PMID: 6107815Oct 1, 1980Paper

The relationship between somatostatin binding and cyclic AMP-stimulated protein kinase inhibition

Metabolism: Clinical and Experimental
J W LeitnerK E Sussman

Abstract

Somatostatin binding and the ability to inhibit cyclic AMP stimulated protein kinase were investigated utilizing isolated pancreatic islets, anterior pituitary plasma membranes, adipocytes, erythrocyte ghosts, hepatic plasma membranes, and anterior pituitary secretion vesicles. Three types of response were observed. With type I response, somatostatin bound specifically to pancreatic islets and anterior pituitary secretion vesicles and inhibited cyclic AMP stimulated protein kinase. In type II response, adipocytes and anterior pituitary plasma membranes exhibited somatostatin binding but no effect of the ligand on the kinase. In erythrocyte membrane ghosts and hepatic plasma membranes, there was neither specific somatostatin binding nor protein kinase inhibition (type III response). The absence of somatostatin binding in erythrocytes or hepatic plasma membranes cannot be explained by degradation of the ligand per se. Secretory vesicles isolated from the anterior pituitary gland bind somatostatin with an average affinity which exceeds that observed in plasma membrane (for pituitary secretory vesicles Kd1 = 8.5 X 10(-8)M, Kd2 = 5.2 X 10(-7)M; for pituitary membranes Kd1 = 1.9 X 10(-8)M, Kd2 = 8.1 X 10(-7)M). The molar concentratio...Continue Reading

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Citations

Apr 1, 1986·Neurochemical Research·R E CatalanM D Aragones
Nov 1, 1987·Regulatory Peptides·V BarriosE Arilla
Dec 1, 1988·Regulatory Peptides·M A SimónC Calle
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Sep 1, 1982·Metabolism: Clinical and Experimental·K E SussmanP S Mehler
Jun 1, 1983·The American Journal of Physiology·A D CherringtonK E Steiner

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