K. Rajeshwari et Aa. Karande, Molecular mimicry by antiidiotypic monoclonal antibody to gonadotropin releasing hormone, IMMUNOL INV, 28(2-3), 1999, pp. 103-114
Antipeptide and antiidiotypic antibodies to several receptors are known to
mimic their respective ligands in transducing signals on binding their rece
ptors. In our attempts to study gonadotropin releasing hormone receptor, an
tipeptide and antiidiotypic monoclonal antibodies specific to the receptor
were established earlier. The antipeptide mAb F1G4 was to a synthetic pepti
de corresponding to the extracellular domain of human GnRH receptor and the
antiidiotypic mAb 4D10C1 was to the idiotype of a GnRH specific mAb. Here
we report the physiological effects of the two mAbs on binding the receptor
, as investigated using in vitro cultures of(a) human term placental villi
and (b) rat pituitaries. The mAb 4D10C1 exerted a dose-dependent release of
human chorionic gonadonopin in cultures of human term placental villi as w
ell as luteinising and follicle stimulating hormones in cultures of rat pit
uitaries.