Apoptosis induced by (E)-5-(2-bromovinyl)-2'-deoxyuridine in varicella zoster virus thymidine kinase-expressing cells is driven by activation of c-Jun/activator protein-1 and Fas ligand/caspase-8

Mol Pharmacol. 2003 Feb;63(2):439-49. doi: 10.1124/mol.63.2.439.

Abstract

The molecular mode of cell killing by the antiviral drug (E)-5-(2-bromovinyl-2'-deoxyuridine (BVDU) was studied in Chinese hamster ovary (CHO) cells stably transfected with the thymidine kinase gene (tk) of varicella zoster virus (CHO-VZVtk). The colony-forming ability of the cells was reduced to <1% at a concentration of approximately 1 microM BVDU, whereas for nontransfected cells or cells transfected with tk gene of herpes simplex virus type 1 (CHO-HSVtk), a 1000-fold higher dose was required to achieve the same response. BVDU inhibited thymidylate synthase in CHO-VZVtk but not in CHO-HSVtk and control cells. On the other hand, the drug was incorporated into DNA of VZVtk- and HSVtk-expressing cells to nearly equal amounts. Because coexposure of CHO-VZVtk cells to exogenous thymidine protected them from BVDU-induced cell killing, the cells obviously die because of thymidine depletion. At highly cytotoxic BVDU doses (50 microM) and longer exposure times (24-48 h), VZVtk cells were blocked to some extent in S and G2/M phase and underwent apoptosis (48-72 h). Not only apoptosis but also necrosis was induced. The findings also show that the drug causes the induction of c-Jun and the activation of activator protein-1 resulting in increased level of Fas ligand (FasL) and caspase-8/-3 activation. Bid and poly(ADP-ribose) polymerase were cleaved by caspases. Expression of Bax increased, whereas Bcl-2/Bcl-x(L) remained unchanged. Transfection of dominant-negative Fas-associated death domain and inhibition of caspase-8 by N-benzyloxycarbonyl-IETD-fluoromethyl ketone strongly abrogated BVDU-induced apoptosis, indicating Fas/FasL to be crucially involved. Thus, BVDU-triggered apoptosis differs significantly from that induced by ganciclovir, which induces in the same cellular background the mitochondrial damage pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Animals
  • Antiviral Agents / pharmacology*
  • Apoptosis*
  • Bromodeoxyuridine / analogs & derivatives*
  • Bromodeoxyuridine / pharmacology*
  • CHO Cells
  • Carrier Proteins / biosynthesis
  • Caspase 8
  • Caspase 9
  • Caspases / metabolism
  • Cell Cycle / drug effects
  • Cricetinae
  • DNA / biosynthesis
  • DNA / drug effects
  • DNA / metabolism
  • Fas Ligand Protein
  • Fas-Associated Death Domain Protein
  • Genome
  • Herpesvirus 3, Human / enzymology
  • JNK Mitogen-Activated Protein Kinases
  • Membrane Glycoproteins / metabolism
  • Mitogen-Activated Protein Kinases / metabolism
  • Necrosis
  • Simplexvirus / enzymology
  • Thymidine Kinase / physiology*
  • Thymidylate Synthase / antagonists & inhibitors
  • Transcription Factor AP-1 / metabolism
  • Transcription Factor AP-1 / physiology
  • Transfection

Substances

  • Adaptor Proteins, Signal Transducing
  • Antiviral Agents
  • Carrier Proteins
  • FADD protein, human
  • FASLG protein, human
  • Fas Ligand Protein
  • Fas-Associated Death Domain Protein
  • Membrane Glycoproteins
  • Transcription Factor AP-1
  • brivudine
  • DNA
  • Thymidylate Synthase
  • Thymidine Kinase
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 8
  • Caspase 9
  • Caspases
  • Bromodeoxyuridine