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Previous studies indicated that the anti-idiotypic antibody (clone 1D₅) significantly increased the specific activity of creatine kinase (CK) activity in the rat uterus, and in vitro in skeletal cells capable of responding to oestradiol (E₂), suggesting that the antibody has oestrogenic-like activity. Moreover, the F(ab')₂ dimer of clone 1D₅ acted like an antagonist and completely inhibited the increase in CK specific activity by either E₂ or clone 1D₅ in these skeletal cells. In the present study, we examined the in vivo effects of clone 1D₅ and its proteolytic fragment, the F(ab')₂ dimer, E₂ and dihydrotestosterone (DHT) on CK specific activity in the epiphyseal cartilage, diaphyseal bone, uterus, prostate, thymus and pituitary of immature or gonadectomized female and male rat animal models. In the intact immature animals, clone 1D₅ caused an increase in CK in all organs of the female except in the pituitary. In the diaphyseal bone and prostate of male rats there was no stimulation by 1D₅. The CK response in the uterus, epiphysis, and diaphysis of immature female rats was dose-dependent and was blocked by either the anti-oestrogen tamoxifen or the F(ab')₂ dimer of clone 1D₅. E₂, DHT, as well as clone 1D₅, stimulated CK specific activity in both the diaphysis and epiphysis of ovariectomized female and castrated male rats, whereas sex specificity in the CK response was observed also in the uterus and the prostate of gonadectomized animals. Collectively, these results suggest that, as in cell culture, an intact antibody is necessary for the observed stimulation of CK specific activity and the F(ab')₂ dimer can act as an antagonist. Furthermore, the observed biological effects of clone 1D₅ which are absolutely parallel to E₂, imply that the anti-idiotypic antibody is able to penetrate the cell and reach the nuclear oestrogen receptor and transduces a signal to the nucleus, by as yet uncharacterized mechanisms.

Journal of Endocrinology (1996) 149, 305–312