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2',3'‐Dialdehyde of GTP blocks regulatory functions of adenylate cyclase N s protein
Author(s) -
Skurat Alexander V.,
Yurkova Maria S.,
Khropov Yuri V.,
Bulargina Tamara V.,
Severin Eugene S.
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)80893-0
Subject(s) - adenylate kinase , cyclase , gtp' , forskolin , caudate nucleus , chemistry , membrane , stimulation , biochemistry , enzyme , biophysics , biology , receptor , endocrinology
Preincubation of bovine caudate nucleus membranes with the 2',3'‐dialdehyde of GTP (oGTP) reduces adenylate cyclase activation by guanylyl imidodiphosphate (GppNHp) in a time‐dependent fashion. A slower rate of inhibition is observed if membranes are treated with both GTP and oGTP. The efficacy of oGTP action is enhanced by raising the Mg 2+ concentration. Reduction of adenylate cyclase sensitivity to GppNHp is followed by an irreversible decrease of enzyme stimulation by forskolin. Addition of a Lubrol soluble preparation from guinea pig lung membranes to oGTP‐treated caudate nucleus membranes causes restoration of the adenylate cyclase sensitivity to GppNHp. These data suggest that oGTP blocks the GTP‐binding site of the adenylate cyclase system localized on the N s protein. Such modification leads to the elimination of the N s ‐mediated regulation of the enzyme.