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Title 

Identification of caspase-3 degradome by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis

Authors 

Ah Young LeeByoung Chul ParkMi JangS Y ChoDo Hee LeeSang Chul LeeP K MyungSung Goo Park

Publisher 

Wiley-Blackwell

Issue Date 

2004

Citation 

Proteomics, vol. 4, no. 11, pp. 3429-3436

Keywords 

caspase-3degradomematrix-assisted laser desorption/ionization-time of flighttwo-dimensional gel electrophoresisvinculincaspase 3matrix assisted laser desorption ionization time of flight mass spectrometrytwo dimensional gel electrophoresiscaspases

Abstract 

The activation of caspases is a critical event for the execution phase of programmed cell death. Caspases are highly specific in their ability to activate or inhibit many crucial proteins in the cell via site-specific cleavage. To date, more than 60 proteins have been shown to be substrates of one or more caspases in mammalian cells, and the list is still growing. In this study, to identify human caspase-3 substrates, we digested lysates obtained from a caspase-3-deficient MCF-7 cell line with purified caspase-3 and analyzed eliminated or decreased spots by 2-DE. Proteins degraded by caspase-3, termed as caspase-3 degradome, are involved in a variety of cellular functions, such as stress-responsive proteins, signaling molecules, structural proteins, and unclassified proteins. Interestingly, the cellular level of vinculin, a caspase-3 substrate, was dramatically reduced during the apoptotic process, where the expression level of caspase-3 was increased. This degradomic approach could provide a powerful tool in finding physiological substrates of many proteolytic enzymes whose functions remain to be determined.

ISSN 

1615-9853

Link 

http://dx.doi.org/10.1002/pmic.200400979

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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