© 1995 American Heart Association, Inc.
Articles |
Cardiac Troponin I Phosphorylation Increases the Rate of Cardiac Muscle Relaxation
From the Department of Molecular and Cellular Pharmacology, University of Miami (Fla) School of Medicine.
Correspondence to Dr James D. Potter, Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, PO Box 016189, Miami, FL 33101.
Abstract Cardiac troponin (Tn) I (CTnI), compared with
skeletal TnI, contains extra amino acids (32 to 33) at its amino
terminus, including two adjacent serine residues. These two serine
residues are believed to be phosphorylated by protein
kinase A (PKA) upon stimulation of the heart by ß-agonists. In this
study, we found that phosphorylation of a cardiac skinned muscle
preparation by PKA, mainly at CTnI, results in a decrease in the
Ca2+ sensitivity of muscle contraction. The
pCa50 decreased by 
0.27±0.06 pCa units upon
phosphorylation. To study cardiac muscle relaxation, we used diazo-2, a
photolabile Ca2+ chelator with a low
Ca2+ affinity in its intact form that is converted
to a high-affinity form after photolysis. We found that the rate of
cardiac muscle relaxation increased from a time of half-relaxation
(t1/2)=110±10 milliseconds to t1/2=70±8
milliseconds after CTnI phosphorylation. This result demonstrates that
CTnI phosphorylation can be linked with the increased rate of muscle
relaxation in a relatively intact muscle preparation. Since CTnI
phosphorylation has been shown previously to affect the
Ca2+ affinity and Ca2+ off-rate
of CTnC in vitro, it is likely that the faster relaxation seen here
reflects faster dissociation of Ca2+ from cardiac
TnC (CTnC). Model calculations show that increased dissociation of
Ca2+ from CTnC, coupled with the faster uptake of
Ca2+ by the sarcoplasmic reticulum stimulated by PKA
phosphorylation of phospholamban, can account for the faster relaxation
seen in the inotropic response of the heart to catecholamines.
Key Words: cardiac troponin I • cardiac skinned muscle
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