Activation of the chick oviduct progesterone receptor by heparin in the presence or absence of hormone

Yang, Chang-Ren; Mešter, Ján; Wolfson, Adele J.; Renoir, Jack‐Michel; Baulieu, Étienne Émile

doi:10.1042/bj2080399

Cited by 42 publications

(11 citation statements)

References 22 publications

(21 reference statements)

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“…Stabilization of the oligomeric structure was observed as indicated by sedimentation as 8S species in the absence of molybdate and in the presence of 0.4 M KC1 either in glycerol (Figure 1) or in sucrose gradients (not shown). In all these conditions, the non-cross-linked receptor was transformed and sedimented at ~4 S (Yang et al, 1982). Covalent stabilization of the 8S structure was also observed when cytosol was prepared in the absence of molybdate (Figure 1C).…”

Section: Resultsmentioning

confidence: 86%

Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical crosslinking

Arányi¹,

Radanyi²,

Renoir³

et al. 1988

Biochemistry

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The nontransformed forms of the chick oviduct cytosol progesterone receptor of sedimentation coefficient approximately 8 S (8S-PR) are heterooligomers including one hormone binding molecule, either B, approximately 110,000, or A, approximately 79,000, and two non-hormone binding subunits recently identified as heat-shock protein Mr approximately 90,000 (hsp 90) [Renoir, J. M., Buchou, T., Mester, J., Radanyi, C., & Baulieu, E. E. (1984) Biochemistry 23, 6016-6023]. In the crude cytosol, bisimidates reacted under mild conditions and gave rise to complexes, binding progesterone and reacting with BF4, an anti-hsp 90 monoclonal antibody. These complexes have a sedimentation coefficient of 8.4 S and Rs of 8.1 nm in the presence of 0.4 M KCl and in the absence of molybdate ions, i.e., in conditions that would transform non-cross-linked 8S-PR to Rs approximately 5 nm forms of approximately 4-S sedimentation coefficient. All bisimidates tested, of an effective reagent length between 0.73 and 1.09 nm, gave comparable results in the cytosol prepared with or without molybdate ions, confirming that the latter were not responsible for the formation of the cross-linked 8S complexes. It was found that the dimethyl pimelimidate cross-linked 8S-PR was more resistant to inactivating conditions, urea, or heat treatment than the non-cross-linked 8S-PR. The 8S-PR cross-linked in the cytosol was purified by affinity chromatography in the absence of molybdate ions. After purification, it also reacted with the monoclonal antibody BF4 and had the same Rs (8.0 nm), sedimentation coefficient (approximately 8.5 S), and thus Mr (approximately 290,000) as the original cytosol.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultsmentioning

confidence: 86%

Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical crosslinking

Arányi¹,

Radanyi²,

Renoir³

et al. 1988

Biochemistry

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“…The association between this 9OkDa polypeptide and the hormone-binding proteins (1 lOkDa and 75-8OkDa) in 8S PR, is apparently strong, since it is resistant to conditions such as high ionic strength (Yang et al, 1982) or 2.5 M-urea ) when stabilized by 20mM-Na2MoO4. It is unlikely that the 8S PR complexes could be an artefact due to addition of molybdate to the cytosol, since they are also found in absence of molybdate in cytosol and, when complexes are dissociated, for instance by high-salt treatment, they do not re-form by dialysis against low-salt, molybdate-containing buffer (Yang et al, 1982). The fact that the 90 kDa protein belongs to the untransformed 8S PR is confirmed by a recent experiment showing no 9OkDa protein in the eluate of affinity chromatography of molybdate-containing cytosol preincubated with 2juM-progesterone (Baulieu et al, 1983).…”

Section: Daysmentioning

confidence: 99%

Purification by affinity chromatography and immunological characterization of a 110kDa component of the chick oviduct progesterone receptor

Renoir¹,

Mešter²,

Buchou³

et al. 1984

Biochemical Journal

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A 110kDa component of the chick oviduct progesterone receptor (PR) has been purified to homogeneity according to electrophoretic criteria and specific activity (assuming one progestagen-binding site/110kDa). The procedure involved affinity chromatography of 0.3 M-KCl-prepared cytosol, followed by DEAE-Sephacel chromatography (elution at 0.2 M-KCl). The final yield was about 12% in terms of binding activity. Properties of the 110kDa component indicate that it is identical with the 'B' subunit described previously [Stokes radius approximately 6.1 nm; sedimentation coefficient, (S20, w) approximately 4S; frictional ratio approximately 1.77]. It reacted with the IgG-G3 polyclonal antibody, but not with BF4 monoclonal antibody raised against the 8S molybdate-stabilized chick oviduct PR and reacting with its 90kDa component. Another progesterone-binding component, corresponding to the 'A' subunit, also previously described, was eluted from the DEAE-Sephacel column at approximately 0.08 M-KCl, and contained a peptide of molecular mass approx. 75-80kDa, which had S20, w approximately 4S in a sucrose gradient. This component was also recognized by IgG-G3, but not by BF4; it was very unstable in terms of hormone-binding activity.

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“…2,4). The reaction is accelerated by temperature increase and/or by high ionic strength [48,49], and in fact is obtainable in vitro in absence of hormone, but more slowly [50,51]. Whole cell experiments favor the physiological significance of the 8s structure, which is certainly not a molybdate artefact 1171, and appears to be present in intact cells [52], the reversible equilibrium 8S+4S being shifted to the right by hormone [53].…”

Section: + + H (R Hsp) > (H-r Hsp)+ (H-r+ Hsp) 8smentioning

confidence: 99%

Steroid hormone antagonists at the receptor level: A role for the heat‐shock protein MW 90,000 (hsp 90)

Baulieu

1987

J of Cellular Biochemistry

141

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Antisteroid hormones compete for hormone binding at the receptor level and prevent the hormonal response. A new concept is proposed for explaining the antiglucocorticosteroid activity of RU 486 in the chick oviduct system. It is based on the ability of the antisteroid to stabilize the hetero-oligomeric 8S-form of the glucocorticosteroid receptor (GR), which involves the interaction of the 94k-receptor and heat-shock protein MW 90,000 (hsp 90). It is proposed that hsp 90 caps the DNA binding site of the receptor, and this prevents it from binding to the DNA of hormone regulatory elements (HRE) and increasing transcription of regulated genes. This paper reviews other antiglucocorticosteroid and antiestrogen systems with reference to this hypothesis and also describes a four-step analysis of the molecular mechanism of antisteroid hormone action at the receptor level.

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Activation of the chick oviduct progesterone receptor by heparin in the presence or absence of hormone

Cited by 42 publications

References 22 publications

Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical crosslinking

Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical crosslinking

Purification by affinity chromatography and immunological characterization of a 110kDa component of the chick oviduct progesterone receptor

Steroid hormone antagonists at the receptor level: A role for the heat‐shock protein MW 90,000 (hsp 90)

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