Characteristics of high-affinity [3H]adenosine binding to rat brain synaptosomes and turkey erythrocyte membranes.
High affinity binding sites for [3H]adenosine in rat brain and in turkey erythrocytes can be identified by binding experiments. Displacement experiments using a number of adenosine analogs indicate that these high affinity sites do not represent the R-type adenosine receptors which mediate activation of adenylate cyclase, although the binding is theophylline sensitive. Similarly, the binding of [3H]adenosine is not to the P-site, which mediates inhibition of adenylate cyclase, since the high affinity binding persists in the presence of 2',5'-dideoxyadenosine. Furthermore, these results remain qualitatively similar also in the presence of dipyridamole which blocks adenosine transport sites. We conclude that theophylline sensitivity does not indicate that [3H]adenosine binding sites correspond to adenosine receptors coupled to adenylate cyclase.
D000241:Adenosine / Q000378:metabolism*; D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism*; D007700:Kinetics; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011983:Receptors, Purinergic; D013574:Synaptosomes / Q000378:metabolism*; D014018:Tissue Distribution; D014316:Tritium; D014422:Turkeys
D011956:Receptors, Cell Surface; D011983:Receptors, Purinergic; D014316:Tritium; D000241:Adenosine