CLONING AND REGULATION BY GLUCOCORTICOID RECEPTOR LIGANDS OF A RAT HSP90

被引：15

作者：

MCGUIRE, JA

POELLINGER, L

WIKSTROM, AC

GUSTAFSSON, JA

机构：

[1] Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital F60, 141 86 Huddinge, Novum

来源：

JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1992年 / 42卷 / 08期

关键词：

D O I：

10.1016/0960-0760(92)90089-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have isolated a full length cDNA that encodes a heat shock protein, hsp90, from a rat brain library and present the nucleotide sequence and deduced amino acid sequence. Comparison of the entire nucleotide sequence with mouse hsp84 and human hsp90-beta cDNAs reveal sequence similarities of 92 and 87%, respectively. The coding region of 2172 nucleotides corresponds to a polypeptide chain of 724 amino acids. Comparison with mouse hsp84 and human hsp90-beta amino acid sequences indicates a similarity of 97%, respectively. Characterization of the constitutive expression of this cDNA both by RNA blot hybridization and immunoblotting, reveals that it is expressed in all rat tissues examined. Hsp90 has been shown to form a transient complex with steroid hormone receptors. In order to further elucidate the role of hsp90 in the endocrine response of cells, we have examined the effects of dexamethasone and RU38486 on the level of hsp90 mRNA in a system in which glucocorticoids down-regulate glucocorticoid receptor mRNA levels. In this system, a subtle but reproducible approx. 2-fold decrease in hsp90 mRNA levels is observed after 48 h treatment with dexamethasone.

引用

页码：813 / 822

页数：10

共 38 条

[1] REGULATION OF HEAT-SHOCK PROTEIN-SYNTHESIS BY GONADOTROPINS IN CULTURED GRANULOSA-CELLS [J].

BENZEEV, A ;

AMSTERDAM, A .

ENDOCRINOLOGY, 1989, 124 (05) :2584-2594

[2] THE CDNA-DERIVED AMINO-ACID SEQUENCE OF CHICK HEAT-SHOCK PROTEIN M 90,000 (HSP 90) REVEALS A DNA LIKE STRUCTURE - POTENTIAL SITE OF INTERACTION WITH STEROID-RECEPTORS [J].

BINART, N ;

CHAMBRAUD, B ;

DUMAS, B ;

ROWLANDS, DA ;

BIGOGNE, C ;

LEVIN, JM ;

GARNIER, J ;

BAULIEU, EE ;

CATELLI, MG .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 159 (01) :140-147

[3]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[4] THE SPECIFIC INTERACTION OF THE ROUS-SARCOMA VIRUS TRANSFORMING PROTEIN, PP60SRC, WITH 2 CELLULAR PROTEINS [J].

BRUGGE, JS ;

ERIKSON, E ;

ERIKSON, RL .

CELL, 1981, 25 (02) :363-372

[5]

BRUGGE JS, 1986, CURR TOP MICROBIOL, V123, P1

[6]

CIDLOWSKI JA, 1981, ENDOCRINOLOGY, V109, P1975

[7] RETINOIC ACID RECEPTOR BELONGS TO A SUBCLASS OF NUCLEAR RECEPTORS THAT DO NOT FORM DOCKING COMPLEXES WITH HSP90 [J].

DALMAN, FC ;

STURZENBECKER, LJ ;

LEVIN, AA ;

LUCAS, DA ;

PERDEW, GH ;

PETKOVITCH, M ;

CHAMBON, P ;

GRIPPO, JF ;

PRATT, WB .

BIOCHEMISTRY, 1991, 30 (22) :5605-5608

[8] REQUIREMENT OF HORMONE FOR THERMAL-CONVERSION OF THE GLUCOCORTICOID RECEPTOR TO A DNA-BINDING STATE [J].

DENIS, M ;

POELLINGER, L ;

WIKSTOM, AC ;

GUSTAFSSON, JA .

NATURE, 1988, 333 (6174) :686-688

[9]

DENIS M, 1987, J BIOL CHEM, V262, P11803

[10] REGULATION OF GLUCOCORTICOID RECEPTOR EXPRESSION - EVIDENCE FOR TRANSCRIPTIONAL AND POSTTRANSLATIONAL MECHANISMS [J].

DONG, Y ;

POELLINGER, L ;

GUSTAFSSON, JA ;

OKRET, S .

MOLECULAR ENDOCRINOLOGY, 1988, 2 (12) :1256-1264

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