title: Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF-1).
abstract: 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)
authors.affiliation: Department of Biomedical Sciences, University of Tampere, Finland.
authors.forename: Y H
authors.initials: YH
authors.lastname: Zhuang
authors.forename: J P
authors.initials: JP
authors.lastname: Landers
authors.forename: M D
authors.initials: MD
authors.lastname: Schuchard
authors.forename: H
authors.initials: H
authors.lastname: Syvälä
authors.forename: B
authors.initials: B
authors.lastname: Gosse
authors.forename: T
authors.initials: T
authors.lastname: Ruesink
authors.forename: T C
authors.initials: TC
authors.lastname: Spelsberg
authors.forename: P
authors.initials: P
authors.lastname: Tuohimaa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D030161:Avian Proteins; D015153:Blotting, Western; D002352:Carrier Proteins / Q000032:analysis*; D002467:Cell Nucleus / Q000737:chemistry; D002645:Chickens; D002843:Chromatin / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000032:analysis*; D004848:Epithelium / Q000737:chemistry; D004958:Estradiol / Q000494:pharmacology; D005260:Female; D007150:Immunohistochemistry; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010057:Oviducts / Q000737:chemistry* / Q000648:ultrastructure; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; D051381:Rats; D011980:Receptors, Progesterone / Q000032:analysis*
chemical_list: D000911:Antibodies, Monoclonal; D030161:Avian Proteins; D002352:Carrier Proteins; D002843:Chromatin; D004268:DNA-Binding Proteins; D047908:Intracellular Signaling Peptides and Proteins; C085646:RBF-1 protein, Gallus gallus; D011980:Receptors, Progesterone; D004958:Estradiol; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C434934:trans-2-enoyl-CoA reductase (NADPH)