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Phorbol ester induces loss of VIP stimulation of adenylate cyclase and VIP‐binding sites in HT29 cells
Author(s) -
Bozou Jean-Claude,
Couvineau Alain,
Rouyer-Fessard Christiane,
Laburthe Marc,
Vincent Jean-Pierre,
Kitabgi Patrick
Publication year - 1987
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(87)81426-6
Subject(s) - adenylate kinase , forskolin , cyclase , cholera toxin , vasoactive intestinal peptide , protein kinase c , stimulation , receptor , protein kinase a , medicine , phorbol , endocrinology , chemistry , biology , microbiology and biotechnology , biochemistry , kinase , neuropeptide
Treatment of HT29 cells with the tumor promoting phorbol ester PMA resulted in an attenuation of VIP‐stimulated cAMP production in intact cells and VIP‐stimulated adenylate cyclase activity in cell membranes. PMA did not decrease the ability of cholera toxin and forskolin to elevate cAMP levels in intact cells. Fluoride‐stimulated adenylate cyclase activity in HT29 cells homogenates was not affected byPMA. The maximal VIP binding capacity of homogenates prepared from HT29 cells treated with PMA was decreased by 50%. It is concluded that protein kinase C regulates VIP receptor function possibly through phosphorylation of the VIP receptor.