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 3â,5âmonophosphate (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
AJP - Heart and Circulatory Physiology – The American Physiological Society
Published: May 1, 1978
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