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KMID : 0578320080250010086
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Molecules and Cells
2008 Volume.25 No. 1 p.86 ~ p.90
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HS 1-Associated Protein X-1 Is Cleaved by Caspase-3 During Apoptosis
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Lee A-Young
Lee You-Ra
Park Yun-Kyung
Cho Sa-yoen
Park Byoung-Chul
Park Byoung-Chul
Kang Sung-Hyun
Park Sung-Goo
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Abstract
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Caspase-3 (CASP3) plays a key role in apoptosis. In this study, HAX-1 was identified as a new substrate of CASP3 during apoptosis. HAX-1 was cleaved by CASP3 during etoposide-(ETO) induced apoptosis, and this event was inhibited by a CASP3-specific inhibitor. The cleavage site of HAX-1, at Asp127, was located using N-terminal amino acid sequencing of in vitro cleavage products of recombinant HAX-1. Overexpression of HAX-1 inhibited ETO-induced apoptotic cell death. It also inhibited CASP3 activity. Together, these results suggest that HAX-1, a substrate of CASP3, inhibits the apoptotic process by inhibiting CASP3 activity.
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KEYWORD
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Apoptosis, Caspase-3, HAX-1.
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