Solubilization of oxytocin receptors in porcine renal LLC-PK1 cell membranes.
The present studies were undertaken to better characterize the pharmacological properties of oxytocin receptors (OTRs) of the porcine kidney cell line, LLC-PK1, in their natural membranous environment and after solubilization. In intact membranes, binding of a selective radioligand was rapid, reversible, saturable, and of high affinity. High-affinity agonist binding was reduced by a GTP analogue, suggesting that these OTRs are associated with G-protein(s). After solubilization with the zwitterionic detergent CHAPSO, OTRs retained their high affinity for the radioligand and rank order potency for oxytocin analogues, and agonist binding remained biphasic and GTP sensitive.
Flanagan-Cato
L M
LM
Department of Psychology, University of Pennsylvania, Philadelphia 19104, USA.
Moga
C N
CN
Fluharty
S J
SJ
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002793:Cholic Acids; D019204:GTP-Binding Proteins / Q000378:metabolism; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D007700:Kinetics; D018374:LLC-PK1 Cells; D010121:Oxytocin / Q000031:analogs & derivatives / Q000378:metabolism; D018045:Receptors, Oxytocin / Q000737:chemistry* / Q000187:drug effects; D012995:Solubility; D013552:Swine
D002793:Cholic Acids; D018045:Receptors, Oxytocin; C101067:oxytocin, 1-d(CH2)5-(2-O-methyl)Tyr-Thr(4)-Orn(8)-Tyr-NH2(9)-; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D010121:Oxytocin; C048531:chapso; D019204:GTP-Binding Proteins