Abstract

In synaptosomal membranes from rat cerebellum, additive responses to adenylate cyclase activity are observed between the beta adrenergic receptors present on the Purkinje cells and the adenosine A-1 receptors or gamma-aminobutyric acid B (GABAB) receptors, which are both associated with the granule cells. In contrast, nonadditive responses are found with the activation of the adenosine A-1 and the GABAB receptors. Because both receptors are mainly associated with the same cell type, the nonadditive response indicates an interaction between the adenosine A-1, GABAB receptors and the adenylate cyclase. The present study suggests that the nonadditivity results from a limited number of adenylate cyclase catalytic units, which both receptor systems share. This conclusion was derived indirectly by showing that 1) a GABAB agonist did not affect the adenosine A-1 recognition site; 2) both receptors additively activated the high-affinity guanosine 5'-triphosphatase, which is believed to reflect the activation of the inhibitory guanine nucleotide unit; and 3) the nonadditivity was still observed after stimulation of adenylate cyclase activity with forskolin.