Disentanglement of protease substrate repertoires
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Petra Van Damme
Abstract
Identification of protease substrates and detailed characterization of processed sites are essential for understanding the biological function of proteases. Because of inherent complexity reasons, this however remains a formidable analytical challenge, illustrated by the fact that the majority of the more than 500 human proteases are uncharacterized to date. Recently, in addition to conventional genetic and biochemical approaches, diverse quantitative peptide-centric proteomics approaches, some of which selectively recover N-terminal peptides, have emerged. These latter proteomic technologies in particular allow the identification of natural protease substrates and delineation of cleavage sites in a complex, natural background of thousands of different proteins. We here review current biochemical, genetic and proteomic methods for global analysis of substrates of proteases and discuss selected applications.
©2008 by Walter de Gruyter Berlin New York
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- The histone H1 family: specific members, specific functions?
- ATP-dependent chromatosome remodeling
- Role of histone modifications in defining chromatin structure and function
- Differential loss of histone H3 isoforms mono-, di- and tri-methylated at lysine 4 during X-inactivation in female embryonic stem cells
- Disentanglement of protease substrate repertoires
- p53-dependent repression of the human MCL-1 gene encoding an anti-apoptotic member of the BCL-2 family: the role of Sp1 and of basic transcription factor binding sites in the MCL-1 promoter
- 5′-End maturation of tRNA in Aquifex aeolicus
- Smurf1 directly targets hPEM-2, a GEF for Cdc42, via a novel combination of protein interaction modules in the ubiquitin-proteasome pathway
- Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform
- Human butyrylcholinesterase components differ in aryl acylamidase activity
- Ribosome display and selection of human anti-CD22 scFvs derived from an acute lymphocytic leukemia patient
- Sub-chronic administration of the 11β-HSD1 inhibitor, carbenoxolone, improves glucose tolerance and insulin sensitivity in mice with diet-induced obesity
- Inhibitory effect of the sugarcane cystatin CaneCPI-4 on cathepsins B and L and human breast cancer cell invasion
Articles in the same Issue
- Highlight: 59th Mosbach Kolloquium
- The role of long non-coding RNAs in chromatin structure and gene regulation: variations on a theme
- The histone H1 family: specific members, specific functions?
- ATP-dependent chromatosome remodeling
- Role of histone modifications in defining chromatin structure and function
- Differential loss of histone H3 isoforms mono-, di- and tri-methylated at lysine 4 during X-inactivation in female embryonic stem cells
- Disentanglement of protease substrate repertoires
- p53-dependent repression of the human MCL-1 gene encoding an anti-apoptotic member of the BCL-2 family: the role of Sp1 and of basic transcription factor binding sites in the MCL-1 promoter
- 5′-End maturation of tRNA in Aquifex aeolicus
- Smurf1 directly targets hPEM-2, a GEF for Cdc42, via a novel combination of protein interaction modules in the ubiquitin-proteasome pathway
- Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform
- Human butyrylcholinesterase components differ in aryl acylamidase activity
- Ribosome display and selection of human anti-CD22 scFvs derived from an acute lymphocytic leukemia patient
- Sub-chronic administration of the 11β-HSD1 inhibitor, carbenoxolone, improves glucose tolerance and insulin sensitivity in mice with diet-induced obesity
- Inhibitory effect of the sugarcane cystatin CaneCPI-4 on cathepsins B and L and human breast cancer cell invasion
