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Title: Vasopressin antisense peptide interactions with the V1 receptor.
Austin Authors: Kelly, J M;Trinder, D;Phillips, P A;Casley, David J;Kemp, Bruce E;Mooser, V;Johnston, Colin I
Affiliation: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australia
Issue Date: 8-Jul-1990
Publication information: Peptides; 11(4): 857-62
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.
Gov't Doc #: 2146598
Type: Journal Article
Subjects: Amino Acid Sequence
Cell Membrane.metabolism
Molecular Sequence Data
Receptors, Angiotensin.isolation & purification.metabolism
Receptors, Vasopressin
Appears in Collections:Journal articles

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