Please use this identifier to cite or link to this item:
Title: Monoclonal antibodies to arginine vasopressin receptor bind to liver, kidney and pituitary membranes.
Austin Authors: Trinder, D;Mooser, V;Phillips, P A;Smith, A I;Casley, David J;Johnston, Colin I
Affiliation: Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australia
Issue Date: 1-Jun-1993
Publication information: Clinical and Experimental Pharmacology & Physiology; 20(6): 443-9
Abstract: 1. A vasopressin binding protein purified from rat liver membranes was used to immunize Balb/c mice and, subsequently, for the screening of hybrids raised in two different cell fusions. 2. Three hybrids were obtained which secreted monoclonal antibodies (MoAb) that bound to the purified solubilized receptor as detected by an enzyme-linked immunosorbent assay technique. All three MoAb immunoprecipitated the purified receptor. 3. In addition, the MoAb bound in a concentration-dependent manner to crude liver, kidney and anterior pituitary membranes, tissues known to contain arginine vasopressin (AVP) receptors but not to cardiac ventricle membranes which lack AVP receptors. 4. However, the binding of [125I]-[d(CH2)5,Sar7]AVP (a specific radiolabelled V1 antagonist) to the membrane-bound receptor was not inhibited by these antibodies. 5. These results suggest that MoAb recognize epitopes which are common to rat liver, kidney and anterior pituitary membranes but are not at the ligand binding site.
Gov't Doc #: 8339468
Type: Journal Article
Subjects: Animals
Antibodies, Monoclonal.immunology
Arginine Vasopressin.analogs & derivatives.metabolism
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Mice, Inbred BALB C
Pituitary Gland.immunology.metabolism
Pituitary Gland, Anterior.immunology.metabolism
Receptors, Vasopressin.immunology.metabolism
Appears in Collections:Journal articles

Show full item record

Page view(s)

checked on Dec 2, 2022

Google ScholarTM


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.