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Cloning of a mu-class glutathione S-transferase complementary DNA and characterization of its glucocorticoid inducibility in a smooth muscle tumor cell line

Academic Article
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Overview

authors

  • Norris, J. S.
  • Schwartz, D. A.
  • Macleod, S. L.
  • Fan, W. M.
  • Obrien, T. J.
  • Harris, S. E.
  • Trifiletti, R.
  • Cornett, L. E.
  • Cooper, T. M.
  • Levi, W. M.
  • Smith, Roy

publication date

  • 1991

journal

  • Molecular Endocrinology  Journal

abstract

  • A cDNA (designated hGSTYBX) encompassing the complete coding sequence of a hamster mu-class glutathione S-transferase (GST) subunit was cloned from a lambda ZAP library constructed with mRNA isolated from triamcinolone acetonide-treated smooth muscle tumor cells (DDT1 MF-2). Analysis of its nucleotide and deduced amino acid sequences demonstrated highest homology to the rat mu-class GST YB2 subunit. In proliferating subconfluent cells, in which constitutive expression of hGSTYBX mRNA was undetectable, glucocorticoid treatment induced hGSTYBX expression after a time lag of 3 h, and maximal induction occurred at 10 h. Nuclear run-on analysis showed that glucocorticoid induction resulted at least in part from an increased rate of transcription. Simultaneous treatment with glucocorticoid and cycloheximide prevented glucocorticoid induction, but had little effect on basal expression in confluent cells. In contrast, cycloheximide treatment 3 h after glucocorticoid treatment resulted in nearly full induction. These results taken together suggest that hGSTYBX induction may be a secondary glucocorticoid response.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Cricetinae
  • Cycloheximide
  • DNA
  • Gene Expression
  • Glucocorticoids
  • Glutathione Transferase
  • Kinetics
  • Molecular Sequence Data
  • Muscle, Smooth
  • RNA, Messenger
  • Triamcinolone Acetonide
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0888-8809

Digital Object Identifier (DOI)

  • 10.1210/mend-5-7-979

PubMed ID

  • 1944302
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Additional Document Info

start page

  • 979

end page

  • 986

volume

  • 5

issue

  • 7

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