Regulation of nuclear binding of the avian oviduct progesterone receptor. Changes during estrogen-induced oviduct development, withdrawal, and secondary stimulation.

Boyd-Leinen, P. A.; Gosse, Barbara; Rasmussen, K.; Martin-Dani, G.; Spelsberg, Thomas C.

doi:10.1016/s0021-9258(17)43368-0

Cited by 47 publications

(21 citation statements)

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“…This problem could explain the nonspecific inhibition of the acceptor sites on whole chromatin. Therefore, all of the subsequent studies utilized the more soluble NAP, which appears to contain the same PRov acceptor sites as the native chromatin (Webster et al, 1976;Spelsberg et al, 1983Spelsberg et al, , 1984Goldberger et al, 1986).…”

Section: Resultsmentioning

confidence: 99%

“…Chromatin, Nucleoacidic Protein, and DNA. Chromatin and NAP isolations from avian oviduct as well as DNA isolation from hen spleen are described elsewhere (Spelsberg et al, 1984). Native NAP results from the extraction of chromatin with 4.0 M guanidine hydrochloride (Gdn-HCl) and represents enriched acceptor sites from whole chromatin.…”

Section: Methodsmentioning

confidence: 99%

“…The receptor binding to NAP was corrected for binding to pure DNA by subtraction of the DNA binding from the binding to NAP. Binding of a nonfunctional receptor (Boyd-Leinen et al, 1984) was used to correct for nonspecific receptor binding to chromatin. Data shown are representative of two to three major experiments.…”

Section: Methodsmentioning

confidence: 99%

“…Partially purified acceptor protein was reannealed onto hen DNA, and the excess DNA was removed by limited DNase I digestion to give enriched reconstituted acceptor sites. The reconstituted PRov binding sites were previously shown to be similar to native sites (Spelsberg et al, 1984). The MAbs (as ascites fluids) were able to inhibit PRov binding to native acceptor sites without affecting the receptor itself or the nonspecific receptor binding to pure DNA.…”

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confidence: 87%

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Characterization of the chromatin acceptor sites for the avian oviduct progesterone receptor using monoclonal antibodies

et al. 1987

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Monoclonal antibodies (MAb) against the chromatin acceptor sites for the avian oviduct progesterone receptor were prepared with highly purified hen oviduct acceptor proteins reconstituted to hen DNA. Addition of the MAbs to a cell-free assay blocked progesterone receptor from chick oviduct (PRov) binding to native-like acceptor sites on nucleoacidic protein (NAP) representing a partially deproteinized chromatin, which has been shown to be enriched in these binding sites. However, the antibodies do not block PRov binding to pure DNA, nor do they affect the receptor itself. Estrogen receptor binding to NAP was not inhibited, supporting a receptor specificity of the PRov acceptor sites as reported previously from direct competition studies. These data support earlier studies showing that (1) the reconstituted PRov acceptor sites resemble the native sites, (2) the acceptor sites are receptor specific, and (3) the PRov binding sites of NAP are different from those of pure DNA. While some animal-species specificity in the PRov binding inhibition was observed, no tissue specificity was seen. Direct binding of the antibodies to native acceptor sites was demonstrated in an enzyme-linked immunosorbent assay (ELISA) system. The antibodies showed little recognition of free acceptor protein or DNA alone, indicating specificity for the protein-DNA complex. A partial evolutionary conservation of the nuclear acceptor sites for PRov was shown by the fact that about 50% of the inhibition seen with hen NAP was obtained with NAPs from several other species, and this partial cross-reactivity of the MAbs with the same NAPs from other animal species was also seen in the ELISA.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 87%

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Characterization of the chromatin acceptor sites for the avian oviduct progesterone receptor using monoclonal antibodies

et al. 1987

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“…This class of nuclear binding sites has previously been shown to consist of specific protein bound to specific DNA sequences (Spelsberg et al, 1983;Toyoda et al, 1985). The high-affinity, saturable binding of PR to these sites is receptor dependent (Pikler et al, 1976) and receptor specific (Kon & Spelsberg, 1982) and mimics binding patterns seen in vivo Spelsberg et al, 1983;Boyd-Leinen et al, 1984). The specific PR binding is lost once the protein is removed from the DNA (Spelsberg et al, 19799, 1983(Spelsberg et al, 19799, , 1984Toyoda et al, 1985).…”

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confidence: 99%

Partial purification and preparation of polyclonal antibodies against candidate chromatin acceptor proteins for the avian oviduct progesterone receptor

Goldberger

Spelsberg²

1988

Biochemistry

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Steroid hormones bind to specific receptors in target cells that in turn bind to chromatin acceptor sites to alter gene expression. These chromatin acceptor sites, for a variety of steroid receptors, appear to be composed of acceptor proteins tightly bound to the DNA. This paper describes the preparation of new polyclonal antibodies against the chromatin acceptor proteins of the avian oviduct progesterone receptor (PR) and their use in monitoring the purification of the acceptor proteins. This laboratory recently reported the preparation of monoclonal antibodies that do recognize the intact chromatin acceptor sites containing DNA-bound acceptor proteins but not the unbound acceptor protein for PR [Goldberger, A., Horton, M., Katzmann, J., & Spelsberg, T. C. (1987) Biochemistry 26, 5811-5816]. In order to obtain antibodies that recognize the unbound acceptor protein, polyclonal antibodies were prepared against a highly purified preparation of the acceptor protein(s). Analyses by ELISA indicate that the polyclonal antibodies recognize both the intact acceptor sites and the unbound (free) acceptor protein(s). Using these antibodies in Western immunoblots, two antigenic species of 10 and 6 kDa were detected in crude fractions of acceptor protein. These two protein species could be separated and further enriched while still retaining acceptor activity, i.e., the capacity to generate specific binding of the PR. Thus, the antigenic activity is closely associated with, if not identical with, the acceptor activity. Whether one or both species are used in vivo or whether the 6-kDa species is a proteolytic product of the 10-kDa species is unknown.(ABSTRACT TRUNCATED AT 250 WORDS)

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Expression of the Chicken Progesterone Receptor Forms A and B Is Differentially Regulated by Estrogenin Vivo

Syvälä¹,

Vienonen

Ylikomi

et al. 1997

Biochemical and Biophysical Research Communications

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Regulation of nuclear binding of the avian oviduct progesterone receptor. Changes during estrogen-induced oviduct development, withdrawal, and secondary stimulation.

Cited by 47 publications

References 50 publications

Characterization of the chromatin acceptor sites for the avian oviduct progesterone receptor using monoclonal antibodies

Characterization of the chromatin acceptor sites for the avian oviduct progesterone receptor using monoclonal antibodies

Partial purification and preparation of polyclonal antibodies against candidate chromatin acceptor proteins for the avian oviduct progesterone receptor

Expression of the Chicken Progesterone Receptor Forms A and B Is Differentially Regulated by Estrogenin Vivo

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