Induction of apoptosis and Fas receptor/Fas ligand expression by ischemia/reperfusion in cardiac myocytes requires serine 727 of the STAT-1 transcription factor but not tyrosine 701

J Biol Chem. 2001 Jul 27;276(30):28340-7. doi: 10.1074/jbc.M101177200. Epub 2001 Apr 17.

Abstract

Previously we reported that ischemia results in apoptosis and is accompanied by phosphorylation on Tyr-701 and increased expression and transcriptional activity of the signal transducer and activator of transcription-1 (STAT-1). In the present study, we show that exposure of cardiomyocytes to ischemia induced the phosphorylation of STAT-1 at another site, Ser-727. Moreover, STAT-1 is critical for the induction of Fas receptor and Fas ligand expression by ischemia/reperfusion (I/R). Transcriptional activation of Fas and FasL was dependent on Ser-727 of STAT-1 but was independent of Tyr-701. Similarly, Ser-727 but not Tyr-701 was required for enhancement of cardiomyocyte cell death by STAT-1 during I/R. In addition, inhibition of the p38 pathway prevented the induction and transcriptional activation of Fas and FasL in cardiac cells exposed to I/R, whereas inhibition of p42/p44 MAPK had no effect. Finally, I/R also induced phosphorylation of STAT-1 on Ser-727 and expression of Fas/FasL in ventricular myocytes in the intact heart ex vivo. These results indicate that Fas/FasL genes and apoptosis are activated by STAT-1 in cardiac myocytes exposed to I/R and these effects are dependent on the Ser-727 but not the Tyr-701 phosphorylation sites of STAT-1.

MeSH terms

  • Animals
  • Animals, Newborn
  • Apoptosis*
  • Blotting, Western
  • Cells, Cultured
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • Enzyme Inhibitors / pharmacology
  • Fas Ligand Protein
  • Imidazoles / pharmacology
  • In Situ Nick-End Labeling
  • Membrane Glycoproteins / biosynthesis*
  • Microscopy, Fluorescence
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinases / metabolism
  • Myocardium / cytology*
  • Phosphorylation
  • Plasmids / metabolism
  • Pyridines / pharmacology
  • Rats
  • Rats, Sprague-Dawley
  • Reperfusion Injury / metabolism*
  • STAT1 Transcription Factor
  • Serine / chemistry
  • Signal Transduction
  • Trans-Activators / chemistry
  • Transcriptional Activation
  • Transfection
  • Tyrosine / chemistry
  • fas Receptor / biosynthesis*
  • p38 Mitogen-Activated Protein Kinases

Substances

  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Fas Ligand Protein
  • Faslg protein, rat
  • Imidazoles
  • Membrane Glycoproteins
  • Pyridines
  • STAT1 Transcription Factor
  • Stat1 protein, rat
  • Trans-Activators
  • fas Receptor
  • Tyrosine
  • Serine
  • DNA
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • SB 203580