Using a Caesalpinia echinata Lam. protease inhibitor as a tool for studying the roles of neutrophil elastase, cathepsin G and proteinase 3 in pulmonary edema

2013 ◽  
Vol 96 ◽  
pp. 235-243 ◽  
Author(s):  
Ilana Cruz-Silva ◽  
Christiane Neuhof ◽  
Andrezza Justino Gozzo ◽  
Viviane Abreu Nunes ◽  
Izaura Yoshico Hirata ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Pulmonary Edema ◽  
Neutrophil Elastase ◽  
Cathepsin G ◽  
Proteinase 3 ◽  
Caesalpinia Echinata

Unopposed Cathepsin G, Neutrophil Elastase, and Proteinase 3 Cause Severe Lung Damage and Emphysema

2014 ◽  
Vol 184 (8) ◽  
pp. 2197-2210 ◽  
Author(s):  
Nicolas Guyot ◽  
Julien Wartelle ◽  
Laurette Malleret ◽  
Alexandre A. Todorov ◽  
Gilles Devouassoux ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Cathepsin G ◽  
Lung Damage ◽  
Proteinase 3 ◽  
Severe Lung

Measurement of Neutrophil Elastase, Proteinase 3, and Cathepsin G Activities using Intramolecularly Quenched Fluorogenic Substrates

2011 ◽  
pp. 125-138 ◽  
Author(s):  
Brice Korkmaz ◽  
Sylvie Attucci ◽  
Christophe Epinette ◽  
Elodie Pitois ◽  
Marie-Lise Jourdan ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Cathepsin G ◽  
Proteinase 3 ◽  
Fluorogenic Substrates

scholarly journals A novel locust (Schistocerca gregaria) serine protease inhibitor with a high affinity for neutrophil elastase

2006 ◽  
Vol 400 (3) ◽  
pp. 467-476 ◽  
Author(s):  
Michèle Brillard-Bourdet ◽  
Ahmed Hamdaoui ◽  
Eric Hajjar ◽  
Christian Boudier ◽  
Nathalie Reuter ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Neutrophil Elastase ◽  
Schistocerca Gregaria ◽  
Serine Protease Inhibitor ◽  
Cathepsin G ◽  
Human Neutrophil Elastase ◽  
Sequence Alignments ◽  
Putative Gene

We have purified to homogeneity two forms of a new serine protease inhibitor specific for elastase/chymotrypsin from the ovary gland of the desert locust Schistocerca gregaria. This protein, greglin, has 83 amino acid residues and bears putative phosphorylation sites. Amino acid sequence alignments revealed no homology with pacifastin insect inhibitors and only a distant relationship with Kazal-type inhibitors. This was confirmed by computer-based structural studies. The most closely related homologue is a putative gene product from Ciona intestinalis with which it shares 38% sequence homology. Greglin is a fast-acting and tight binding inhibitor of human neutrophil elastase (kass=1.2×107 M−1·s−1, Ki=3.6 nM) and subtilisin. It also binds neutrophil cathepsin G, pancreatic elastase and chymotrypsin with a lower affinity (26 nM≤Ki≤153 nM), but does not inhibit neutrophil protease 3 or pancreatic trypsin. The capacity of greglin to inhibit neutrophil elastase was not significantly affected by exposure to acetonitrile, high temperature (90 °C), low or high pH (2.5–11.0), N-chlorosuccinimide-mediated oxidation or the proteolytic enzymes trypsin, papain and pseudolysin from Pseudomonas aeruginosa. Greglin efficiently inhibits the neutrophil elastase activity of sputum supernatants from cystic fibrosis patients. Its biological function in the locust ovary gland is currently unknown, but its physicochemical properties suggest that it can be used as a template to design a new generation of highly resistant elastase inhibitors for treating inflammatory diseases.

Neutrophil elastase increases secretory leukocyte protease inhibitor transcript levels in airway epithelial cells

1993 ◽  
Vol 265 (3) ◽  
pp. L286-L292 ◽  
Author(s):  
J. M. Abbinante-Nissen ◽  
L. G. Simpson ◽  
G. D. Leikauf
Keyword(s):  
Epithelial Cells ◽  
Protease Inhibitor ◽  
Neutrophil Elastase ◽  
Airway Epithelial Cells ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Cathepsin G ◽  
Dependent Manner ◽  
Airway Epithelial ◽  
Necrosis Factor Alpha ◽  
Transcript Levels

