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

Autor:	Ah Young, Lee, Yoora, Lee, Yun Kyung, Park, Kwang-Hee, Bae, Sayeon, Cho, Do Hee, Lee, Byoung Chul, Park, Sunghyun, Kang, Sung Goo, Park
Rok vydání:	2008
Předmět:	Aspartic Acid Caspase 3 Humans Proteins Apoptosis Blood Proteins Adaptor Proteins Signal Transducing Cell Line
Zdroj:	Molecules and cells. 25(1)
ISSN:	1016-8478
Popis:	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 Asp(127), 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::f52197001e5f8195ac074d8bda8f51d3 https://pubmed.ncbi.nlm.nih.gov/18319618 Zobrazit plný text záznamu Full text from SpringerLink