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Identification of atypical (non‐AT 1 , non‐AT 2 ) angiotensin binding sites with high affinity for angiotensin I on IEC‐18 rat intestinal epithelial cells
Author(s) -
Smith Roger D.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01039-h
Subject(s) - angiotensin ii , chemistry , renin–angiotensin system , angiotensin 1 , identification (biology) , angiotensin receptor , endocrinology , biology , biochemistry , receptor , blood pressure , botany
Specific high‐affinity ( Kd = 3.4 nM) binding sites for 125 I‐labelled angiotensin I ([ 125 I]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 AT 1 ‐ and AT 2 ‐specific angiotensin receptor antagonists, The rank order of potency with which various angiotensin peptides inhibited[ 125 I]Ang I binding to the cells (Ang I ≥ Ang II > Ang(1–7) > [Sar 1 ,Ile 8 ]‐Ang II > Ang(3–8) > Ang III) also distinguishes these sites from AT 1 and AT 2 angiotensin receptors.