Caspase-9

K Kuida - The international journal of biochemistry & cell biology, 2000 - Elsevier
K Kuida
The international journal of biochemistry & cell biology, 2000Elsevier
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 …
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.
Elsevier