title: Vasopressin receptors in human seminal vesicles: identification, pharmacologic characterization, and comparison with the vasopressin receptors present in the human kidney.
abstract: Because of the presence of a high density of vasopressin receptors in the epithelial cells of porcine seminal vesicles similar to the V2 vasopressin receptors of renal tubules, human seminal vesicles and kidney were investigated using quantitative binding and adenylate cyclase studies. Tissues were obtained at surgery from 17 patients with urologic diseases. A homogeneous class of vasopressin binding sites have been found in both seminal vesicles and renal medulla. However, the vasopressin receptors present in these tissues are different in terms of ligand specificity and adenylate cyclase activation. In seminal vesicles, the V1 vasopressin antagonist d(CH2)5 TyrMeAVP is 36-fold, more potent than the V2 agonist dVDAVP in displacing [3H]AVP binding, while in the medullopapillary portion of kidney dVDAVP is 24-fold, more selective than d(CH2)5 TyrMeAVP for the arginine vasopressin binding site. Furthermore, arginine vasopressin induces a dose-dependent increase in adenylate cyclase activity in renal membranes, while it was ineffective in seminal vesicle membranes. These results indicate that a very high affinity (0.2 nM), low capacity (14 fmoles/mg protein) class of vasopressin receptors is present in human seminal vesicles, having pharmacologic characteristics similar to the V1 subtype of vasopressin receptors. The presence of a high affinity (1.6 nM), high capacity (350 fmoles/mg protein) V2 subtype of vasopressin receptors in human renal membranes is also confirmed. The density of the vasopressin receptors present in human seminal vesicles is inversely correlated with patient age, consistent with a physiologic role for vasopressin in the regulation of accessory sex gland activity.
authors.affiliation: Department of Clinical Physiopathology, University of Florence, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Maggi
authors.forename: E
authors.initials: E
authors.lastname: Baldi
authors.forename: A D
authors.initials: AD
authors.lastname: Genazzani
authors.forename: S
authors.initials: S
authors.lastname: Giannini
authors.forename: A
authors.initials: A
authors.lastname: Natali
authors.forename: A
authors.initials: A
authors.lastname: Costantini
authors.forename: D
authors.initials: D
authors.lastname: Rodbard
authors.forename: M
authors.initials: M
authors.lastname: Serio
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism*; D000367:Age Factors; D000368:Aged; D001127:Arginine Vasopressin / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D001667:Binding, Competitive; D002462:Cell Membrane / Q000032:analysis / Q000378:metabolism; D003894:Deamino Arginine Vasopressin / Q000031:analogs & derivatives / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D006801:Humans; D007679:Kidney Medulla / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D008297:Male; D008875:Middle Aged; D010121:Oxytocin / Q000378:metabolism; D011945:Receptors, Angiotensin / Q000032:analysis* / Q000378:metabolism; D017483:Receptors, Vasopressin; D012669:Seminal Vesicles / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D011945:Receptors, Angiotensin; D017483:Receptors, Vasopressin; D001127:Arginine Vasopressin; D010121:Oxytocin; C007223:vasopressin, 1-deamino-4-Val-8-Arg-; C025043:vasopressin, 1-(1-mercaptocyclohexaneacetic acid)-2-(O- methyl-L-tyrosine)-8-L-arginine-; D000262:Adenylyl Cyclases; D003894:Deamino Arginine Vasopressin