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Regulation of [ 3 H]forskolm binding to human platelet membranes by GppNHp, NaF, and prostaglandin E 1
Author(s) -
Nelson Carol A.,
Seamon Kenneth B.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80808-5
Subject(s) - forskolin , adenylate kinase , cyclase , binding site , chemistry , prostaglandin e1 , membrane , prostaglandin , nucleotide , endocrinology , biochemistry , biology , receptor , gene
Displaceable binding of [ 3 H]forskolin to human platelet membranes can be detected in the presence of magnesium. There is an increase in the number of [ 3 H]forskolin binding sites when membranes are incubated with GppNHp or NaF in the presence of magnesium. Prostaglandin E 1 , which stimulates human platelet adenylate cyclase, does not affect the binding of [ 3 H]forskolin in the absence of GppNHp. However, the dose‐response curve for the GppNHp‐dependent increase in [ 3 H]forskolin binding sites is shifted to lower concentrations in the presence of prostaglandin E 1 . Prostaglandin E 1 potentiates the effect of GppNHp on [ 3 H]forskolin binding most likely by facilitating the binding of the guanine nucleotide at the stimulatory quanine nucleotide regulatory protein of adenylate cyclase.