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Cardiovascular Research 1993 27(3):416-422; doi:10.1093/cvr/27.3.416
© 1993 by European Society of Cardiology
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Copyright © 1993, European Society of Cardiology

Correlated expression of atrial myosin heavy chain and regulatory light chain isoforms with pressure overload hypertrophy in the non-human primate

Richard D Henkel, Candace M Kammerer, Laura V Escobedo, John L VandeBerg and Richard A Walsh

Department of Genetics, Southwest Foundation for Biomedical Research, PO Box 28147, San Antonio, Texas, USA: R D Henkel, C M Kammerer, L V Escobedo, J L VandeBerg; Department of Medicine, Division of Cardiology, University of Cincinnati, 231 Bethesda Avenue, Cincinnati, Ohio 45267-0542, USA: R A Walsh.

Correspondence to Dr Walsh.

Objective: The aim was to determine the extent to which myosin heavy chain and light chain isoform transitions in atrial myocardium are coordinately regulated under pathological conditions in tissue from normal baboons, hypertensive baboons with myocardial hypertrophy, and baboons in which hypertrophy had regressed. Methods: Quantitative distributions of myosin heavy chain (MHC) and regulatory myosin light chain (MLC2) isoforms in atrial myocardium from 35 adult baboons were determined by electrophoresis under denaturing conditions and laser densitometry. Results: A significant association was observed between the ratios of MHC and MLC2 isoforms in atrial myocardium (r=0.73, p<0.001, n=69). Expressions of {alpha} MHC and atrial MLC2 (ALC2) isoforms were correlated in atrial myocardium, as were those of β MHC and ventricular MLC2 (VLC2) isoforms. In a subset of baboons with experimentally induced renal hypertension (n=12) both β MHC and VLC2 isoforms were found at higher levels in left atria than were present in normotensive baboons (p=0.006, n=15). Left atria from hypertensive baboons with regressed LVH contained intermediate levels of both β MHC and VLC2 isoforms. Conclusions: There is tight coupling between the expression of myosin subunit isoforms under pathological conditions from a primate species closely related to humans. The data suggest that the synthesis of these subunits of myosin may be coordinated at the molecular level.

Cardiovascular Research 1993;27:416-422

KEYWORDS myosin heavy chain; myosin light chain isoforms


We gratefully recognise Dr Robert Lanford and Lili Yamasaki for their assistance with the densitometry procedures used in this study. We also thank Dr Jean Leger for providing monoclonal antibodies and Mabel Meeks for typing the manuscript. RAW was supported by a grant from the National Institutes of Health.


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