Angiotensin-(1-7) is a novel peptide of the renin-angiotensin system t
hat counteracts the presser and proliferative responses to angiotensin
II. We now report that cultured bovine aortic endothelial cells conta
in a saturable, high-affinity [I-125]angiotensin-(1-7) binding site wi
th an affinity of 19.3 +/- 10.7 nmol/L and a density of 1351 +/- 710 f
mol/mg protein. Angiotensin-(1-7) competed at a second lower-affinity
site, with an IC50 of 2.9 mu mol/L. The high-affinity angiotensin II r
eceptor antagonist sarcosine(1)-isoleucine(8)-angiotensin II blocked [
I-125]angiotensin-(1-7) binding to bovine aortic endothelial cells at
both a high- (IC50 = 1.3 nmol/L) and a low-affinity (IC50 = 6.2 mu mol
/L) binding site. In contrast, D-alanine(7)-angiotensin-(1-7) complete
ly blocked [I-125]angiotensin-(1-7) binding, with an IC50 of 19.8 nmol
/L, suggesting that D-alanine(7)-angiotensin-(1-7) may selectively blo
ck responses to angiotensin-(1-7) in endothelial cells.