| First Author | Kuida K | Year | 2000 |
| Journal | Int J Biochem Cell Biol | Volume | 32 |
| Issue | 2 | Pages | 121-4 |
| PubMed ID | 10687948 | Mgi Jnum | J:60453 |
| Mgi Id | MGI:1353334 | Doi | 10.1016/s1357-2725(99)00024-2 |
| Citation | Kuida K (2000) Caspase-9. Int J Biochem Cell Biol 32(2):121-4 |
| abstractText | Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP. The resultant complex recruits Caspase-9 leading to its activation. Activated Caspase-9 cleaves downstream caspases such as Caspase-3, -6 and -7 initiating the caspase cascade. The majority of homozygous Caspase-9 null mice die perinatally with a markedly enlarged and malformed cerebrum caused by a reduction of apoptosis during early brain development. Thus, Caspase-9 function is essential for apoptosis during normal development of the central nervous system. These data suggest that inhibition of Caspase-9 activity would render opportunity to treat patients suffering from neurological diseases such as stroke, neurodegenerative diseases or brain injury caused by hypoxia. |
