Monoclonal antibodies to the rat liver glucocorticoid receptor.

Westphal, Hannes M.; Moldenhauer, Gerhard; Beato, Miguel

doi:10.1002/j.1460-2075.1982.tb01339.x

Cited by 116 publications

(43 citation statements)

References 18 publications

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“…(3) The N-terminal region (~ 400 amino acid residues), of which the function is not clearly defined. Most of the antibodies are raised against this part of the receptor protein (CarlstedtDuke et al, 1982;Westphal et al, 1982).…”

Section: Primary Structurementioning

confidence: 99%

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Joëls

Kloet

1994

Progress in Neurobiology

368

168

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Section: Primary Structurementioning

confidence: 99%

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Joëls

Kloet

1994

Progress in Neurobiology

368

168

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“…1A) represents nonspecific labeling of proteins since dexamethasone-21-mesylate binding was not reduced by an excess ofunlabeled hormone. The presence ofGR protein in the high molecular mass peak was further suggested by immunoprecipitation of samples, prior to gel electrophoresis, with GR494 mAb that recognizes chicken GR (27). The proteins present in the high molecular mass peak were efficiently precipitated by this mAb, with only a trace of the low molecular mass peak protein (Fig.…”

mentioning

confidence: 94%

Developmental changes in the expression and compartmentalization of the glucocorticoid receptor in embryonic retina.

Gorovits

Ben-Dror

Fox

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Inducibility by glucocorticoids of the glutamine synthetase gene in chicken embryo retina and the transcriptional activity of the glucocorticoid receptor (GR) greatly increase between embryonic days 6 and 10 (E6, E10), although the level of GR does not markedly change during that time. This apparent discrepancy was investigated by exming the pattern of GR expression in undifferentiated E6 retina and in E10 retina, which consists mostly of differentiated cells. Two GR Isoforms, 90 and 95 kDa, were found to be expressed at both of these ages at a similar total level but in different proportions: in E6 retina the level of the 90-kDa isoform was higher, whereas in E10 retina the 95-kDa receptor was higher.However, following treatment of the retinas with cortisol, the 95-kDa isoform became the predominant receptor at both ages.Immunohistochemical analysis revealed that the cellular localization of GR markedly changed in the course of development: in the undifferentiated E6 retina GR was expressed in virtually all cells, whereas in the more differentiated E10 and E12 retina, GR was detected only in Mfiller glia cells. The latfer represent 20% of the cells in this tissue and are the only cells in which glucocorticoid hormone induces the glutamine synthetase gene.We suggest that the compatmentalization of GR in Muller glia is a majior aspect of the mechanism that modulates receptor activity during retina development and results in the temporal increase in the inducibility of glutamine synthetase and its specific localization in Mfuller glia cells.

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“…DNA binding of the glucocorticoid receptor was detected using the monoclonal antibody GR49/4 as described (6,14).…”

mentioning

confidence: 99%

Binding of hormone accelerates the kinetics of glucocorticoid and progesterone receptor binding to DNA.

Schauer

Chalepakis

Willmann

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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Steroid hormone receptors induce genes by virtue of their interaction with DNA regulatory sequences. The hormonal response of a particular gene in vivo correlates with binding of the hormone to the receptor and supposedly reflects the degree of occupancy of the corresponding DNA regulatory sequences. However, in vitro the steroid-free glucocorticoid and progesterone receptors bind specifically to the regulatory sequences of mouse mammary tumor virus, thus raising questions on the role of the hormone in DNA binding in vivo. By using monoclonal antibodies, gel retardation assays, and filter binding techniques we show here that binding of a functional steroid to either the glucocorticoid or the progesterone receptors influences the kinetics of the protein-DNA interaction in vitro. In the presence of hormone the on rate of receptor binding to DNA fragments with or without regulatory sequences is accelerated 2-to 5-fold, and the off rate is accelerated 10-to 20-fold. The receptors complexed to an antihormone bind to DNA with kinetics intermediate between those of the steroid-free and the hormone-bound protein. Thus, ligand binding accelerates the kinetics of receptor binding to DNA and this could partly account for the behavior of the hormone receptor observed in vivo.The cis elements that mediate gene induction by steroid hormones are hormone-dependent enhancers (1) and have been designated hormone-responsive or -regulatory elements (HREs). The trans-acting factors that interact with the HREs are the steroid hormone receptors, a family of proteins that has been widely studied due to their ability to specifically bind the corresponding hormone. The domain of the receptor that binds the steroid hormone is located in a large region of the C-terminal half of the protein and is separated from the DNA-binding domain by a hinge region (2). Exactly how the DNA-binding domain and the steroid-binding domain of the receptor interact is not known.The magnitude of the hormone response observed in vivo correlates with the degree of saturation of the corresponding receptor (see, for instance, ref.3). According to the prevailing view, binding of the hormone to the receptor is followed by a conformational change of the protein leading to the exposition of the preformed DNA-binding domain that is masked in the hormone-free receptor (1). Whether this masking is accomplished intramolecularly by the steroidbinding domain or intermolecularly by interaction with other factors, such as the 90-kDa heat shock protein, is a matter of debate (4). In cell fractionation studies one consequence of hormone administration is the association of the otherwise cytosolic receptor with the nuclear fraction, suggesting a tighter interaction with DNA in chromatin. In agreement with this model, the HRE of the tyrosine amino transferase gene in rat liver has been shown to be protected against methylation by dimethyl sulfate in vivo only after hormone administration, whereas no protection is detected prior to hormone treatment (5).To understand the p...

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Monoclonal antibodies to the rat liver glucocorticoid receptor.

Cited by 116 publications

References 18 publications

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Developmental changes in the expression and compartmentalization of the glucocorticoid receptor in embryonic retina.

Binding of hormone accelerates the kinetics of glucocorticoid and progesterone receptor binding to DNA.

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