© 1995 American Heart Association, Inc.
Articles |
1-Adrenergic Receptor Stimulation Decreases Maximum Shortening Velocity of Skinned Single Ventricular Myocytes From Rats
From the Department of Physiology, School of Medicine, University of Wisconsin, Madison, Wis.
Correspondence to Kevin T. Strang, Department of Physiology, 1300 University Ave, Madison, WI 53706.
Abstract 
1-Adrenergic agonists have negative
inotropic effects on mammalian myocardium under some
conditions, and biochemical experiments measuring the
Ca2+-activated actomyosin ATPase activity of
myofibrillar preparations suggest that this may result from a decrease
in cross-bridge cycling rate caused by phosphorylation
of myofilament proteins. Experiments with intact
ventricular preparations, however, have failed to
demonstrate a mechanical manifestation of a decrease in cycling rate.
The present study examined the effect of
1-adrenergic receptor stimulation on maximum shortening
velocity in skinned single ventricular myocytes from rats.
Enzymatically isolated myocytes were incubated with the ß-receptor
antagonist propranolol in the presence or
absence of the 1-adrenergic receptor agonist
phenylephrine and were then rapidly skinned to preserve the
phosphorylation state of myofilament proteins. The
velocity of unloaded shortening (Vo) was determined
by use of the slack-test method and compared between skinned control
and phenylephrine-treated cells. The relationship between
isometric tension and [Ca2+] was also assessed for
each myocyte. Vo was significantly lower in the
1-adrenergic receptor agonist–treated cells than in the
control cells, but there was no effect on Ca2+
sensitivity of isometric tension. In addition, the myosin heavy chain
isoform composition accounted for a significant amount of the variation
in Vo within the treatment groups. On the basis of these
and previous results we propose that 1-adrenergic
receptor stimulation inhibits cross-bridge cycling rate at the level of
myofilament proteins by a mechanism that may involve
phosphorylation of troponin I by protein kinase C.
Key Words: 1-adrenergic receptor • cardiac myocyte • shortening velocity • phosphorylation
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