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|Title:||Vasopressin antisense peptide interactions with the V1 receptor.|
|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.|
|Citation:||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.|
|Internal ID Number:||2146598|
|Subjects:||Amino Acid Sequence|
Molecular Sequence Data
Receptors, Angiotensin.isolation & purification.metabolism
|Appears in Collections:||Journal articles|
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