dynamics in rat hearts.

Authors:  James T Pearson; Mikiyasu Shirai; Hirotsugu Tsuchimochi; Daryl O Schwenke; Takayuki Ishida; Kenji Kangawa; Hiroyuki Suga; Naoto Yagi
Journal:  Biophys J       Date:  2007-08-31       Impact factor: 4.033

6.  Sarcomere length dependence of power output is increased after PKA treatment in rat cardiac myocytes.

Authors:  Laurin M Hanft; Kerry S McDonald
Journal:  Am J Physiol Heart Circ Physiol       Date:  2009-02-27       Impact factor: 4.733

7.  The length-tension curve in muscle depends on lattice spacing.

Authors:  C David Williams; Mary K Salcedo; Thomas C Irving; Michael Regnier; Thomas L Daniel
Journal:  Proc Biol Sci       Date:  2013-09-07       Impact factor: 5.349

8.  Length-dependent activation is modulated by cardiac troponin I bisphosphorylation at Ser23 and Ser24 but not by Thr143 phosphorylation.

Authors:  Paul J M Wijnker; Vasco Sequeira; D Brian Foster; Yuejin Li; Cristobal G Dos Remedios; Anne M Murphy; Ger J M Stienen; Jolanda van der Velden
Journal:  Am J Physiol Heart Circ Physiol       Date:  2014-02-28       Impact factor: 4.733

9.  Phosphorylation of protein kinase C sites Ser42/44 decreases Ca(2+)-sensitivity and blunts enhanced length-dependent activation in response to protein kinase A in human cardiomyocytes.

Authors:  Paul J M Wijnker; Vasco Sequeira; E Rosalie Witjas-Paalberends; D Brian Foster; Cristobal G dos Remedios; Anne M Murphy; Ger J M Stienen; Jolanda van der Velden
Journal:  Arch Biochem Biophys       Date:  2014-05-09       Impact factor: 4.013

Review 10.  Myofilament length dependent activation.

Authors:  Pieter P de Tombe; Ryan D Mateja; Kittipong Tachampa; Younss Ait Mou; Gerrie P Farman; Thomas C Irving
Journal:  J Mol Cell Cardiol       Date:  2010-01-04       Impact factor: 5.000

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