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

  • Mol Cells. 2008 Feb 29;25(1):86-90.
Ah Young Lee  1 ,  Yoora Lee ,  Yun Kyung Park ,  Kwang-Hee Bae ,  Sayeon Cho ,  Do Hee Lee ,  Byoung Chul Park ,  Sunghyun Kang ,  Sung Goo Park
Affiliations
  • 1. Translational Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
PMID: 18319618
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 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.