Airway inflammation is often associated with the infiltration of activated neutrophils and subsequent protease release. Although aiding in the digestion and phagocytosis of foreign proteins and microorganisms, neutrophil proteases can indiscriminately damage healthy lung tissue. In the conducting airway, proteases, particularly neutrophil elastase, are counter-balanced by several antiproteases, including secretory leukocyte protease inhibitor (SLPI). SLPI can be produced locally by a number of cells including the airway epithelial cell. To examine the effects of neutrophil granule components on SLPI transcript levels, airway epithelial cells were treated (up to 96 h) with elastase, other proteases, or enzymes isolated from human sputum. We found that neutrophil elastase increased SLPI transcript levels in primary and transformed human airway epithelial cells in a time- and dose-dependent manner. Other neutrophil products, such as cathepsin G, myeloperoxidase, and lysozyme, had little or no effect on SLPI transcript levels. However, two nonneutrophil proteases, trypsin and pancreatic elastase, also increased SLPI transcript levels at higher doses than that required of neutrophil elastase. Two inflammatory cytokines, tumor necrosis factor-alpha and interleukin-8, produced little or no effect on SLPI transcript levels. This study demonstrates one way in which SLPI is regulated, via a protease that it inhibits, neutrophil elastase.

Cleaved SLPI, a novel biomarker of chymase activity

2008 ◽  
Vol 389 (9) ◽  
Author(s):  
Stanley M. Belkowski ◽  
John Masucci ◽  
Andrew Mahan ◽  
Jukka Kervinen ◽  
Matthew Olson ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Disulfide Bonds ◽  
Ex Vivo ◽  
Human Saliva ◽  
Cathepsin G ◽  
Proteinase 3 ◽  
Liquid Chromatography Mass Spectrometry ◽  
Enzymatic Assays ◽  
Reducing Conditions

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.

Neutrophil elastase enzymatically antagonizes the in vitro action of G-CSF: implications for the regulation of granulopoiesis

Blood ◽  
2003 ◽  
Vol 101 (5) ◽  
pp. 1752-1758 ◽  
Author(s):  
Frank El Ouriaghli ◽  
Hiroshi Fujiwara ◽  
J. Joseph Melenhorst ◽  
Giuseppe Sconocchia ◽  
Nancy Hensel ◽  
...  
Keyword(s):  
Negative Feedback ◽  
Neutrophil Elastase ◽  
Serine Proteases ◽  
Cathepsin G ◽  
Proteinase 3 ◽  
Gm Csf ◽  
Cd34 Cells ◽  
Macrophage Colony ◽  
Serum Free Suspension

There is evidence that neutrophil production is a balance between the proliferative action of granulocyte–colony-stimulating factor (G-CSF) and a negative feedback from mature neutrophils (the chalone). Two neutrophil serine proteases have been implicated in granulopoietic regulation: pro–proteinase 3 inhibits granulocyte macrophage–colony-forming unit (CFU-GM) growth, and elastase mutations cause cyclic and congenital neutropenia. We further studied the action of the neutrophil serine proteases (proteinase 3, elastase, azurocidin, and cathepsin G) on granulopoiesis in vitro. Elastase inhibited CFU-GM in methylcellulose culture. In serum-free suspension cultures of CD34+ cells, elastase completely abrogated the proliferation induced by G-CSF but not that of GM-CSF or stem cell factor (SCF). The blocking effect of elastase was prevented by inhibition of its enzymatic activity with phenylmethylsulfonyl fluoride (PMSF) or heat treatment. When exposed to enzymatically active elastase, G-CSF, but not GM-CSF or SCF, was rapidly cleaved and rendered inactive. These results support a role for neutrophil elastase in providing negative feedback to granulopoiesis by direct antagonism of G-CSF.

scholarly journals Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA

FEBS Letters ◽  
2000 ◽  
Vol 473 (2) ◽  
pp. 154-156 ◽  
Author(s):  
Jérôme Duranton ◽  
Didier Belorgey ◽  
Jacqueline Carrère ◽  
Lionel Donato ◽  
Thomas Moritz ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Cathepsin G ◽  
Proteinase 3

Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: A role for inflammatory cells in tumor invasion and angiogenesis

2001 ◽  
Vol 189 (2) ◽  
pp. 197-206 ◽  
Author(s):  
Peter Shamamian ◽  
Jess D. Schwartz ◽  
Ben J.Z. Pocock ◽  
Sara Monea ◽  
David Whiting ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Tumor Invasion ◽  
Inflammatory Cells ◽  
Cathepsin G ◽  
Proteinase 3
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