Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis = 세포사멸 동안의 caspase-3과 -7에 의한 PDI의 절단

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Title
Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis = 세포사멸 동안의 caspase-3과 -7에 의한 PDI의 절단
Author(s)
K S Na; Byoung Chul Park; Mi Jang; S Cho; Do Hee Lee; Sunghyun Kang; C K Lee; Kwang-Hee BaeSung Goo Park
Bibliographic Citation
Molecules and Cells, vol. 24, no. 2, pp. 261-267
Publication Year
2007
Abstract
Apoptotic signals are typically accompanied by activation of aspartate-specific cysteine proteases called caspases, and caspase-3 and -7 play crucial roles in the execution of apoptosis. Previously, using the proteomic approach, protein disulfide isomerase (PDI) was found to be a candidate substrate of caspase-7. This abundant 55 kDa protein introduces disulfide bonds into proteins (via its oxidase activity) and catalyzes the rearrangement of incorrect disulfide bonds (via its isomerase activity). PDI is abundant in the ER but is also found in non-ER locations. In this study we demonstrated that PDI is cleaved by caspase-3 and -7 in vitro. In addition, in vivo experiment showed that it is cleaved during etoposide-induced apoptosis in HL-60 cells. Subcellular fractionation showed that PDI was also present in the cytosol. Furthermore, only cytosolic PDI was clearly digested by caspase-3 and -7. It was also confirmed by confocal image analysis that PDI and caspase-7 partially co-localize in both resting and apoptotic MCF-7 cells. Overexpression of cytosolic PDI (ER retention sequence deleted) inhibited cell death after an apoptotic stimulus. These data indicate that cytosolic PDI is a substrate of caspase-3 and -7, and that it has an anti-apoptotic action.
Keyword
apoptosiscaspase-3caspase-7protein disulfide isomerase
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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