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    Adenylate cyclase activity in platelet membrane preparations was measured in the presence of prostaglandin E1 (PGE1), GTP and a non-hydrolysable analogue of GDP, guanosine 5'-[beta-thio]diphosphate (GDP[beta S]). A dose-dependent inhibition of adenylate cyclase by GDP[beta S] was observed that could be reversed either by adding increased amounts of GTP or of PGE1.
    Prostaglandin E1
    Guanosine diphosphate
    BETA (programming language)
    Citations (13)
    Guanine nucleotides are successfully used in the studies of regulatory N-proteins coupled with adenylate cyclase. In the present work N-chloroacetylhydrazones of oxo-GTP and oxo-GDP are described. After 4 hr preincubation of these nucleotides with plasma membranes from bovine brain caudate nucleus, the ability of adenylate cyclase to be activated by guanylyl-5'-methylene-diphosphonate is blocked. The degree of inhibition depends on preincubation time and increases in the presence of Mg2+. Guanylyl-5'-methylenediphosphonate protects adenylate cyclase from the action of N-chloroacetylhydrazone of oxo-GTP. These findings suggest that adenylate cyclase activation is diminished as a result of covalent modification of the Ns. N-chloroacetyl-hydrazone of oxo-GDP also causes a loss of the adenylate cyclase sensitivity to the fluoride ion and cholera toxin.
    Cholera toxin
    Citations (0)
    A hypothesis on the role of the hormone-induced desensitization of adenylate cyclase is proposed. It is suggested that the desensitization process could provide the cell with a highly efficient cyclic AMP system for transmitting hormone stimulus without requiring a large energy consumption. Theoretical considerations show that in fact the desensitization phenomenon allows the cyclic AMP system to present a good compromise between the efficiency and economy requirements of the cells.
    Stimulus (psychology)
    Citations (25)
    Adenylate cyclase activity was measured in suspensions of E. coli B, rendered permeable with toluene. The enzyme was activated in a dose‐dependent manner by GTP and by its non‐hydrolysable analogue, GTP[γS]. In contrast, incubation with GDP[βS], a non‐phosphorylatable analogue of GDP, caused a dose‐related inhibition of adenylate cyclase; this was partially overcome by addition of GTP. GTP did not relieve, and GDP[βS] augmented, the non‐competitive and dose‐related inhibition of E.coli adenylate cyclase by glucose.
    Guanosine diphosphate