| First Author | Zou H | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 17 | Pages | 11549-56 |
| PubMed ID | 10206961 | Mgi Jnum | J:320091 |
| Mgi Id | MGI:6867323 | Doi | 10.1074/jbc.274.17.11549 |
| Citation | Zou H, et al. (1999) An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 274(17):11549-56 |
| abstractText | We report here the reconstitution of the de novo procaspase-9 activation pathway using highly purified cytochrome c, recombinant APAF-1, and recombinant procaspase-9. APAF-1 binds and hydrolyzes ATP or dATP to ADP or dADP, respectively. The hydrolysis of ATP/dATP and the binding of cytochrome c promote APAF-1 oligomerization, forming a large multimeric APAF-1.cytochrome c complex. Such a complex can be isolated using gel filtration chromatography and is by itself sufficient to recruit and activate procaspase-9. The stoichiometric ratio of procaspase-9 to APAF-1 is approximately 1 to 1 in the complex. Once activated, caspase-9 disassociates from the complex and becomes available to cleave and activate downstream caspases such as caspase-3. |
