Yoshioka Kazuaki, Nakata Hiroyasu
Department of Molecular Cell Signaling, Tokyo Metropolitan Institute for Neuroscience, Tokyo, Japan.
J Pharmacol Sci. 2004 Feb;94(2):88-94. doi: 10.1254/jphs.94.88.
Adenosine A(1) receptors (A(1)R) are able to form a heteromeric complex with P2Y(1) receptors (P2Y(1)R) that generates A(1)R with P2Y(1)R-like agonistic pharmacology. A potent P2Y(1)R agonist, adenosine 5'-O-(2-thiotriphosphate), binds the A(1)R binding pocket of the A(1)R/P2Y(1)R complex and inhibits adenylyl cyclase activity via G(i/o) protein. These mechanisms might be used to fine-tune purinergic inhibition locally at sites where there is a particular oligomerization structure between purinergic receptors and explain the undefined purinergic functions by adenosine and adenine nucleotides.
腺苷A(1)受体（A(1)R）能够与P2Y(1)受体（P2Y(1)R）形成异源复合物，从而产生具有类似P2Y(1)R激动剂药理学特性的A(1)R。一种强效的P2Y(1)R激动剂，腺苷5'-O-(2-硫代三磷酸)，结合A(1)R/P2Y(1)R复合物的A(1)R结合口袋，并通过G(i/o)蛋白抑制腺苷酸环化酶活性。这些机制可能用于在嘌呤能受体之间存在特定寡聚化结构的部位对嘌呤能抑制进行局部微调，并解释腺苷和腺嘌呤核苷酸未明确的嘌呤能功能。
