The carboxyl-terminal activation domain of the STAT-1 transcription factor enhances ischemia/reperfusion-induced apoptosis in cardiac myocytes

FASEB J. 2002 Nov;16(13):1841-3. doi: 10.1096/fj.02-0150fje. Epub 2002 Sep 5.

Abstract

We have demonstrated previously that the STAT-1 transcription factor plays a key role in ischemia/reperfusion (I/R)-induced apoptosis in cardiac myocytes. In the present study we assessed which region of the STAT-1 molecule mediates apoptosis in cardiac myocytes. A STAT-1 construct (amino acid 350-750) lacking the N-terminus could enhance I/R-induced apoptosis in cardiac myocytes. However, a STAT-1 construct, which lacks 60 amino acids at the C-terminus (amino acid 691-750), was ineffective in promoting I/R-induced apoptosis in cardiac myocytes. Furthermore, overexpression of a C-terminal STAT-1 construct (amino acid 691-750) containing the transcriptional activation domain, but not the DNA binding domain, strongly enhanced I/R-induced apoptotic cell death. Cardiac myocytes isolated from mice expressing a truncated C-terminal STAT-1 were more sensitive to I/R-induced cell death. Finally, isolated hearts from these animals exposed to I/R injury had larger infarct size and greater number of TUNEL-positive myocytes than control hearts. These studies demonstrate that the C-terminal transactivation domain of STAT-1 is necessary and sufficient for I/R injury-induced apoptosis in cardiac myocytes.

Publication types

  • Retracted Publication

MeSH terms

  • Animals
  • Animals, Newborn
  • Apoptosis / physiology*
  • Binding Sites / genetics
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / physiology*
  • Genotype
  • In Situ Nick-End Labeling
  • Mice
  • Mice, Knockout
  • Myocardial Infarction / genetics
  • Myocardial Infarction / pathology
  • Myocardial Reperfusion Injury / physiopathology*
  • Myocardium / metabolism*
  • Myocardium / pathology
  • Peptide Fragments / genetics
  • Phosphorylation
  • STAT1 Transcription Factor
  • Serine / metabolism
  • Trans-Activators / chemistry
  • Trans-Activators / genetics
  • Trans-Activators / physiology*
  • Transfection

Substances

  • DNA-Binding Proteins
  • Peptide Fragments
  • STAT1 Transcription Factor
  • Stat1 protein, mouse
  • Trans-Activators
  • Serine