在IEC-18大鼠肠上皮细胞上鉴定对血管紧张素I具有高亲和力的非典型（非AT1、非AT2）血管紧张素结合位点。

Identification of atypical (non-AT1, non-AT2) angiotensin binding sites with high affinity for angiotensin I on IEC-18 rat intestinal epithelial cells.

作者信息

Smith R D

机构信息

Department of Clinical Biochemistry, Addenbrooke's Hospital, Cambridge, UK.

出版信息

FEBS Lett. 1995 Oct 16;373(3):199-202. doi: 10.1016/0014-5793(95)01039-h.

DOI:10.1016/0014-5793(95)01039-h

PMID:7589465

Abstract

Specific high-affinity (Kd = 3.4 nM) binding sites for 125I-labelled angiotensin I ([125I]Ang I) were identified on an epithelial cell line (IEC-18) derived from the rat small intestine. The sites, which also have high affinity for Ang II, are insensitive to both AT1- and AT2-specific angiotensin receptor antagonists. The rank order of potency with which various angiotensin peptides inhibited [125I]Ang I binding to the cells (Ang I > or = Ang II > Ang(1-7) > [Sar1,Ile8]-Ang II > Ang(3-8) > Ang III) also distinguishes these sites from AT1 and AT2 angiotensin receptors.

摘要

在源自大鼠小肠的上皮细胞系（IEC - 18）上鉴定出了针对125I标记的血管紧张素I（[125I]Ang I）的特异性高亲和力（Kd = 3.4 nM）结合位点。这些位点对血管紧张素II也具有高亲和力，对AT1和AT2特异性血管紧张素受体拮抗剂均不敏感。各种血管紧张素肽抑制[125I]Ang I与细胞结合的效力排序（血管紧张素I≥血管紧张素II＞血管紧张素（1 - 7）＞[Sar1，Ile8] - 血管紧张素II＞血管紧张素（3 - 8）＞血管紧张素III）也将这些位点与AT1和AT2血管紧张素受体区分开来。