Mechanisms of Bcl-2 protein function

• Wang, H.G. ^[1] ; Reed, J.C. ^[1]
  1. [1] The Burnham Institute, Program on Apoptosis & Cell Death Research, La Jolla, CA, USA
• Localización: Histology and histopathology: cellular and molecular biology, ISSN-e 1699-5848, ISSN 0213-3911, Vol. 13, Nº. 2, 1998, págs. 521-530
• Idioma: inglés
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• Resumen

  • The 8c1-2 protein blocks a distal step in an evolutionarily conserved pathway for programmed cell death and apoptosis. The gene encoding this protein was first discovered because of its involvement in the t(14;18) chromosomal translocations commonly found in 8-cell lymphomas. Overexpression of 8c1-2 also occurs in many other types of human cancers, and prevents cell death induced by nearly all anticancer drugs and radiation. Since the discovery of 8c1-2 over ten years ago, several cellular and viral homologs have been identified, some of which suppress cell death and others which promote apoptosis. Many of these proteins can interact with each other through a complex network of homo- and heterodimers. Though functionally important, dimerization events still do not explain in a broader sense how these proteins actually control cell life and death. Recent findings that BcI-2 can function both as an ion channel and as an adapter or docking protein however are beginning to provide insights into the molecular mechanisms through which these proteins regulate the programmed cell death pathway in normalcy and disease .