Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 48, Pages 32989-32994Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R109.027946
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Funding
- Research Committee of the University of Patras [C. 186]
- European Union-European Social Fund [PENED2003(03EDelta430)]
- Greek Ministry of Development General Secretariat for Research and Technology
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Kallikrein-related peptidases constitute a single family of 15 (chymo) trypsin-like proteases (KLK1-15) with pleiotropic physiological roles. Aberrant regulation of KLKs has been associated with diverse diseases such as hypertension, renal dysfunction, skin disorders, inflammation, neurodegeneration, and cancer. Recent studies suggested that coordinated activation and regulation of KLK activity are achieved via a complex network of interactions referred to as the KLK activome. However, it remains to be validated whether these hypothetical KLK activation cascade pathways are operative in vivo. In addition, KLKs have emerged as versatile signaling molecules. In summary, KLKs represent attractive biomarkers for clinical applications and potential therapeutic targets for common human pathologies.
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