title: Vasopressin antisense peptide interactions with the V1 receptor.
abstract: The molecular recognition hypothesis, that peptide ligands and their receptor binding sites are encoded by complementary nucleotide sequences, was tested for arginine vasopressin (AVP) and its V1 receptor. Binding of [125I] [d(CH2)5,Sar7]AVP (a selective V1 vasopressin antagonist radioligand) or [3H]AVP to rat liver plasma membranes was inhibited by peptides known to bind to V1 receptors but not by the AVP complementary peptide (Ser-Ser-Trp-Ala-Val-Leu-Glu-Val-Ala) (PVA). Rabbit anti-PVA antibodies were nonimmunoreactive with any protein in rat liver membranes or in a partially purified preparation from rat liver containing reconstitutable vasopressin binding activity. Furthermore, there was no suppression of the AVP pressor effect by PVA in vivo using a rat blood pressure bioassay. These findings do not support the hypothesis that the V1 receptor binding site is encoded by the antisense DNA strand to AVP.
authors: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australia.
authors: J M
authors: JM
authors: Kelly
authors: D
authors: D
authors: Trinder
authors: P A
authors: PA
authors: Phillips
authors: D J
authors: DJ
authors: Casley
authors: B
authors: B
authors: Kemp
authors: V
authors: V
authors: Mooser
authors: C I
authors: CI
authors: Johnston
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D015151:Immunoblotting; D008099:Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D051381:Rats; D011945:Receptors, Angiotensin / Q000302:isolation & purification / Q000378:metabolism*; D017483:Receptors, Vasopressin; D014667:Vasopressins
chemical_list: D009842:Oligopeptides; D011945:Receptors, Angiotensin; D017483:Receptors, Vasopressin; D014667:Vasopressins; C056203:peptide PVA