Liver cytosol corticosteroid binder IB, a new binding protein.

Litwack, Gerald; Rosenfield, Sheila

doi:10.1016/s0021-9258(19)41002-8

Cited by 47 publications

(6 citation statements)

References 14 publications

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“…After activation by heat (30 min at 25 °C), liver cytosol radioactivity was largely associated with the less acidic fraction eluted with 0.2-0.25 M KC1, corticosteroid binder II (Litwack et al, 1973). The radioactivity bound to the protein fraction in the buffer wash is identified as the previously characterized (Litwack & Rosenfield, 1975) corticosteroid binder IB (Figure 1C). Following heat activation, almost all radioactivity from kidney cytosol was bound to the protein which is eluted in the position of IB (Figure 1G).…”

Section: Resultsmentioning

confidence: 77%

“…The results here indicate the existence of a distinctive and identical glucocorticoid receptor type in all the tissues studied except for kidney cortex, whose 0006-2960/80/0419-4556S01.00/0 © 1980 American Chemical Society 19, NO. 20, 1 980 4557 major receptor is similar to a second form in liver cytosol, corticosteroid binder IB (Litwack & Rosenfield, 1975).…”

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confidence: 99%

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Evidence for a physiological role of corticosteroid binder IB

Markovic¹,

Eisen²,

Parchman³

et al. 1980

Biochemistry

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Glucocorticoid binding proteins in liver and kidney of adrenalectomized rats have been analyzed by rapid ionexchange chromatography, gel filtration, and specific interactions with antibodies against purified liver cytosol receptor and purified transcortin. In both tissues, the unactivated form of the [3H]triamcinolone acetonide-receptor complex is eluted by 0.4-0.5 M KC1 from DEAE-Sephadex minicolumns. After heat activation, the major form in liver cytosol, corticosteroid binder II, is eluted by 0.2 M KC1 from the DEAE minicolumn; a minor component in the buffer wash is identified as corticosteroid binder IB. Binders II and IB are shown to be DNA-binding proteins whereas the unactivated forms do not bind to DNA. In contrast, the major activated form in kidney cytosol has the properties of corticosteroid binder IB (e.g., it is eluted in the buffer wash of the DEAE minicolumn, is a DNA-binding protein, and has a Stokes radius of 20-26 Á). Evidence is presented which suggests that IB is not a proteolytic product of II. Antibody to highly purified rat liver glucocorticoid receptor was immobilized on Sepharose 4B-CL. The major unactivated and activated [3H]triamcinolone acetonide-receptor complexes from rat liver are adsorbed by the Cxiucocorticoids regulate gene expression in eukaryotic cells via a two-step mechanism common for all steroid hormones

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Section: Resultsmentioning

confidence: 77%

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confidence: 99%

Evidence for a physiological role of corticosteroid binder IB

Markovic¹,

Eisen²,

Parchman³

et al. 1980

Biochemistry

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“…The effect of molybdate on the formation of activated glucocorticoid-receptor complexes from liver cytosol is shown in Figure 2. Using chromatography on DEAE-Sephadex our laboratory has identified two proteins in rat liver cytosol which preferentially bind synthetic glucocorticoids (Litwack et al, 1973; Litwack & Rosenfield, 1975). Liver binder II, which binds to DEAE-Sephadex, fulfills the criteria of the glucocorticoid receptor (Litwack et al, 1973), while liver binder IB, which does not bind to DEAE-Sephadex, represents a binding protein of unknown physiological function (Litwack & Rosenfield, 1975).…”

Section: Resultsmentioning

confidence: 99%

“…Using chromatography on DEAE-Sephadex our laboratory has identified two proteins in rat liver cytosol which preferentially bind synthetic glucocorticoids (Litwack et al, 1973; Litwack & Rosenfield, 1975). Liver binder II, which binds to DEAE-Sephadex, fulfills the criteria of the glucocorticoid receptor (Litwack et al, 1973), while liver binder IB, which does not bind to DEAE-Sephadex, represents a binding protein of unknown physiological function (Litwack & Rosenfield, 1975). More recent work from this laboratory (Litwack et al, 1980) had established that the major glucocorticoid binding protein in rat kidney medulla resembles liver binder II (the glucocorticoid receptor).…”

Section: Resultsmentioning

confidence: 99%

Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors, and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes

Barnett¹,

Schmidt²,

Litwack³

1980

Biochemistry

116

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“…observed, it appeared to be due to limited receptor proteolysis (Wrange & Gustafsson, 1978;Carlstedt-Duke et al, 1979;Govindan, 1980;Govindan & Manz, 1980;Stevens & Stevens, 1981;Tsawdaroglou et al, 1981). However, in at least one instance (Litwack & Rosenfield, 1975;Markovic et al, 1980), a second species of glucocorticoid receptor, designated binder IB, which did not appear to be a proteolytic fragment of the major receptor form (binder II; Litwack et al, 1973), was found to occur in a tissue-specific fashion. In the present study, the activated receptor eluted as a single, symmetrical peak on all the columns tested, regardless of the activation method used.…”

Section: Discussionmentioning

confidence: 98%

Activation and chromatographic properties of the AtT-20 mouse pituitary tumor cell line glucocorticoid receptor

Vedeckis¹

1981

Biochemistry

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The physicochemical properties of the glucocorticoid receptor (GC-R) from the mouse AtT-20 pituitary tumor cell line were studied. Analyses involved ion-exchange (diethylaminoethylcellulose, phosphocellulose), gel filtration (Sephadex G-150), and adsorption (DNA-cellulose, hydroxylapatite) chromatography. The receptor was characterized in four different states: native (unactivated), activated, nuclear, and Na2Mo04 stabilized. The unactivated receptor had chromatographic properties which were very similar to those of other steroid hormone receptor proteins; that is, it was not adsorbed to phosphocellulose (PC) or DNA-cellulose but did adsorb to diethylaminoethylcellulose (DEAE-cellulose) and eluted at 0.2 M KCl. In addition, a single peak, which eluted at 0.11 M phosphate, was obtained upon hydroxylapatite (HAP) chromatography. Because of aggregation, it was not possible to estimate the size of the unactivated GC-R. After activation by Sephadex G-25 gel filtration or by precipitation at 40% saturated (NH4)2S04, the receptor adsorbed to both PC and DNA-cellulose, eluting in a single, symmetrical peak at 0.17 and 0.14 M KC1, respectively. The fact that the

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Liver cytosol corticosteroid binder IB, a new binding protein.

Cited by 47 publications

References 14 publications

Evidence for a physiological role of corticosteroid binder IB

Evidence for a physiological role of corticosteroid binder IB

Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors, and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes

Activation and chromatographic properties of the AtT-20 mouse pituitary tumor cell line glucocorticoid receptor

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