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Am J Physiol Heart Circ Physiol (May 23, 2002). doi:10.1152/ajpheart.00128.2002
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Articles in PresS, published online ahead of print May 23, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00128.2002
Submitted on February 21, 2002
Accepted on May 22, 2002

Troponin I Serines 43/45 and Regulation of Cardiac Myofilament Function

W. Glen Pyle1*, Marius P. Sumandea1, R. John Solaro1, and Pieter P. de Tombe1

1 Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois, USA

* To whom correspondence should be addressed. E-mail: gpyle{at}uic.edu.

We studied Ca2+ dependence of tension and actomyosin ATPase rate in detergent extracted fiber bundles isolated from transgenic mice (TG) in which cardiac troponin I (cTnI) serines 43 and 45 were mutated to alanines (cTnI S43A/S45A). Basal phosphorylation levels of cTnI were lower in TG than wild-type (WT), but phosphorylation of cTnT was increased. Compared to WT, TG fiber bundles showed a 13% decrease in maximum tension and a 20% increase in maximum MgATPase activity, yielding an increase in tension cost. PKC activation with endothelin (ET) or phenylephrine plus propranolol (PP) prior to detergent extraction induced a decrease in maximum tension and MgATPase activity in WT fibers, whereas ET or PP increased maximum tension and stiffness in TG fibers. TG MgATPase activity was unchanged by ET, but increased by PP. Measurement of protein phosphorylation revealed differential effects of agonists between WT and TG myofilaments and within the TG myofilaments. Our results demonstrate the importance of PKC-mediated phosphorylation of cTnI S43/S45 in the control of myofilament activation and cross-bridge cycling rate.




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