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Interdependence of kallikrein-related peptidases in proteolytic networks
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Nathalie Beaufort
Published/Copyright:
March 20, 2010
Abstract
Human kallikrein-related peptidases (KLKs) are 15 homologous serine proteases involved in several (patho)physiological processes, including cancer. Secreted as precursors, they are activated upon proteolytic release of a short pro-peptide. We searched for interconnection of KLKs within extracellular proteolytic networks leading to activation of protease zymogens and found that (i) pro-KLK activation by other KLKs is scarce, with the exception of pro-KLK11, which is efficiently activated by KLK4 and 5; (ii) pro-KLK4 is activated by matrix metalloproteinase 3; and (iii) trypsin-like KLKs efficiently activate the serine protease urokinase. Our observations provide new insights into the regulation of these important tumor-associated proteases.
Received: 2010-1-5
Accepted: 2010-2-9
Published Online: 2010-3-20
Published in Print: 2010-5-1
©2010 by Walter de Gruyter Berlin New York
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Keywords for this article
cancer;
matrix metalloproteinases;
proteases;
urokinase;
zymogen activation
Articles in the same Issue
- REVIEW
- Chaperone-assisted degradation: multiple paths to destruction
- MINIREVIEWS
- Principles, implementation, and application of biology-oriented synthesis (BIOS)
- The molecular biology of moenomycins: towards novel antibiotics based on inhibition of bacterial peptidoglycan glycosyltransferases
- Kallikrein-related peptidase genes as promising biomarkers for prognosis and monitoring of human malignancies
- GENES AND NUCLEIC ACIDS
- Zinc supplement greatly improves the condition of parkin mutant Drosophila
- MOLECULAR MEDICINE
- Differential role of cathepsins B and L in autophagy-associated cell death induced by arsenic trioxide in U87 human glioblastoma cells
- CELL BIOLOGY AND SIGNALING
- Role of N-acetyl-N-nitroso-tryptophan as nitric oxide donor in the modulation of HIF-1-dependent signaling
- The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity
- PROTEOLYSIS
- Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates
- Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor
- Expression and activity profiling of selected cysteine cathepsins and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis
- Interdependence of kallikrein-related peptidases in proteolytic networks
