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

Zhuang, Yibo; Landers, James P.; Schuchard, Mark D.; Syvälä, Heimo; Gosse, Barbara; Ruesink, Terry; Spelsberg, Thomas C.; Tuohimaa, Pentti

doi:10.1002/jcb.240530416

Cited by 5 publications

(3 citation statements)

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“…1B). This is in agreement with that described in several other avian species including the domestic fowl (Gasc et al, 1984;Zhuang et al, 1993) and quail (Pageaux et al, 1983;Tsutsui, personal communication). Furthermore, these findings are consistent with an earlier study in the ring dove showing the greatest binding of radiolabelled progesterone in anterior and posterior hypothalamic tissue (Balthazart et al, 1980).…”

Section: Immunolocalization Of Steroid Receptorssupporting

confidence: 92%

Changes in central steroid receptor expression, steroid synthesis, and dopaminergic activity related to the reproductive cycle of the ring dove

Lea

Clark

Tsutsui

2001

Microscopy Res & Technique

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This review examines possible neural mechanisms involved in the expression of parental behavior in the ring dove, Streptopelia risoria. This avian species has proved an excellent animal model for studies concerning endocrine-behavior interactions for many years. Studies were performed to localize the expression of central androgen and progesterone receptor in both sexes. Expression of androgen receptor (androgen receptor immunoreactivity, AR-ir) was widespread but increased, similarly in both sexes, with increasing day-length. Progesterone receptor-immunoreactivity (PR-ir) was more localized in several discrete areas of the hypothalamus. Similarly, no sex differences were observed in PR-ir, and expression increased in birds maintained on long days. AR-ir demonstrated dramatic changes over the breeding cycle, being greatest in courting birds and almost undetectable in parenting birds of both sexes brooding their young. PR-ir showed a differential expression over the breeding cycle relative to its hypothalamic localization. PR-ir decreased in the tuberal hypothalamic area in brooding birds of both sexes; whereas in the preoptic area, PR-ir was maintained. Significant increases in dopaminergic activity during the parenting phase of the breeding cycle occurred in specific neural regions including the PVM and DMA. Studies demonstrated the ability of the diencephalon of both sexes of the ring dove brain to synthesize progesterone, with indications that in the male brooding dove, synthesis is increased. Finally, a model is presented that proposes a mechanism whereby these central systems may interact to result in the expression of full parental behavior in both sexes of the ring dove.

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Section: Immunolocalization Of Steroid Receptorssupporting

confidence: 92%

Changes in central steroid receptor expression, steroid synthesis, and dopaminergic activity related to the reproductive cycle of the ring dove

Lea

Clark

Tsutsui

2001

Microscopy Res & Technique

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“…Using immunohistochemical techniques with antibodies against the purified RBF, the RBF was localized to the nuclei of selected cell types in certain avian and rat tissues (27,28). In similar studies, colocalizations of RBF and PR in the same cell types in the avian oviduct and rat reproductive organs were also shown.…”

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confidence: 65%

A DNA-binding Element for a Steroid Receptor-binding Factor Is Flanked by Dual Nuclear Matrix DNA Attachment Sites in the c-myc Gene Promoter

