Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF-1).

An avian oviduct nuclear matrix protein in the 6-10 kDa size range has been implicated to function in the cell-free nuclear binding of the avian oviduct progesterone receptor (PR). This protein, termed the receptor binding factor-1 (RBF-1), has been purified and partially characterized [Schuchard et al.: Biochemistry 30:4535-4542, 1991]. This paper describes the immunohistochemical co-localization of the RBF-1 and PR in the avian oviduct cell nuclei and rat reproductive cell nuclei using antibodies directed specifically against the RBF-1 and activated PR. In the undifferentiated oviduct, the immunoreactivities for both PR and RBF-1 were co-localized in the nuclei of only epithelial cells, but not the stromal cells or smooth muscle cells. In the partially differentiated oviduct of estrogen treated chicks, the immunoreactivity co-localized in the nuclei of not only epithelial but also glandular and stromal cells. Staining for the PR, but not RBF-1, was detected in the smooth muscle cells. The intensity of the PR but not the RBF-1 staining was markedly down-regulated in these cells at 2 and 6 h after treatment of the animals with progesterone (P). However, the band patterns for RBF-1 in the Western blots did show qualitative changes which may reflect P-induced posttranslational modifications which alter the epitope on the RBF-1. Interestingly, immunohistochemical analysis of several reproductive tissues of the rat showed that certain cell types in the uterus, ovary, and prostate displayed strong positive nuclear staining for an RBF-1-like antigen(s).(ABSTRACT TRUNCATED AT 250 WORDS)