NF-kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells

Proc Natl Acad Sci U S A. 2000 May 23;97(11):6055-60. doi: 10.1073/pnas.100119497.

Abstract

Epstein-Barr virus (EBV) transforms B lymphocytes into lymphoblastoid cell lines usurping the Notch and tumor necrosis factor receptor pathways to effect transcription including NF-kappaB activation. To determine whether NF-kappaB activity is essential in the growth and survival of EBV-transformed lymphoblastoid cell lines, a nondegradable IkappaBalpha mutant was expressed under tetracycline regulation. Despite continued Bcl-2 and Bcl-x/L expression, NF-kappaB inhibition induced apoptosis as evidenced by poly(ADP-ribose) polymerase cleavage, nuclear condensation and fragmentation, and hypodiploid DNA content. Both caspase 3 and 8 activation and loss of mitochondrial membrane potential were observed in apoptotic cells. However, caspase inhibition failed to block apoptosis. These experiments indicate that NF-kappaB inhibitors may be useful in the therapy of EBV-induced cellular proliferation.

Publication types

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

MeSH terms

  • Amino Acid Chloromethyl Ketones / pharmacology
  • Apoptosis / physiology*
  • B-Lymphocytes / cytology*
  • B-Lymphocytes / virology
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspase Inhibitors
  • Caspases / metabolism
  • Cell Cycle / drug effects
  • Cell Line, Transformed / cytology
  • Cell Transformation, Viral*
  • Cysteine Proteinase Inhibitors / pharmacology
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / physiology*
  • Drug Design
  • Flow Cytometry
  • Gene Expression Regulation
  • Herpesvirus 4, Human / physiology*
  • Humans
  • I-kappa B Proteins*
  • Intracellular Membranes / physiology
  • Lymphoproliferative Disorders / drug therapy
  • Lymphoproliferative Disorders / virology
  • Membrane Potentials
  • Microscopy, Confocal
  • Minor Histocompatibility Antigens
  • Mitochondria / physiology
  • NF-KappaB Inhibitor alpha
  • NF-kappa B / antagonists & inhibitors
  • NF-kappa B / physiology*
  • Protein Biosynthesis
  • Proteins / genetics
  • Proto-Oncogene Proteins c-bcl-2*
  • Recombinant Fusion Proteins / physiology
  • Transfection

Substances

  • Amino Acid Chloromethyl Ketones
  • BCL2-related protein A1
  • Caspase Inhibitors
  • Cysteine Proteinase Inhibitors
  • DNA-Binding Proteins
  • I-kappa B Proteins
  • Minor Histocompatibility Antigens
  • NF-kappa B
  • NFKBIA protein, human
  • Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Fusion Proteins
  • benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
  • NF-KappaB Inhibitor alpha
  • CASP3 protein, human
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspases