Identifies a novel, atypical angiotensin binding site on rat intestinal epithelial cells that is distinct from classical AT1 and AT2 receptors.
Does not yet alter clinical renin-angiotensin therapies; leaves open a novel non-AT1/AT2 binding site on intestinal epithelium.
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.
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Roger Smith (1995) studied this question.
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