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- Identification of the novel substrates for caspase-6 in apoptosis using proteomic approaches
- Jin Hwa Cho; Phil Young Lee; W C Son; Seung-Wook Chi; Byoung Chul Park; Jeong Hoon Kim; Sung Goo Park
- Bibliographic Citation
- BMB Reports, vol. 46, no. 12, pp. 588-593
- Publication Year
- 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.
- Apoptosis; Caspase-6; Degradomics; Proteomic screening; Substrate
- South Korea
- Appears in Collections:
- Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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