Cleaved SLPI, a novel biomarker of chymase activity
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Stanley M. Belkowski
Abstract
Secretory leukocyte protease inhibitor (SLPI) is a protease inhibitor of the whey acidic protein-like family inhibiting chymase, chymotrypsin, elastase, proteinase 3, cathepsin G and tryptase. Performing in vitro enzymatic assays using both Western blotting and liquid chromatography/mass spectrometry techniques we showed that, of the proteases known to interact with SLPI, only chymase could uniquely cleave this protein. The peptides of the cleaved SLPI (cSLPI) remain coupled due to the disulfide bonds in the molecule but under reducing conditions the cleavage can be observed as peptide products. Subsequent ex vivo studies confirmed the presence of SLPI in human saliva and its susceptibility to cleavage by chymase. Furthermore, inhibitors of chymase activity are able to inhibit this cleavage. Human saliva from both normal and allergic individuals was analyzed for levels of cSLPI and a correlation between the level of cSLPI and the extent of allergic symptoms was observed, suggesting the application of cSLPI as a biomarker of chymase activity in humans.
©2008 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Review
- Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
- Protein Structure and Function
- The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme
- Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGAP interaction
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- Molecular mechanisms of aromatase inhibition by new A, D-ring modified steroids
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- Putative identification of an amphipathic α-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation
- Proteolysis
- Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
- Cleaved SLPI, a novel biomarker of chymase activity
- Expression of tissue and plasma kallikreins and kinin B1 and B2 receptors in lung cancer
- Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
- Novel Techniques
- Fast in vitro translation system immobilized on a surface via specific biotinylation of the ribosome
