Abstract

other. Each group shows marked sequence similarities in their putative transmembrane spanning regions, whereas the two groups are structurally different from each other. Operational information suggests a similar subdivision, since the pharmacological profiles of SSTRliSSTR4 receptors (virtually no affinity for octreotide, seglitide, RC 160) are markedly different from the profiles of SSTR2/SSTR-3/SSTR-5 receptors (intermediate to very high affinity for these compounds). The previously termed SS1 or SRIF-1 receptors correspond to the SSTR-2 receptors, whereas the SSTR-1 receptor is equivalent to SS-2 and presumably to SRIF-2 receptors (both initially defined by their lack of afIinity for octreotide and seglitide). Transductional information shows that all 5 cloned receptors couple negatively to adenylyl cyclase activity. Since all cloned receptors have similarly high affinity for SRIF14 and -28, the following nomenclature can be proposed: 3 subtypes of SRIF-1 (lA, lB, 1C) receptors (SSTR-2, -5 and -3) and 2 subtypes of SRIF-2 (2A, 2B) receptors (SSTR-1 and -4). Operational, structural and transductional data in support of the present proposal, as well as brain distribution of the different receptors wilI be presented.

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