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Adenylate cyclase inhibition and GTPase stimulation by somatostatin in S49 lymphoma cyc − variants are prevented by islet‐activating protein
Author(s) -
Aktories Klaus,
Schultz Günter,
Jakobs Karl H.
Publication year - 1983
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(83)80701-7
Subject(s) - cyclase , adenylate kinase , gtp' , somatostatin , gtpase , gtp binding protein regulators , g protein , chemistry , guanine , nucleotide , stimulation , biochemistry , biology , medicine , endocrinology , enzyme , signal transduction , gene
cyc − ‐Variants of S49 lymphoma cells are defective in the stimulatory guanine nucleotide site of the adenylate cyclase but contain an inhibitory site. Treatment of cyc − cells with islet‐activating protein (IAP), which causes ADP‐ribosylation of an M r 40 000 polypeptide in cyc − membranes, abolishes adenylate cyclase inhibition by GTP and the peptide hormone, somatostatin, but not that induced by GTPγS. Furthermore, somatostatin‐induced stimulation of GTP hydrolysis is lost. Thus, the data indicate that IAP interferes with the adenylate cyclase system by an action at the inhibitory guanine nucleotide site.