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Am J Physiol Heart Circ Physiol 283: H958-H965, 2002; doi:10.1152/ajpheart.00078.2002
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Vol. 283, Issue 3, H958-H965, September 2002

Altered dose response to beta -agonists in SERCA1a-expressing hearts ex vivo and in vivo

Sabine Huke1, Vikram Prasad1, Michelle L. Nieman2, Kalpana J. Nattamai1, Ingrid L. Grupp3, John N. Lorenz2, and Muthu Periasamy1

1 Department of Physiology and Cell Biology, Ohio State University College of Medicine and Public Health, Columbus 43210; and Departments of 2 Molecular and Cellular Physiology and 3 Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267

H965, 2002; 10.1152/ajpheart.00078.2002. ---In this study we evaluated the contractile characteristics of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)1a-expressing hearts ex vivo and in vivo and in particular their response to beta -adrenergic stimulation. Analysis of isolated, work-performing hearts revealed that transgenic (TG) hearts develop much higher maximal rates of contraction and relaxation than wild-type (WT) hearts. Addition of isoproterenol only moderately increased the maximal rate of relaxation (+20%) but did not increase contractility or decrease relaxation time in TG hearts. Perfusion with varied buffer Ca2+ concentrations indicated an altered dose response to Ca2+. In vivo TG hearts displayed fairly higher maximal rates of contraction (+ 25%) but unchanged relaxation parameters and a blunted but significant response to dobutamine. Our study also shows that the phospholamban (PLB) level was decreased (-40%) and its phosphorylation status modified in TG hearts. This study clearly demonstrates that increases in SERCA protein level alter the beta -adrenergic response and affect the phosphorylation of PLB. Interestingly, the overall cardiac function in the live animal is only slightly enhanced, suggesting that (neuro)hormonal regulations may play an important role in controlling in vivo heart function.

transgenic mice; contractility; sarco(endo)plasmic reticulum calcium adenosinetriphosphatase; phospholamban


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