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Proc Natl Acad Sci U S A. 2007 Sep 4;104(36):14294-9. Epub 2007 Aug 29.

Proteome-wide identification of family member-specific natural substrate repertoire of caspases.

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  • 1School of Pharmacy and Carolina Center for Genome Sciences, University of North Carolina, Chapel Hill, NC 27599, USA.

Abstract

Caspases are proteolytic enzymes that are essential for apoptosis. Understanding the many discrete and interacting signaling pathways mediated by caspases requires the identification of the natural substrate repertoire for each caspase of interest. Using an amplification-based protein selection technique called mRNA display, we developed a high-throughput screen platform for caspase family member specific substrates on a proteome-wide scale. A large number of both known and previously uncharacterized caspase-3 substrates were identified from the human proteome. The proteolytic features of these selected substrates, including their cleavage sites and specificities, were characterized. Substrates that were cleaved only by caspase-8 or granzyme B but not by caspase-3, were readily selected. The method can be widely applied for efficient and systematic identification of the family member specific natural substrate repertoire of any caspase in an organism of interest, in addition to that of numerous other proteases with high specificity.

PMID:
17728405
[PubMed - indexed for MEDLINE]
PMCID:
PMC1958819
Free PMC Article

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