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Regulation of cardiac contractile function by troponin I phosphorylation

Research output: Contribution to journalLiterature review

J Layland, R J Solaro, A M Shah

Original languageEnglish
Pages (from-to)12 - 21
Number of pages10
JournalCardiovascular Research
Issue number1
Publication statusPublished - 1 Apr 2005

King's Authors


Cardiac troponin I (cTnl) is a key regulatory protein in cardiac muscle contraction and relaxation, linking Ca2+ -troponin C binding with activation of crossbridge reactions with the thin filament. In recent years, it has become increasingly apparent that myofilament properties as well as changes in intracellular Ca2+ have a major role in the dynamic modulation of contractile function. The phosphorylation of specific serine and threonine residues on cTnl by several different kinases represents a major physiological mechanism for alteration of myofilament properties. Furthennore, altered thin filament function plays an important role in the contractile dysfunction associated with heart failure. Modification of cTn1 by protein kinases A and C has been extensively studied with especially useful information deriving from (a) in vitro studies in reconstituted detergent-skinned fibre bundles in which endogenous cTn1 was replaced with various targeted cTn1 mutants and (b) transgenic animals in which endogenous cTn1 was similarly manipulated through overexpression of cardiomyocyte-targeted cTn1 mutants. cTn1 may also be specifically modified by protein kinase G, p21-activated kinases and by dephosphorylation. This review focuses on recent advances in understanding the mechanisms of cTn1 modification by these kinases and the consequent functional effects both under physiological conditions and in pathophysiological settings. (c) 2005 European Society of Cardiology. Published by Elsevier B.V. All rights reserved

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