Radioligand binding studies reveal marked species differences in the vasopressin V1 receptor of rat, rhesus and human tissues.
The [3H]arginine-vasopressin ([3H]AVP) binding site in rat, rhesus and human liver and nonpregnant human uterus was characterized and contrasted. [3H]AVP bound with high affinity (Ki values, 0.2-0.6 nM) to preparations of all tissues studied. Competition binding studies using a series of compounds from three structural classes indicate a marked species difference between the rat and primate liver AVP-V1 site. This site in rhesus and human liver however, is essentially identical, indicating that the rhesus liver is an appropriate surrogate for human tissue. These studies also indicate that the AVP-V1 site of nonpregnant human uterus and human liver is equivalent.
Pettibone
D J
DJ
Department of New Lead Pharmacology, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
Kishel
M T
MT
Woyden
C J
CJ
Clineschmidt
B V
BV
Bock
M G
MG
Freidinger
R M
RM
Veber
D F
DF
Williams
P D
PD
D000818:Animals; D001127:Arginine Vasopressin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001665:Binding Sites; D001667:Binding, Competitive; D005260:Female; D006801:Humans; D008099:Liver / Q000378:metabolism*; D008253:Macaca mulatta; D008297:Male; D009842:Oligopeptides / Q000378:metabolism; D011869:Radioligand Assay; D051381:Rats; D011919:Rats, Inbred Strains; D011945:Receptors, Angiotensin / Q000378:metabolism*; D017483:Receptors, Vasopressin; D013045:Species Specificity; D014599:Uterus / Q000378:metabolism*
D009842:Oligopeptides; D011945:Receptors, Angiotensin; D017483:Receptors, Vasopressin; D001127:Arginine Vasopressin