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Title 

HS 1-associated protein X-1 is cleaved by caspase-3 during apoptosis

 

세포사멸과정중의 캐스페이즈에 의한 Hax-1의 절단

Authors 

Ah Young LeeY R LeeY K ParkKwang-Hee BaeS ChoDo Hee LeeByoung Chul ParkSunghyun KangSung Goo Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2008

Citation 

Molecules and Cells, vol. 25, no. 1, pp. 86-90

Keywords 

apoptosiscaspase-3HAX-1caspase 3HS 1 associated protein X 1inhibitor of apoptosis proteinprotein hax1gene expression regulationprotein analysis

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.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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