Adenosine 3', 5'-Monophosphate-Dependent Membrane Phosphorylation
- 1 August 1974
- journal article
- research article
- Published by Wolters Kluwer Health in Circulation Research
- Vol. 35 (2), 298-306
- https://doi.org/10.1161/01.res.35.2.298
Abstract
The role of cyclic adenosine 3', 5'-monophosphate (AMP) in the control of microsomal calcium ion (Ca2+) transport was studied in microsomes prepared from rabbit heart. These cardiac microsomes contained intrinsic cyclic AMP-dependent protein kinase activity that phosphorylated serine residues in a microsomal protein component with a molecular weight of about 20,000 (determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Intrinsic phosphoprotein phosphatase activity of the microsomal membranes resulted in rapid dephosphorylation of these residues. Microsomes phosphorylated in the presence of 1 x 10-6M cyclic AMP exhibited enhanced Ca2+ uptake. We conclude that reversible phosphorylation of microsomal membranes may be an important mechanism for regulation of microsomal Ca2+ transport by cyclic AMP.Keywords
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