发现血管紧张素II（3-8）的一个独特结合位点，一种假定的血管紧张素IV受体。

Discovery of a distinct binding site for angiotensin II (3-8), a putative angiotensin IV receptor.

作者信息

Swanson G N, Hanesworth J M, Sardinia M F, Coleman J K, Wright J W, Hall K L, Miller-Wing A V, Stobb J W, Cook V I, Harding E C

机构信息

Department of Veterinary and Comparative Anatomy, Washington State University, Pullman 99164-6520.

出版信息

Regul Pept. 1992 Aug 13;40(3):409-19. doi: 10.1016/0167-0115(92)90527-2.

DOI:10.1016/0167-0115(92)90527-2

PMID:1438983

Abstract

We report here the discovery of a unique and novel angiotensin binding site and peptide system based upon the C-terminal 3-8 hexapeptide fragment of angiotensin II (NH3(+)-Val-Tyr-Ile-His-Pro-Phe-COO-) (AII(3-8) (AIV)). This fragment binds saturably, reversibly, specifically, and with high affinity to membrane-binding sites in a variety of tissues and from many species. The binding site is pharmacologically distinct from the classic angiotensin receptors (AT1 or AT2) displaying low affinity for the known agonists (AII and AIII) and antagonist (Sar1,Ile8-AII). Although a definitive function has not been assigned to this system in many of the tissues in which it resides, AIV's interaction with endothelial cells may involve a role in endothelial cell-dependent vasodilation. Consequent to this action, AIV is a potent stimulator of renal cortical blood flow.

摘要

我们在此报告基于血管紧张素II（NH3(+)-Val-Tyr-Ile-His-Pro-Phe-COO-）（AII(3-8)（AIV））的C末端3-8六肽片段发现了一种独特且新颖的血管紧张素结合位点和肽系统。该片段可饱和、可逆、特异性且高亲和力地结合多种组织和许多物种的膜结合位点。该结合位点在药理学上与经典血管紧张素受体（AT1或AT2）不同，对已知激动剂（AII和AIII）和拮抗剂（Sar1，Ile8-AII）显示出低亲和力。尽管在其所在的许多组织中尚未确定该系统的明确功能，但AIV与内皮细胞的相互作用可能在内皮细胞依赖性血管舒张中起作用。基于此作用，AIV是肾皮质血流的强效刺激剂。