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Monoclonal antibody to the δ opioid receptor acts as an agonist in dual regulation of adenylate cyclase in NG108‐15 cells
Author(s) -
Gomes Ivone,
Gupta Achla,
Singh S.P,
Sharma Shail K
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00878-9
Subject(s) - monoclonal antibody , adenylate kinase , microbiology and biotechnology , cyclase , immunoprecipitation , epitope , receptor , chemistry , western blot , agonist , antibody , chaps , polyclonal antibodies , damgo , opioid receptor , biology , biochemistry , membrane , immunology , gene
Monoclonal antibodies generated against multiple antigenic peptides of the N‐terminal sequence ( 3 LVPSARAELQSSPLV 17 ) of the cloned δ opioid receptor immunoprecipitated a 58 kDa protein from CHAPS‐solubilized NG108‐15 membranes. The immunoprecipitates bound [ 3 H]DPDPE – but not [ 3 H]DAMGO – with a K d of 6.4 nM and a B max of 75 pM. Western blot analysis revealed a distinct band of 58 kDa. The antibodies inhibited basal and PGE 1 ‐stimulated cAMP levels, and mimicked the effect of agonists manifest in a compensatory increase in cAMP formation. The antibody will be potentially useful in the analysis of functional epitopes on the δ opioid receptor.