HS 1-associated protein X-1 is cleaved by caspase-3 during apoptosis = 세포사멸과정중의 캐스페이즈에 의한 Hax-1의 절단

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Title
HS 1-associated protein X-1 is cleaved by caspase-3 during apoptosis = 세포사멸과정중의 캐스페이즈에 의한 Hax-1의 절단
Author(s)
Ah Young Lee; Y R Lee; Y K Park; Kwang-Hee Bae; S Cho; Do Hee Lee; Byoung Chul ParkSunghyun KangSung Goo Park
Bibliographic Citation
Molecules and Cells, vol. 25, no. 1, pp. 86-90
Publication Year
2008
Abstract
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-terminat 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.
Keyword
apoptosiscaspase-3HAX-1
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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