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

Research output: Contribution to journalArticleAcademicpeer-review

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 - 19 Apr 2003

Cite this

Van Der Velden, J., Papp, Z., Boontje, N. M., Zaremba, R., De Jong, J. W., Janssen, P. M. L., ... Stienen, G. J. M. (2003). Myosin light chain composition in non-failing donor and end-stage failing human ventricular myocardium. Advances in Experimental Medicine and Biology, 538, 3-15.
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. / Myosin light chain composition in non-failing donor and end-stage failing human ventricular myocardium. In: Advances in Experimental Medicine and Biology. 2003 ; Vol. 538. pp. 3-15.
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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.",
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Van Der Velden, J, Papp, Z, Boontje, NM, Zaremba, R, De Jong, JW, Janssen, PML, Hasenfuss, G & Stienen, GJM 2003, 'Myosin light chain composition in non-failing donor and end-stage failing human ventricular myocardium' Advances in Experimental Medicine and Biology, vol. 538, pp. 3-15.

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

In: Advances in Experimental Medicine and Biology, Vol. 538, 19.04.2003, p. 3-15.

Research output: Contribution to journalArticleAcademicpeer-review

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AB - 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.

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