Apoptosis in cancer: cause and cure

Bioessays. 2000 Nov;22(11):1007-17. doi: 10.1002/1521-1878(200011)22:11<1007::AID-BIES7>3.0.CO;2-4.


The accumulation of neoplastic cells can occur through enhanced proliferation, diminished cell turnover, or a combination of both processes. Although the potential contribution of diminished cell turnover to tumor development has been appreciated for a decade, more recent studies in animal models and clinical cancer specimens have elucidated the mechanisms by which alterations in the apoptotic machinery contribute to the process of carcinogenesis. At the same time, a different group of studies have demonstrated the feasibility of eliminating neoplastic cells by selectively inducing apoptosis. In this essay, we review recent developments in the fields of carcinogenesis and molecular therapeutics in light of new understanding of apoptotic pathways.

Publication types

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

MeSH terms

  • Animals
  • Apoptosis*
  • Caspases / metabolism
  • Enzyme Activation
  • Fusion Proteins, bcr-abl / metabolism
  • Humans
  • Inhibitor of Apoptosis Proteins
  • Neoplasms* / metabolism
  • Neoplasms* / therapy
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein-Serine-Threonine Kinases*
  • Proteins / metabolism
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Receptors, TNF-Related Apoptosis-Inducing Ligand
  • Receptors, Tumor Necrosis Factor / metabolism
  • Tumor Cells, Cultured
  • bcl-2-Associated X Protein


  • Inhibitor of Apoptosis Proteins
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Receptors, TNF-Related Apoptosis-Inducing Ligand
  • Receptors, Tumor Necrosis Factor
  • TNFRSF10A protein, human
  • TNFRSF10B protein, human
  • bcl-2-Associated X Protein
  • Phosphatidylinositol 3-Kinases
  • Fusion Proteins, bcr-abl
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Caspases