Protease research in the era of systems biology
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Ulrich auf dem Keller
Abstract
Proteases are specific modulators of signaling molecules and their underlying pathways in addition to their degradative roles. However, proteases do not act alone, but form cascades, circuits and networks that all dynamically interconnect to form the protease web, which defines the proteolytic potential of a cell or tissue in a defined condition. To describe the protease web and its net activity several novel high-throughput proteomic techniques, in the field termed degradomics, have been developed. Emerging systems biology methods to evaluate the expression, activity and substrate discovery of proteases are presented. Understanding the protease web and its perturbations in pathology will help to develop new therapeutics for the treatment of diseases, such as cancer, arthritis and chronic obstructive pulmonary diseases.
©2007 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Proteinase Inhibitors and Biological Control – An Attractive International Symposia Series
- Two decades of thyroglobulin type-1 domain research
- Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
- Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells
- ‘Species’ of peptidases
- Protease research in the era of systems biology
- Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities
- Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
- Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
- Cellular localization of MAGI-1 caspase cleavage products and their role in apoptosis
- Differential methylation kinetics of individual target site strands by T4Dam DNA methyltransferase
- Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
- Defining the extended substrate specificity of kallikrein 1-related peptidases
- Latent MMP-9 is bound to TIMP-1 before secretion
- Novel expression of kallikreins, kallikrein-related peptidases and kinin receptors in human pleural mesothelioma
- Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease
- Clinical chemistry reference database for Wistar rats and C57/BL6 mice
Artikel in diesem Heft
- Proteinase Inhibitors and Biological Control – An Attractive International Symposia Series
- Two decades of thyroglobulin type-1 domain research
- Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
- Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells
- ‘Species’ of peptidases
- Protease research in the era of systems biology
- Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities
- Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
- Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
- Cellular localization of MAGI-1 caspase cleavage products and their role in apoptosis
- Differential methylation kinetics of individual target site strands by T4Dam DNA methyltransferase
- Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
- Defining the extended substrate specificity of kallikrein 1-related peptidases
- Latent MMP-9 is bound to TIMP-1 before secretion
- Novel expression of kallikreins, kallikrein-related peptidases and kinin receptors in human pleural mesothelioma
- Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease
- Clinical chemistry reference database for Wistar rats and C57/BL6 mice
