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Phorbol ester treatment impairs hormone‐ but not stable GTP analog‐induced inhibition of adenylate cyclase
Author(s) -
Bauer Silvia,
Jakobs Karl H.
Publication year - 1986
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(86)81181-4
Subject(s) - gtp' , adenylate kinase , cyclase , guanosine , phorbol ester , chemistry , g protein , phorbol , guanosine triphosphate , biochemistry , protein kinase c , receptor , signal transduction , enzyme
Treatment of intact human platelets and S49 lymphoma cyc − cells with the phorbol ester, 12‐ O ‐tetradecanoylphorbol‐13‐acetate, impairs GTP‐dependent and hormone‐induced inhibition of adenylate cyclase, an action mediated by the inhibitory coupling protein N i . In contrast, receptor‐independent activation of N i with subsequent adenylate cyclase inhibition induced by the stable GTP analog, guanosine 5'‐[γ‐thio]triphosphate, was affected in neither the potency nor onset of N i activation by the stable GTP analog, in both membrane systems studied. The data indicate that modification of N i following phorbol ester treatment does not impair its activation by stable GTP analogs.