Lauber

Barrett

Subramaniam

et al. 1997

Journal of Biological Chemistry

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The receptor-binding factor (RBF) for the avian oviduct progesterone (Pg) receptor (PR) has previously been shown to be a unique 10-kDa nuclear matrix protein that generates high affinity PR-binding sites on avian DNA. This paper describes the use of Southwestern blot and DNA gel shift analyses with RBF protein to identify a minimal 54-base pair RBF-binding element in the matrix-associated region (MAR) of the Pg-regulated c-myc gene promoter. This element contains a 5 -GC-rich domain and a 3 -AT-rich domain, the latter of which has a homopurine/homopyrimidine structure. The gel shift assays required the generation of an RBF-maltose fusion protein (RBF-MBP), which specifically binds this element and is supershifted when the anti-RBF polyclonal antibody is added. Computer analysis of the fulllength amino acid sequence for RBF predicts a DNAbinding motif involving a ␤-sheet structure at the N-terminal domain. Southern blot analyses using nuclear matrix DNA suggests that there are dual MAR sites in the c-myc promoter, which flank an intervening domain containing the RBF element. The co-transfection of this MAR sequence, containing the RBF element and cloned into a luciferase reporter vector, together with an RBF expression vector construct, into steroid treated human MCF-7 cells, results in a decrease of the c-myc promoter activity relative to control transfections containing only the parent vector of the RBF expression construct. These data suggest that a unique chromatin/ nuclear matrix structure, composed of the RBF-DNA element complex which is flanked by nuclear matrix attachment sites, serves to bind the PR and repress the c-myc promoter.The classic model of steroid hormone action suggests that ligand-bound receptors dimerize and bind to specific sites (acceptor sites) on the chromatin/DNA to alter gene expression. In many genes, the steroid receptors (SR) 1 bind to specific cisacting DNA sequences, referred to as hormone response elements (for reviews, see Refs. 1-3). These elements function as enhancer-like DNA sequences and are required for the steroid hormone regulation of transcription. However, not all steroidresponsive genes contain these elements, and several other pathways and participating nuclear proteins have now been identified. The SR regulation of gene transcription has now been shown to involve 1) interactions of the SR with transcription factors, such as the AP-1 complex (for review, see Refs. 2-4); 2) interactions of SR with accessory factors, which appear to function by assisting the binding of the receptor to the steroid response elements, or to transcription factors (for reviews see Refs. 4 -6 and references therein); and finally, 3) interactions of SR with specific chromatin structures including the nuclear matrix (see Refs. 7-15 and references therein). In the latter, a class of high affinity binding sites (acceptor sites) for SRs in the nuclei, chromatin, and nuclear matrix DNAbinding proteins (e.g. acceptor proteins) has been reported by many laboratories for most of the steroid hormone...

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“…These data support that the RBF appears to be an essential protein component of progesterone receptor nuclear acceptor sites, or, at least, a component of a subset of these sites in the chromatin structure and that specific DNA elements may be required for these sites. Immunohistochemical staining showed that RBF was located in the nucleus and colocalized in cells that also expressed progesterone receptor, such as avian oviduct and rat reproductive tissues (18).…”

mentioning

confidence: 99%

Interactions of the Nuclear Matrix-Associated Steroid Receptor Binding Factor with Its DNA Binding Element in the c-myc Gene Promoter

et al. 2000

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Steroid receptor binding factor (RBF) was originally isolated from avian oviduct nuclear matrix. When bound to avian genomic DNA, RBF generates saturable high-affinity binding sites for the avian progesterone receptor (PR). Recent studies have shown that RBF binds to a 54 bp element in the 5'-flanking region of the progesterone-regulated avian c-myc gene, and nuclear matrix-like attachment sites flank the RBF element [Lauber et al. (1997) J. Biol. Chem. 272, 24657-24665]. In this paper, electrophoretic mobility shift assays (EMSAs) and S1 nuclease treatment are used to demonstrate that the RBF-maltose binding protei (MBP) fusion protein binds to single-stranded DNA of its element. Only the N-terminal domain of RBF binds the RBF DNA element as demonstrated by southwestern blot analyses, and by competition EMSAs between RBF-MBP and the N-terminal domain. Mass spectrometric analysis of the C-terminal domain of RBF demonstrates its potential to form noncovalent protein-protein interactions via a potential leucine-isoleucine zipperlike structure, suggesting a homo- and/or possible heterodimer structure in solution. These data support that the nuclear matrix binding site (acceptor site) for PR in the c-myc gene promoter is composed of RBF dimers bound to a specific single-stranded DNA element. The dimers of RBF are generated by C-terminal leucine zipper and the DNA binding occurs at the N-terminal parallel beta-sheet DNA binding motif. This complex is flanked by nuclear matrix attachment sites.

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

Cited by 5 publications

References 50 publications

Changes in central steroid receptor expression, steroid synthesis, and dopaminergic activity related to the reproductive cycle of the ring dove

Changes in central steroid receptor expression, steroid synthesis, and dopaminergic activity related to the reproductive cycle of the ring dove

A DNA-binding Element for a Steroid Receptor-binding Factor Is Flanked by Dual Nuclear Matrix DNA Attachment Sites in the c-myc Gene Promoter

Interactions of the Nuclear Matrix-Associated Steroid Receptor Binding Factor with Its DNA Binding Element in the c-myc Gene Promoter

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