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Am J Physiol Heart Circ Physiol 282: H1665-H1671, 2002. First published January 3, 2002; doi:10.1152/ajpheart.00938.2001
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Vol. 282, Issue 5, H1665-H1671, May 2002

Cardiac troponin T isoforms demonstrate similar effects on mechanical performance in a regulated contractile system

Peter VanBuren1,2, Shari L. Alix1, Joseph A. Gorga1, Kelly J. Begin1, Martin M. LeWinter1, and Norman R. Alpert2

1 Cardiology Unit, Department of Medicine, and 2 Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont 05405

Alteration of troponin T (TnT) isoform expression has been reported in human and animal models of myocardial failure. The two adult beef cardiac TnT isoforms (TnT3 and TnT4) were isolated for comparative functional analysis. Thin filaments were reconstituted containing pure populations of the isoforms. The in vitro motility assay was used to directly compare the effect of the two TnT isoforms on force and unloaded shortening as a function of free calcium. We found no significant differences between the two isoforms in terms of calcium sensitivity, cooperativity, or maximal activation (velocity and force) as assessed in a fully calcium-regulated system. Activation by myosin strong binding was similar for thin filaments containing either of the two TnT isoforms. Whereas maximally activated velocity and cooperativity was depressed at pH 6.5, no difference between thin filaments containing the two isoforms was detected. From the small magnitude of the TnT isoform shifts detected in myocardial failure and the lack of significant mechanical effect detected in the motility assay, variable TnT isoform expression is unlikely to be any functional significance in heart failure.

thin filament; myocardial failure; in vitro motility


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