Okadaic acid markedly potentiates the heat-induced hsp 70 promoter activity

N. T. Chang, L. E. Huang, Alice Liu

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

The effects of okadaic acid (OA), a potent and specific inhibitor of serine/threonine phosphatases 2A and 1, on the transient expression of a human hsp 70 promoter-linked chloramphenicol acetyltransferase gene transfected into N-18 mouse neuroblastoma cells were determined. Assays of reporter gene activity showed that nanomolar concentrations of OA markedly potentiated the heat-induced (but not the basal) expression of pHBCAT, a full-length hsp 70 promoter-driven chloramphenicol acetyltransferase gene construct. This effect of OA was dose-dependent and promoter-specific and appeared to be attributable to inhibition of protein phosphatase 2A as opposed to protein phosphatase 1. The ability of OA to potentiate the heat- induced expression of pHBCAT appeared to be a feature common to several different cell types examined. We propose that the heat-induced transcriptional activation of heat shock genes is associated with the phosphorylation of component(s) of the transcription complex and that OA enhances this phosphorylation, thereby potentiating the heat-induced hsp 70 promoter activity.

Original languageEnglish (US)
Pages (from-to)1436-1439
Number of pages4
JournalJournal of Biological Chemistry
Volume268
Issue number2
StatePublished - 1993

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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