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. 1980 Dec;77(12):7385–7389. doi: 10.1073/pnas.77.12.7385

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

A B Schreiber, P O Couraud, C Andre, B Vray, A D Strosberg
PMCID: PMC350508  PMID: 6261254

Abstract

Rabbit antibodies induced against alprenolol, a potent beta-adrenergic antagonist, bind to other antagonists, and, with less avidity, to catecholamine agonists. Anti-idiotypic antibodies were raised against the anti-alprenolol immunoglobulins. The anti-idiotypic antibodies specifically bind and agglutinate turkey erythrocytes; this is not observed for human agglutinate turkey erythrocytes; this is not observed for human or sheep erythrocytes, which are devoid of beta-adrenergic receptors. The anti-idiotypic antibodies compete with (--)-[3H]-dihydroalprenolol for binding on the beta-adrenergic receptors on purified turkey erythrocyte membranes. The binding to the membrane-bound receptors is prevented by preincubation of the anti-idiotypic antibodies with their immunogen, the antialprenolol immunoglobulins. The binding to the receptor is not merely passive: the anti-idiotypic antibodies stimulate basal adenylate cyclase activity [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] and enhance adenylate cyclase activation by catecholamine. These observations support the notion that antiidiotypic antibodies may constitute an "internal image" of the original antigen and may mimic its biological effects.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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