Regulation of Apoptosis by AFG3L2, a Potential Oncogene
Abstract
Apoptosis, or programmed cell death, is a vitally important cellular process that is disregulated in many different human diseases, including some neurodegenerative disorders, stroke, and many cancers, including breast cancer (Reed 1998; Lee, Zipfel et al. 1999). Because most chemotherapeutic agents act by inducing apoptosis in the target tissue, it is vitally important to understand apoptotic regulation in order to design more effective chemotherapies. The primary machinery of apoptosis is a family of cysteine proteases called caspases (Cryns and Yuan 1998). These molecules are normally present in the cell as inactive zymogens, and are activated by proteolysis in response to apoptotic stimuli. Some caspases, such as caspase 8, reside on the cell surface and become cleaved as part of the primary response to pro-apoptotic cell-surface ligands such as Fas ligand and TNF alpha (Peitsch and Tschopp 1995), whereas other more downstream caspases, such as caspase 3, are activated by diverse stimuli, including multiple upstream caspases (Li, Nijhawan et al. 1997; Muzio, Salvesen et al. 1997; Stennicke, Jurgensmeier et al. 1998).
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 2002
- Accession Number
- ADA412697
Entities
People
- Jessica S. Tashker
Organizations
- Duke University Hospital