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Title 

Mining of caspase-7 substrates using a degradomic approach

 

단백질체를 이용한 신규 캐스페이즈7의 기질 발굴

Authors 

Mi JangByoung Chul ParkSunghyun KangD H LeeS ChoSang Chul LeeKwang-Hee BaeSung Goo Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2008

Citation 

Molecules and Cells, vol. 26, no. 2, pp. 152-157

Keywords 

2-DEApoptosisCaspase-7DegradomeVCPcaspaseenzyme substrateactin related protein 2-3 complexactin related protein 2-3 complex 3caspase 3

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 vito and during apoptosis. Cleavage occurred at both DELD307 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.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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