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[Endocytosis of the androgen-binding-protein (ABP) by the principal cells of rat epididymis].

The present study is based on the comparison between the radioautographic analysis of the fate of the androgen-binding protein purified from rat testes (HPLC) subsequently iodinated and injected into the epididymal lumen using a micromanipulator, and the biochemical analysis of the binding capacities of this molecule to soluble epididymal membrane extracts using HPLC and ultracentrifugation. The various experimental conditions used here allowed to demonstrate that ABP was internalized by the epididymal epithelium and to state that this internalization was not a non specific fluid phase endocytosis but a receptor-mediated-mechanism. Indeed, from a morphological stand point, the labeled ABP was associated rather with the membranes of the endocytic apparatus than with its content. In addition, from the two lumenal cell types able to resorb seminal fluid products, only the principal cells took up the labeled ABP. Our results clearly showed that this internalization was correlated with the presence of a 125I.ABP binding protein. Since the binding of this protein molecule to ABP was saturable and Calcium and pH dependent, it is strongly suggested that this molecule behaves as a receptor, the ligand (or one of the ligands) of which could be ABP.