B2-kinin receptor like binding in rat glomerular membranes.
Incubation of a radiolabeled bradykinin analog, [125I]-Tyr8-BK with a crude membrane preparation obtained from isolated rat glomeruli revealed a time dependent binding. The binding was saturable, reversible and was a linear function of protein membrane concentration. The radiolabeled Tyr8-BK bound to a single class of binding sites with an equilibrium dissociation constant (KD) of 3.9 +/_ 0.7 nM and a density (Bmax) of 31 +/- 5 fmol/mg protein. The BK-receptor complex was not affected by angiotensin II or by arginine vasopressin and atrial natriuretic factor. BK binding was reversed by bradykinin (Ki = 0.3 10(-9) M), and by other kinin analogs in the following order of potency: Lys-BK, Met-Lys-BK, Thi5,8-D Phe7-BK. However, Des-Arg9-BK had no effect on binding of the radiolabelled BK. These results are consistent with the presence of a B2-kinin like receptor in rat glomeruli.
Bascands
J L
JL
INSERM U 133, Toulouse, France.
Pécher
C
C
Cabos
G
G
Girolami
J P
JP
D000818:Animals; D001667:Binding, Competitive; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D007678:Kidney Glomerulus / Q000378:metabolism*; D007700:Kinetics; D051381:Rats; D011919:Rats, Inbred Strains; D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter / Q000378:metabolism*
D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter; C026201:bradykinin, Tyr-; D001920:Bradykinin