Mining of caspase-7 substrates using a degradomic approach
- Authors
- Jang, Mi; Park, Ellyoung Chul; Kang, Sunghyun; Lee, Do Hee; Cho, Sayeon; Lee, Sang Chul; Bae, Kwang-Hee; Park, Sung Goo
- Issue Date
- Aug-2008
- Publisher
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
- Keywords
- 2-DE; apoptosis; caspase-7; degradome; VCP
- Citation
- MOLECULES AND CELLS, v.26, no.2, pp 152 - 157
- Pages
- 6
- Journal Title
- MOLECULES AND CELLS
- Volume
- 26
- Number
- 2
- Start Page
- 152
- End Page
- 157
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23651
- ISSN
- 1016-8478
0219-1032
- Abstract
- Caspases play critical roles in the execution of apoptosis. Caspase-3 and caspase-7 are closely related in sequence as well as in substrate specificity. The two caspases have overlapping substrate specificities with special preference for the DEVD motif. However, they are targeted to different subcellular locations during apoptosis, implying the existence of substrates specific for one or other caspase. To identify new caspase-7 substrates, we digested cell lysates obtained from the caspase-3-deficient MCF-7 cell line with purified recombinant caspase-7, and analyzed spots that disappeared or decreased by 2-DE (we refer to this as the caspase-7 degradome). Several proteins with various cellular functions underwent caspase-7-dependent proteolysis. The substrates of capase-7 identified by the degradomic approach were rather different from those of caspase-3 (Proteomics, 4, 3429-3435, 2004). Among the candidate substrates, we confirmed that Valosin-containing protein (VCP) was cleaved by both capspase-7 and caspase-3 in vitro and during apoptosis. Cleavage occurred at both DELD 307 and DELD580. The degradomic study yielded several candidate caspase-7 substrates and their further analysis should provide valuables clues to the functions of caspase-7 during apoptosis.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > ETC > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23651)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.