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Am J Physiol Heart Circ Physiol 277: H474-H480, 1999;
0363-6135/99 $5.00
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Vol. 277, Issue 2, H474-H480, August 1999

Human heart failure: cAMP stimulation of SR Ca2+-ATPase activity and phosphorylation level of phospholamban

Ulrich Schmidt1, Roger J. Hajjar2, Catherine S. Kim1, Djamel Lebeche1, Angelia A. Doye3, and Judith K. Gwathmey1

1 Integrated Physiology Research Laboratories, Cardiovascular Division, Department of Cardiovascular Medicine and Evans Department of Medicine, Boston University School of Medicine and the Whitaker Cardiovascular Institute, Boston 02118; 2 Massachusetts General Hospital, Boston 02114; and 3 The Institute for Cardiovascular Diseases and Muscle Research, Cambridge, Massachusetts 02138

Failing human myocardium has been associated with decreased sarcoplasmic reticulum (SR) Ca2+-ATPase activity. There remains controversy as to whether the regulation of SR Ca2+-ATPase activity is altered in heart failure or whether decreased SR Ca2+-ATPase activity is due to changes in SR Ca2+-ATPase or phospholamban expression. We therefore investigated whether alterations in cAMP-dependent phosphorylation of phospholamban may be responsible for the reduced SR Ca2+-ATPase activity in human heart failure. Protein levels of phospholamban and SR Ca2+-ATPase, detected by Western blot, were unchanged in failing compared with nonfailing human myocardium. There was decreased responsiveness to the direct activation of the SR Ca2+-ATPase activity by either cAMP (0.01-100 µmol/l) or protein kinase A (1-30 µg) in failing myocardium. Using the backphosphorylation technique, we observed a decrease of the cAMP-dependent phosphorylation level of phospholamban by 20 ± 2%. It is concluded that the impaired SR function in human end-stage heart failure may be due, in part, to a reduced cAMP-dependent phosphorylation of phospholamban.

human myocardium; calcium ion; sarcoplasmic reticulum; calcium ion-adenosinetriphosphatase; phospholamban ; adenosine 3',5'-cyclic monophosphate


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