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Curr Opin Chem Biol. 2007 Feb;11(1):36-45. Epub 2006 Dec 27.

Proteomic discovery of protease substrates.

Author information

1
The UBC Centre for Blood Research, Departments of Oral Biological & Medical Sciences, and Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.

Abstract

Elucidation of in vivo substrate degradomes of a protease is a daunting endeavor because of the large number of proteins in a proteome and often minute and transient amounts of key substrates. Proteomic substrate screens for proteases are currently experiencing impressive progress. Mass spectrometry-based global proteome analysis, interfaced with liquid-chromatography and together with stable isotope labeling strategies, has provided increased coverage and sensitivity for quantitative proteomics. ICAT and iTRAQ labeling have been used to identify a plethora of new matrix metalloproteinase substrates. Emerging techniques focus on the quantitative analysis of proteolytically generated neo amino-termini, which we call terminopes, on a system-wide basis. In vivo SILAC pulse-chase experiments have also enabled the study of individual protein turnover and global proteome dynamics in cells and whole organisms. Together with activity-based probes for the profiling of functional proteases, there is now in place an array of complementary technologies to dissect the 'protease web' and its distortion in pathology.

PMID:
17194619
DOI:
10.1016/j.cbpa.2006.11.037
[Indexed for MEDLINE]

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