|
KMID : 0624620130460120588
|
|
BMB Reports
2013 Volume.46 No. 12 p.588 ~ p.593
|
|
|
Identification of the novel substrates for caspase-6 in apoptosis using proteomic approaches
|
|
Cho Jin-Hwa
Lee Phil-Young
Son Woo-Chan
Chi Seung-Wook
Park Byoung-Chul
Kim Jeong-Hoon
Park Sung-Goo
|
|
|
Abstract
|
|
|
|
Apoptosis, programmed cell death, is a process involved in the development and maintenance of cell homeostasis in multicellular organisms. It is typically accompanied by the activation of a class of cysteine proteases called caspases. Apoptotic caspases are classified into the initiator caspases and the executioner caspases, according to the stage of their action in apoptotic processes. Although caspase-3, a typical executioner caspase, has been studied for its mechanism and substrates, little is known of caspase-6, one of the executioner caspases. To understand the biological functions of caspase-6, we performed proteomics analyses, to seek for novel caspase-6 substrates, using recombinant caspase-6 and HepG2 extract. Consequently, 34 different candidate proteins were identified, through 2-dimensional electrophoresis/MALDI-TOF analyses. Of these identified proteins, 8 proteins were validated with in vitro and in vivo cleavage assay. Herein, we report that HAUSP, Kinesin5B, GEP100, SDCCAG3 and PARD3 are novel substrates for caspase-6 during apoptosis.
|
|
|
KEYWORD
|
|
|
Apoptosis, Caspase-6, Degradomics, Proteomic screening, Substrate
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|