Substitution of arginine for cysteine 643 of the glucocorticoid receptor reduces its steroid-binding affinity and transcriptional activity

Cancer Lett. 2002 Jul 8;181(1):109-14. doi: 10.1016/s0304-3835(02)00042-3.

Abstract

To investigate the mechanism for glucocorticoid resistance in leukemic cells, we sequenced the coding region of glucocorticoid receptor (GR) gene in ten Japanese leukemic cells. We identified a novel heterozygous mutation (C643R) in the ligand-binding domain in P30/OHK cells. Western blot analysis for COS-7 cells transfected with the wild-type or C643R mutant GR plasmid revealed similar protein expression levels. In the ligand-binding assay, the dissociation constant of the C643R GR was six-fold higher than that of the wild-type GR. Moreover, the C643R GR showed no transcriptional activity in the luciferase reporter assay.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution*
  • Arginine*
  • Cysteine*
  • DNA Mutational Analysis
  • Dexamethasone / metabolism
  • Humans
  • Leukemia / genetics*
  • Protein Binding
  • Receptors, Glucocorticoid / genetics*
  • Receptors, Glucocorticoid / metabolism*
  • Transcription, Genetic*
  • Tumor Cells, Cultured

Substances

  • Receptors, Glucocorticoid
  • Dexamethasone
  • Arginine
  • Cysteine