Human Myeloblastin (Leukocyte Proteinase 3): Reactions with Substrates, Inactivators and Activators in Comparison with Leukocyte Elastase

Früh, Hans; Kostoulas, Georgios; Michel, Beat A.; Baici, Antonio

doi:10.1515/bchm3.1996.377.9.579

Cited by 11 publications

(14 citation statements)

References 6 publications

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“…The pellet was then dissolved in the buffer (2 mg/ml) and reacted with 290 nM DNase for 90 min at 25°C. After heating for 5 min at 65°C, the mixture was chromatographed on a 12 HR 10/30 Superose column (Amersham Pharmacia Biotech), calibrated with the pBr 322 plasmid previously digested with HaeIII (14). The fractions containing DNA fragments of about 30 base pairs (M r 20,000) were collected and concentrated.…”

Section: Methodsmentioning

confidence: 99%

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DNA Strongly Impairs the Inhibition of Cathepsin G by α1-Antichymotrypsin and α1-Proteinase Inhibitor

Duranton

Boudier

Belorgey

et al. 2000

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

“…3. The inhibition of 30 nM proteinase 3 by concentrations of 30bp DNA up to 1 M was assessed using 2 mM methoxysuccinyl-Lys(2pico)-Ala-Pro-Val-pNA (14). The effect of 30bp DNA on the elastolytic activity of these two proteinases was tested using Remazol Brilliant Blue elastin as described previously (8).…”

Section: Methodsmentioning

confidence: 99%

DNA Strongly Impairs the Inhibition of Cathepsin G by α1-Antichymotrypsin and α1-Proteinase Inhibitor

Duranton

Boudier

Belorgey

et al. 2000

Journal of Biological Chemistry

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“…There is even data from in vitro studies demonstrating that peptide fragments from human elastin that has been degraded using human neutrophil elastase cause chemotaxis of human blood monocytes and calf skin fibroblasts; evidence compatible with this elastase causing the recruitment of cells other than neutrophils and thus perpetuating inflammation at sites of neutrophil accumulation [73,74]. Furthermore, neutrophils also contain another elastolytic enzyme, proteinase-3, which may cause effects similar to those of neutrophil elastase [75][76][77].…”

Section: Neutrophil Elastasementioning

confidence: 99%

Neutrophils, interleukin-17A and lung disease

Lindén¹

2005

Eur Respir J

221

182

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It is now established that an excessive and sustained mobilisation of neutrophils is a hallmark of several chronic inflammatory lung disorders, including severe obstructive lung disease. This article reviews evidence that the cytokine interleukin (IL)-17A is a major orchestrator of sustained neutrophilic mobilisation.Current evidence suggests that IL-17A is produced by T-lymphocytes, and that it exerts an orchestrating effect on the accumulation and associated activity of neutrophils in the bronchoalveolar space indirectly, through an induced release of specific cytokines and colonystimulating factors in resident lung cells.Although the involvement of IL-17A in inflammatory lung disorders is supported by several recent studies, its causative role is still uncertain.However, the unique position of interleukin-17A at the interface between acquired and innate immunity puts this cytokine forward as an important signal for the reinforcement of host defence; it also implies that interleukin-17A may constitute a useful target for pharmacotherapeutic intervention.

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“…PR3 originally was described as a neutral serine proteinase distinct from NE and Cat G found in the azurophilic granules of human neutrophils (17). It was further characterized as being capable of degrading elastin in vitro and of inducing emphysema in hamsters (24,25). Despite its characterization as an elastase-like enzyme, however, the physiological role of PR3 has remained speculative.…”

mentioning

confidence: 99%

Converting enzyme-independent release of tumor necrosis factor α and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3

Coeshott

Ohnemus

Pilyavskaya

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

335

240

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Two important cytokines mediating inf lammation are tumor necrosis factor ␣ (TNF␣) and IL-1␤, both of which require conversion to soluble forms by converting enzymes. The importance of TNF␣-converting enzyme and IL-1␤-converting enzyme in the production of circulating TNF␣ and IL-1␤ in response to systemic challenges has been demonstrated by the use of specific converting enzyme inhibitors. Many inf lammatory responses, however, are not systemic but instead are localized. In these situations release and͞or activation of cytokines may be different from that seen in response to a systemic stimulus, particularly because associations of various cell populations in these foci allows for the exposure of procytokines to the proteolytic enzymes produced by activated neutrophils, neutrophil elastase (NE), proteinase 3 (PR3), and cathepsin G (Cat G). To investigate the possibility of alternative processing of TNF␣ and͞or IL-1␤ by neutrophil-derived proteinases, immunoreactive TNF␣ and IL-1␤ release from lipopolysaccharide-stimulated THP-1 cells was measured in the presence of activated human neutrophils. Under these conditions, TNF␣ and IL-1␤ release was augmented 2-to 5-fold. In the presence of a specific inhibitor of NE and PR3, enhanced release of both cytokines was largely abolished; however, in the presence of a NE and Cat G selective inhibitor, secretory leucocyte proteinase inhibitor, reduction of the enhanced release was minimal. This finding suggested that the augmented release was attributable to PR3 but not NE nor Cat G. Use of purified enzymes confirmed this conclusion. These results indicate that there may be alternative pathways for the production of these two proinf lammatory cytokines, particularly in the context of local inf lammatory processes.

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Human Myeloblastin (Leukocyte Proteinase 3): Reactions with Substrates, Inactivators and Activators in Comparison with Leukocyte Elastase

Cited by 11 publications

References 6 publications

DNA Strongly Impairs the Inhibition of Cathepsin G by α1-Antichymotrypsin and α1-Proteinase Inhibitor

DNA Strongly Impairs the Inhibition of Cathepsin G by α1-Antichymotrypsin and α1-Proteinase Inhibitor

Neutrophils, interleukin-17A and lung disease

Converting enzyme-independent release of tumor necrosis factor α and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3

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