AJP - Cell Physiology, Vol 270, Issue 5 C1271-C1276, Copyright © 1996 by American Physiological Society

ARTICLES

Isoform-independent heart rate-related variation in cardiac myofibrillar Ca(2+)-activated Mg(2+)-ATPase activity

W. Rouslin and C. W. Broge
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Ohio 45267, USA.

In the present study, we compared the activities of the cardiac myofibrillar Ca(2+)-activated Mg(2+)-ATPase and the content of cardiac muscle mitochondrial ATPase inhibitor protein (IF1) of several mammalian species covering broad ranges of body mass and heart rate, i.e., from beef cattle to mouse. The cardiac myofibrillar ATPase from each species was assayed over a range of pCa values at pH 7.4. While the cardiac myofibrillar ATPase from all species examined showed essentially identical Ca2+ concentration dependencies with the ATPase in each species activating steeply between pCa 6.5 and 5.5, the maximal ATPase specific activity reached varied considerably from species to species, and this variation was largely independent of the predominant cardiac myosin ATPase isoform present. Thus, while adult beef cattle, pig, dog, and rabbit all contain predominantly the slow cardiac myosin ATPase isoform the cardiac myofibrillar ATPase specific activities of these four species varied over approximately a fourfold range. Moreover, there was a fairly smooth curvilinear relationship between maximum Ca(2+)-activated myofibrillar ATPase activity and median conscious heart rate for the slow cardiac myosin ATPase-possessing species examined. This smooth continuum also extended to include two species possessing the fast cardiac myosin ATPase isoform, rat and mouse. This relationship between myofibrillar ATPase activity and heart rate that appears to be applicable to a broad range of species suggests that the myofibrillar ATPase is specifically modeled or fine-tuned to the kinetic (heart rate) demand of each species and, within slow and fast heart rate ranges, is essentially independent of myosin ATPase isoform per se. Only hearts containing predominantly the slow myosin ATPase isoform contained functional levels of IF1. Finally, while it has been reported that the ratio of myosin Ca(2+)-ATPase to actomyosin Mg(2+)-ATPase activity is a good index of the percent of the fast myosin ATPase in rabbit myofibrillar preparations, we found that this relationship may be applicable to only some species.

This article has been cited by other articles:

				K. Ito, X. Yan, M. Tajima, Z. Su, W. H. Barry, and B. H. Lorell Contractile Reserve and Intracellular Calcium Regulation in Mouse Myocytes From Normal and Hypertrophied Failing Hearts Circ. Res., September 29, 2000; 87(7): 588 - 595. [Abstract] [Full Text] [PDF]