Role of cyclic AMP in rat aortic microsomal phosphorylation and calcium uptake

Role of cyclic AMP in rat aortic microsomal phosphorylation and calcium uptake of Anatomy, College of Medicine, RAMESH C., R. CLINTON DIWAN SINGH, TOMMY BROCK. Role of cyclic AMP in rat aortic microsomal phosphorylation calcium uptake. Am. J. Physiol. 234(5): H5WH514, 1978 or Am. J. Physiol.: Heart Circ. Physiol. 3(5): H50&H514, 1978. -The role of adenosine 3’,5’monophosphate (cyclic AMP)-dependent membrane phosphorylation in the regulation of microsomal calcium transport in rat aortic was studied. Cyclic AMP-dependent protein kinase augmented the phosphorylation of serine residues in a microsomal protein component with a molecular weight of about 44,000 (determined by sodium dodecyl sulfatepolyacrylamide gel electrophoresis) the majority of 32P incorporation was in serine residue(s). The phosphorylated protein had stability characteristics of a phosphoester. The phosphorylated substrate was not extracted from the trichloroacetic acid (TCA) precipitate with organic solvents or by suspension in hot TCA; the demonstrated hydroxylamine insensitivity suggested that the substrate was not lipid or nucleic acid. Intrinsic phosphoprotein phosphatase cleaved the labeled phosphate from the cyclic AMP-stimulated microsomes in the first 5 min of incubation. Microsomes phosphorylated in the presence of 1 PM cyclic AMP or 1 PM cyclic AMP plus 0.1 mg/ml protein kinase exhibited enhanced calcium uptake. We suggest that reversible phosphorylation of microsomal membranes may play an important http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Heart and Circulatory Physiology The American Physiological Society

Role of cyclic AMP in rat aortic microsomal phosphorylation and calcium uptake

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Publisher
The American Physiological Society
Copyright
Copyright © 1978 the American Physiological Society
ISSN
0363-6135
eISSN
1522-1539
Publisher site
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Abstract

of Anatomy, College of Medicine, RAMESH C., R. CLINTON DIWAN SINGH, TOMMY BROCK. Role of cyclic AMP in rat aortic microsomal phosphorylation calcium uptake. Am. J. Physiol. 234(5): H5WH514, 1978 or Am. J. Physiol.: Heart Circ. Physiol. 3(5): H50&H514, 1978. -The role of adenosine 3’,5’monophosphate (cyclic AMP)-dependent membrane phosphorylation in the regulation of microsomal calcium transport in rat aortic was studied. Cyclic AMP-dependent protein kinase augmented the phosphorylation of serine residues in a microsomal protein component with a molecular weight of about 44,000 (determined by sodium dodecyl sulfatepolyacrylamide gel electrophoresis) the majority of 32P incorporation was in serine residue(s). The phosphorylated protein had stability characteristics of a phosphoester. The phosphorylated substrate was not extracted from the trichloroacetic acid (TCA) precipitate with organic solvents or by suspension in hot TCA; the demonstrated hydroxylamine insensitivity suggested that the substrate was not lipid or nucleic acid. Intrinsic phosphoprotein phosphatase cleaved the labeled phosphate from the cyclic AMP-stimulated microsomes in the first 5 min of incubation. Microsomes phosphorylated in the presence of 1 PM cyclic AMP or 1 PM cyclic AMP plus 0.1 mg/ml protein kinase exhibited enhanced calcium uptake. We suggest that reversible phosphorylation of microsomal membranes may play an important

Journal

AJP - Heart and Circulatory PhysiologyThe American Physiological Society

Published: May 1, 1978

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