Circulation Research. 2001;88:1059-1065
Published online before print May 10, 2001, doi: 10.1161/hh1001.091640
Published online before print May 10, 2001, doi: 10.1161/hh1001.091640
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© 2001 American Heart Association, Inc.
Integrative Physiology |
Phosphorylation of Troponin I by Protein Kinase A Accelerates Relaxation and Crossbridge Cycle Kinetics in Mouse Ventricular Muscle
From the Centre for Cardiovascular Biology and Medicine (J.C.K., D.T.McC., J.L., S.P.), King’s College London, St Thomas’ Campus, London, UK; Harvard School of Public Health (J.M.L.), Cardiovascular Biology Laboratory, Boston, Mass; Department of Physiology and Biophysics (A.F.M., R.J.S.), University of Illinois at Chicago, Chicago, Ill.
Correspondence to Jonathan C. Kentish, MA, PhD, Centre for Cardiovascular Biology & Medicine, King’s College London, The Rayne Institute, St. Thomas’ Hospital, London SE1 7EH UK. E-mail jon.kentish{at}kcl.ac.uk
Abstract—Phosphorylation
of cardiac myofibrils by cAMP-dependent protein kinase (PKA) can
increase the intrinsic rate of myofibrillar relaxation, which may
contribute to the shortening of the cardiac twitch during
ß-adrenoceptor stimulation. However, it is not known whether the
acceleration of myofibrillar relaxation is due to
phosphorylation of troponin I (TnI) or of myosin
binding protein-C (MyBP-C). To distinguish between these possibilities,
we used transgenic mice that overexpress the nonphosphorylatable, slow
skeletal isoform of TnI in the myocardium and do not
express the normal, phosphorylatable cardiac TnI. The intrinsic rate of
relaxation of myofibrils from wild-type and transgenic mice was
measured using flash photolysis of diazo-2 to rapidly decrease the
[Ca2+] within skinned muscles from the
mouse ventricles. Incubation with PKA nearly doubled the intrinsic rate
of myofibrillar relaxation in muscles from wild-type mice (relaxation
half-time fell from 
150 to 90 ms at 22°C) but had no effect on
the relaxation rate of muscles from the transgenic mice. In parallel
studies with intact muscles, we assessed crossbridge kinetics
indirectly by determining
fmin
(the frequency for minimum dynamic stiffness) during tetanic
contractions. Stimulation of ß-adrenoceptors with isoproterenol
increased
fmin
from 1.9 to 3.1 Hz in muscles from wild-type mice but had no effect on
fmin in
muscles from transgenic mice. We conclude that the acceleration of
myofibrillar relaxation rate by PKA is due to
phosphorylation of TnI, rather than MyBP-C, and that
this may be due, at least in part, to faster crossbridge cycle
kinetics.
Key Words: protein kinase A • phosphorylation • relaxation • troponin I • myosin binding protein-C
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B. M. Wolska, G. M. Arteaga, J. R. Pena, G. Nowak, R. M. Phillips, S. Sahai, P. P. de Tombe, A. F. Martin, E. G. Kranias, and R. J. Solaro Expression of Slow Skeletal Troponin I in Hearts of Phospholamban Knockout Mice Alters the Relaxant Effect of {beta}-Adrenergic Stimulation Circ. Res., May 3, 2002; 90(8): 882 - 888. [Abstract] [Full Text] [PDF]
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