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Biotechnology and Applied Biochemistry (2003) 37, (27–30) (Printed in Great Britain)

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A simplified method for identification of human cardiac myosin heavy-chain isoforms

Shengfu Piao*, Fushun Yu*, Michael J. Mihm*†, Peter J. Reiser‡, Patrick M. McCarthy§, David R. Van Wagoner and John Anthony Bauer*†¶¹

*Division of Pharmacology, College of Pharmacy, The Ohio State University, Columbus, OH 43210, U.S.A., †Center for Developmental Pharmacology and Toxicology, Columbus Children's Research Institute, 700 Children's Drive, Columbus, OH 43205, U.S.A., ‡Department of Oral Biology, College of Dentistry, The Ohio State University, Columbus, OH 43210, U.S.A., §Department of Cardiothoracic Surgery/Kaufman Center for Heart Failure, Cleveland Clinic Foundation, Cleveland, OH 44195, U.S.A., Department of Cardiology, Cleveland Clinic Foundation, Cleveland, OH 44195, U.S.A., and ¶Department of Pediatrics, College of Medicine, The Ohio State University, Columbus, OH 43210, U.S.A.

Key words: atrial fibrillation, electrophoresis, heart failure.

Abbreviation used: AF, atrial fibrillation.

¹To whom correspondence should be addressed (e-mail BauerJ@pediatrics.ohio-state.edu).

Cardiac myosin is a central participant in the cross-bridge cycling that mediates myocyte contraction and consists of multiple subunits that mediate both hydrolysis of ATP and mechanical production of contractile force Two isoforms of myosin heavy chain (MHC-a and MHC-b) are known to exist in mammalian cardiac tissue, and it is within this myosin subunit that ATPase activity resides. These isoforms differ by less than 0.2% in total molecular mass and amino acid sequence, but, strikingly, influence the rate and efficiency of energy utilization for generation of contractile force. Changes in the MHC-a/MHC-b ratio has been classically viewed as an adaptation of a failing myocyte in both animal models and humans; however, their measurement has traditionally required specialized preparations and materials for sufficient resolution. Here we describe a greatly simplified method for routine assessments of myosin isoform composition in human cardiac tissues. The primary advantages of our approach include higher throughput and reduced supply costs with no apparent loss of statistical power, reproducibility or achieved results. Use of this more convenient method may provide enhanced access to an otherwise specialized technique and could provide additional opportunity for investigation of cardiac myocyte adaptive changes.

Received 2 September 2002/22 October 2002; accepted 23 October 2002

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