Literature DB >> 3965298

Heteromeric nature of glucocorticoid receptors.

U Gehring, H Arndt.   

Abstract

The wild-type and a mutant receptor of S49.1 lymphoma cells have been shown by photoaffinity labelling to contain steroid-binding polypeptides of Mr 94 000 and 40 000, respectively. We investigated the molybdate-stabilized forms of these receptors and obtained Mr 325 000 and 285 000, respectively, by gel filtration and sedimentation analysis. Mild chymotrypsin treatment of the large wild-type receptor resulted in a form of about Mr 290 000 which contained a steroid-binding polypeptide of Mr 40 000. The data suggest that the high -Mr forms of glucocorticoid receptors are heteromeric in nature and contain one steroid-binding polypeptide per complex.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3965298     DOI: 10.1016/0014-5793(85)80208-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors.

Authors:  D Picard; V Kumar; P Chambon; K R Yamamoto
Journal:  Cell Regul       Date:  1990-02

2.  [Clinical relevance of glucocorticoid receptors in the treatment of lymphoid neoplasias].

Authors:  U Gehring; A D Ho
Journal:  Klin Wochenschr       Date:  1987-03-16

3.  Cloning of the chick hsp 90 cDNA in expression vector.

Authors:  M G Catelli; N Binart; J R Feramisco; D M Helfman
Journal:  Nucleic Acids Res       Date:  1985-09-11       Impact factor: 16.971

Review 4.  The 'active life' of Hsp90 complexes.

Authors:  Chrisostomos Prodromou
Journal:  Biochim Biophys Acta       Date:  2011-08-04
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.