Abstract：
:The cytosolic protein APAF1, human homolog of C. elegans CED-4, participates in the CASPASE 9 (CASP9)-dependent activation of CASP3 in the general apoptotic pathway. We have generated by gene trap a null allele of the murine Apaf1. Homozygous mutants die at embryonic day 16.5. Their phenotype includes severe craniofacial malformations, brain overgrowth, persistence of the interdigital webs, and dramatic alterations of the lens and retina. Homozygous embryonic fibroblasts exhibit reduced response to various apoptotic stimuli. In situ immunodetection shows that the absence of Apaf1 protein prevents the activation of Casp3 in vivo. In agreement with the reported function of CED-4 in C. elegans, this phenotype can be correlated with a defect of apoptosis. Our findings suggest that Apaf1 is essential for Casp3 activation in embryonic brain and is a key regulator of developmental programmed cell death in mammals.
journal_name
Celljournal_title
Cellauthors
Cecconi F,Alvarez-Bolado G,Meyer BI,Roth KA,Gruss Pdoi
10.1016/s0092-8674(00)81732-8subject
Has Abstractpub_date
1998-09-18 00:00:00pages
727-37issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81732-8journal_volume
94pub_type
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