Binding of antimorphine anti-idiotypic antibodies to opiate receptors

doi:10.1016/0014-2999(84)90357-1

European Journal of Pharmacology

Volume 102, Issue 1, 15 June 1984, Pages 187-190

https://doi.org/10.1016/0014-2999(84)90357-1 Get rights and content

Abstract

Antibodies that specifically recognize and bind opiate receptors were developed by the anti-idiotypic method. Antimorphine antibodies were generated in rabbits and showed selective binding to various opiate ligands. Guinea pigs were immunized with antimorphine antibodies to produce anti-idiotypic antibodies that cross-reacted with opiate receptors. Guinea pig antiserum inhibited binding of naloxone (0.6 nmol) to mouse brain homogenate. In isolated mouse was deferens, contraction of electrically stimulated tissue was inhibited by the antiserum. The results indicate that anti-idiotypic antibodies which interact with opiate receptors were developed without isolating receptors.

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Cited by (16)

A monoclonal anti-idiotypic antibody to μ and δ opioid receptors
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A mouse monoclonal, anti-idiotypic, anti-opioid receptor antibody (Ab2-AOR) has been generated from monoclonal anti-morphine antibodies (Ab1). Hybridoma culture supernatants were screened by a solid phase radioimmunoassay (RIA), based on their competition with radiolabelled morphine for Ab1. One of the Ab2s that gave a positive RIA also competed at rat brain opioid receptors with tritiated opioid ligands dihydromorphine (DHM), naloxone, etorphine, Tyr-d-Ala-Gly-Phe-d-Leu (DADLE), Tyr-d-Ala-Gly-NMe-Phe-Gly-ol (DAMGE) and Tyr-d-Pen-Gly-Phe-d-Pen (DPDPE). SDS-PAGE revealed Ab2-AOR to be highly purified after successive affinity and protein A-Sepharose chromatography. Ab2-AOR at concentrations of 10–100 nM competed with both μ- and δ-selective specific ligands for brain opioid receptors. Less than 13 μg/ml Ab2-AOR completely inhibited specific opioid radioligand binding to both soluble and membrane-bound opioid receptors. To demonstrate its anti-δ receptor activity further, a double-antibody ELISA procedure was developed that is based on the binding of Ab2-AOR to immobilized NG 108-15 cells (which contain only δ opioid receptors). Dose-dependent, opioid peptide- and opiate alkaloid-competitive binding of Ab2-AOR-containing ascites fluid to NG 108-15 cells was observed. A μ opioid agonist effect was demonstrated for Ab2-AOR, in that it decreased by 70% [³H]thymidine incorporation into DNA of fetal brain cell aggregates. This agonist-like action of Ab2-AOR was blocked by naltrexone. The antibody bound specifically to brain tissue sections and the presence of diprenorphine blocked this interaction. Hence, an Ab2 with μ and δ specificity has been characterized.
A monoclonal anti-imipramine antibody with antidepressant binding properties similar to the muscarinic receptor
1990, Biochemical Pharmacology
A murine monoclonal antibody raised using imipramine conjugated to bovine serum albumin bound free imipramine with high affinity (k_d) = 24 nM). The antibody had a binding affinity profile for tricyclic and other uptake-inhibitor type antidepressants which correlated highly with the affinities of the same compounds for the brain acetylcholine muscarinic receptor, but not for plasma-membrane 5-hydroxytryptamine carriers. This antibody was not similar in binding properties to polyclonal antisera produced using the same antigen but was highly similar in binding properties to a monoclonal anti-nortriptyline antibody, ANT3, raised by Marulo et al. (Marulo S, Hoebeke J, Guillet JG, Andre C and Strosberg AD, J Immunol138: 524–526, 1987) using a different antigen.
Production and properties of antimorphine anti-idiotypic antibodies and their antiopiate receptor activity
1989, Methods in Enzymology
Development of an anti-idiotypic antibody that blocks substance P primary antibodies and substance P membrane binding
1987, Brain Research
Polyclonal antibodies against substance P were raised in rabbits and partially purified. This apparently homogeneous immunoglobulin fraction was used to immunize other rabbits. The anti-idiotypic antibodies derived from these rabbits were substantially more effective in competing with substance P than in competing with β-endorphin for binding to their respective primary antibodies. The anti-idiotypic antibody was also 50 times more potent in competing with substance P binding than in competing with substance K binding to rat duodenal membranes, a tissue containing receptors for substance P and substance K. The anti-idiotypic antibodies exhibited significant enhancement of substance P induced spasmogenic response on the rat uterus and guinea pig ileum (GPI). The results indicate that it is possible to develop anti-idiotypic antibodies that recognize substance P receptors. These antibodies will be of value in studies of the physiological roles of the neuropeptide, substance P.
Monoclonal antibodies directed against the drug haloperidol
1987, Neurochemistry International
Haloperidol coupled to albumin via the hydroxyl or carbonyl group has been used to obtain two classes of monoclonal anti-haloperidol antibodies. Both classes of monoclonal antibody bind haloperidol with high affinity but whereas one class is highly specific for haloperidol the other class binds other butyrophenones e.g. droperidol, spiperone. Anti-idiotypic antisera have been obtained that inhibit [³H]haloperidol binding to the anti-haloperidol antibodies but these do not cross react with the D₂ dopamine receptor.
Polyclonal anti-idiotypic opioid receptor antibodies generated by the monoclonal β-endorphin antibody 3-E7
1985, Biochemical and Biophysical Research Communications
Anti-idiotypic antibodies were raised in rabbits against the monoclonal β-endorphin antibody 3-E7. These antibodies inhibit β-endorphin binding to the 3-E7 antibody, binding of ³H-diprenorphine to solubilized opioid receptors and the binding of ¹²⁵I-β-endorphin to rat brain membranes. Exposure of NG-108CC15 hybrid cells to anti-idiotypic antibodies produces an opioid-like inhibition of PGE₁-stimulated cAMP accumulation. These data suggest that the antibodies raised by the anti-idiotypic route both bind to and activate opioid receptors.

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Short communicationBinding of antimorphine anti-idiotypic antibodies to opiate receptors

Abstract

Affinity chromatography of antimorphine antibodies

Res. Comm. Subst. Abuse

Methods in Immunology

An anti-idiotypic antibody that recognizes the beta-adrenergic receptor

J. Clin. Invest.

Anti-alprenolol anti-idiotypic antibodies bind to beta-adrenergic receptors and modulate catecholamine-sensitive adenylate cyclase

Short communication
Binding of antimorphine anti-idiotypic antibodies to opiate receptors