Adenosine analogs inhibit adipocyte adenylate cyclase by a GTP-dependent process: basis for actions of adenosine and methylxanthines on cyclic AMP production and lipolysis.

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Abstract
Adenylate cyclase in purified membranes from rat adipocytes is inhibited by low concentrations of purine-modified adenosine analogs, particularly those modified in the N6 position. Such inhibition is antagonized competitively by methylxanthines, but not by other cyclic nucleotide phosphodiesterase inhibitors, and it is dependent on inhibitory concentrations of GTP in the assay medium. Ribose-modified adenosine analogs inhibit adenylate cyclase through a process that is neither dependent on the GTP concentration nor antagonized by methylxanthines. The potent effects of adenosine and methylxanthines on fat cell metabolism were explained and the importance of GTP in mediating inhibition by agents that act at cell surface receptors was demonstrated.

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