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Am J Physiol Heart Circ Physiol 283: H1446-H1454, 2002. First published June 6, 2002; doi:10.1152/ajpheart.00274.2002
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Vol. 283, Issue 4, H1446-H1454, October 2002

Molecular mechanics of mouse cardiac myosin isoforms

Norman R. Alpert1, Christine Brosseau1, Andrea Federico1, Maike Krenz2, Jeffrey Robbins2, and David M. Warshaw1

1 Department of Molecular Physiology and Biophysics, University of Vermont College of Medicine, Burlington, Vermont 05405; and 2 Molecular Cardiovascular Biology, Children's Hospital, Cincinnati, Ohio 45229

Two myosin isoforms are expressed in myocardium, alpha alpha -homodimers (V1) and beta beta -homodimers (V3). V1 exhibits higher velocities and myofibrillar ATPase activities compared with V3. We also observed this for cardiac myosin from normal (V1) and propylthiouracil-treated (V3) mice. Actin velocity in a motility assay (Vactin) over V1 myosin was twice that of V3 as was the myofibrillar ATPase. Myosin's average force (Favg) was similar for V1 and V3. Comparing Vactin and Favg across species for both V1 and V3, our laboratory showed previously (VanBuren P, Harris DE, Alpert NR, and Warshaw DM. Circ Res 77: 439-444, 1995) that mouse V1 has greater Vactin and Favg compared with rabbit V1. Mouse V3 Vactin was twice that of rabbit Vactin. To understand myosin's molecular structure and function, we compared alpha - and beta -cardiac myosin sequences from rodents and rabbits. The rabbit alpha - and beta -cardiac myosin differed by eight and four amino acids, respectively, compared with rodents. These residues are localized to both the motor domain and the rod. These differences in sequence and mechanical performance may be an evolutionary attempt to match a myosin's mechanical behavior to the heart's power requirements.

contractile proteins; heart; motility assay; molecular motor


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