Activation of caspases triggered by cytochrome c in vitro

FEBS Letters

Humke, Eric W¹  Dixit, Vishva M²  Pan, Guoha³ 

[1] Department of Cellular and Molecular Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA;Department of Molecular Oncology, Genentech, Inc., 1 DNA Way, Bldg. 10, Room 290, Mail Stop 40, South San Francisco, CA 94080, USA;Department of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA

关键词: Apoptosis;    Cytochrome c;    dATP;    Apaf-1;    Caspase;    Cell-free;   

DOI  :  10.1016/S0014-5793(98)00330-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previous studies have shown that Apaf-1 and caspase-9 in the presence of cytochrome c and dATP can form an initiating complex for an apoptotic protease cascade. We have developed a cytochrome c-dependent in vitro system in which caspases downstream of this initiation complex are activated. The activation of caspase-9 from zymogen form to active dimeric protease requires intrinsic enzymatic activity. In contrast, caspase-3 and caspase-7 zymogens are proteolytically processed by active caspase-9. Activation of the above caspases is blocked by a dominant negative form of caspase-9. The in vitro system displays surprising specificity in that other caspases, including 1, 2, 4, 8, 10, and 13, are not activated.

【 授权许可】

Unknown