Myosin light chain composition in non-failing donor and end-stage failing human ventricular myocardium

J. Van Der Velden, Z. Papp, N. M. Boontje, R. Zaremba, J. W. De Jong, P. M.L. Janssen, G. Hasenfuss, G. J.M. Stienen

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16 Citations (Scopus)

Abstract

The increased Ca2+-responsiveness in end-stage human heart failure cannot be attributed to contractile protein isoform changes, but rather is the complex resultant of changes in degree of phosphorylation of VLC-2 and TnI. Despite the decreased basal level of VLC-2 phosphorylation the response to VLC-2 dephosphorylation is enhanced in failing myocytes, which might result from differences in endogenous phosphorylation of thin and thick filament proteins between donor and failing hearts. Taken together decreased VLC-2 phosphorylation in end-stage human heart failure might represent a compensatory process leading to an improvement of myocardial contractility by opposing the detrimental effects of increased Ca2+-responsiveness of force and impaired Ca2+-handling on diastolic function.

Original languageEnglish
Pages (from-to)3-15
Number of pages13
JournalAdvances in experimental medicine and biology
Volume538
Publication statusPublished - Apr 19 2004

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Van Der Velden, J., Papp, Z., Boontje, N. M., Zaremba, R., De Jong, J. W., Janssen, P. M. L., Hasenfuss, G., & Stienen, G. J. M. (2004). Myosin light chain composition in non-failing donor and end-stage failing human ventricular myocardium. Advances in experimental medicine and biology, 538, 3-15.