© 1995 American Heart Association, Inc.
Articles |
Cardiac V1 And V3 Myosins Differ in Their Hydrolytic and Mechanical Activities In Vitro
From the Departments of Molecular Physiology and Biophysics (D.E.H., N.R.A., D.M.W.) and Cardiology (P.V.B.), University of Vermont, Burlington.
Correspondence to Dr David M. Warshaw, University of Vermont, Department of Molecular Physiology and Biophysics, Given Medical Bldg, D-205, Burlington, VT 05405. E-mail warshaw@salus.med.uvm.edu.
Abstract The two mammalian cardiac myosin heavy chain
isoforms, 
and ß, have 93% amino acid homology, but hearts
expressing these myosins exhibit marked differences in their mechanical
activities. To further understand the function of these cardiac myosins
as molecular motors, we compared the ability of these myosins to
hydrolyze ATP and to both translocate actin filaments and generate
force in an in vitro motility assay. V1 myosin has twice
the actin-activated ATPase activity and three times the actin
filament sliding velocity when compared with V3 myosin. In
contrast, the force-generating ability of these myosins is quite
different when the total force produced by a small population of myosin
molecules (>50) is examined. V1 myosin produces only one
half the average cross-bridge force of V3 myosin. With
discrete areas of primary structural heterogeneity
known to exist between and ß heavy chains, the differences we
report in the hydrolytic and mechanical activities of the motors are
explored in the context of potential structural and kinetic differences
between the V1 and V3 myosins.
Key Words: cardiac myosin • -myosin heavy chain • ß-myosin heavy chain • molecular motor • motility assay
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