Akt inhibition upregulates FasL, downregulates c-FLIPs and induces caspase-8-dependent cell death in Jurkat T lymphocytes

Cell Death Differ. 2005 Mar;12(3):233-42. doi: 10.1038/sj.cdd.4401549.

Abstract

In T lymphocytes, the role of Akt in regulating Fas/Fas ligand (FasL)-mediated apoptotic signaling and death is not clearly understood. In this study, we observed that inhibition of Akt causes enhanced expression of FasL mRNA and protein and increased death-inducing signaling complex (DISC) formation with Fas-associated death domain (FADD) and procaspase-8 recruitment. Also, caspase-8 was activated at the DISC with accompanying decrease in c-FLIPs expression. FasL neutralizing antibody significantly decreased apoptotic death in the Akt-inhibited T cells. Additionally, Akt inhibition-induced Fas signaling was observed to link to the mitochondrial pathway via Bid cleavage. Further, inhibition of caspase-8 activity effectively blocked the loss of mitochondrial membrane potential and DNA fragmentation, suggesting that DISC formation and subsequent caspase-8 activation are critical initiating events in Akt inhibition-induced apoptotic death in T lymphocytes. These data demonstrate yet another important survival function governed by Akt kinase in T lymphocytes, which involves the regulation of FasL expression and consequent apoptotic signaling.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • BH3 Interacting Domain Death Agonist Protein
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Carrier Proteins / metabolism
  • Caspase 8
  • Caspases / metabolism*
  • Chromones / pharmacology
  • Down-Regulation
  • Fas Ligand Protein
  • Fas-Associated Death Domain Protein
  • Humans
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Jurkat Cells
  • Membrane Glycoproteins / biosynthesis*
  • Membrane Potentials
  • Mitochondria / physiology
  • Morpholines / pharmacology
  • Phosphoinositide-3 Kinase Inhibitors
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / antagonists & inhibitors*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Signal Transduction
  • T-Lymphocytes / metabolism*
  • Up-Regulation

Substances

  • Adaptor Proteins, Signal Transducing
  • BH3 Interacting Domain Death Agonist Protein
  • BID protein, human
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • CFLAR protein, human
  • Carrier Proteins
  • Chromones
  • FADD protein, human
  • FASLG protein, human
  • Fas Ligand Protein
  • Fas-Associated Death Domain Protein
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Morpholines
  • Phosphoinositide-3 Kinase Inhibitors
  • Proto-Oncogene Proteins
  • 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
  • AKT1 protein, human
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • CASP8 protein, human
  • Caspase 8
  • Caspases