B2 bradykinin receptor-like binding in rat renomedullary interstitial cells.
A particulate fraction from cultured rat renomedullary interstitial cells (RRIC) was prepared for bradykinin (BK) binding studies. Incubation of three radiolabeled BK analogs, [125I-Tyr1]kallidin, [125I-Tyr5]-BK, and [125I-Tyr8]-BK, with the particulate fraction resulted in degradation of these peptides. Assay conditions which prevented hydrolysis of these radiolabeled kinins were determined. Under these conditions, direct binding studies were performed with [125I-Tyr1]kallidin (TlK) as the radioligand. BK binding affinity, apparent Kassoc. = 1.3 X 10(9) M-1, and specificity, determined with 51 BK analogs, were consistent with those expected of a B2 BK receptor.
Fredrick
M J
MJ
Abel
F C
FC
Rightsel
W A
WA
Muirhead
E E
EE
Odya
C E
CE
D000818:Animals; D001920:Bradykinin / Q000031:analogs & derivatives / Q000378:metabolism*; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D007679:Kidney Medulla / Q000378:metabolism*; D051381:Rats; D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter / Q000032:analysis*
D007457:Iodine Radioisotopes; D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter; D001920:Bradykinin