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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

Authors 

K S NaByoung Chul ParkMi JangS ChoDo Hee LeeSunghyun KangC K LeeKwang-Hee BaeSung Goo Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2007

Citation 

Molecules and Cells, vol. 24, no. 2, pp. 261-267

Keywords 

apoptosiscaspase-3caspase-7protein disulfide isomerasecaspase 3caspase 7disulfideisomerasecell strain MCF 7disulfide bond

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.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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