Biochimica et Biophysica Acta (BBA) - Protein Structure
The degradation of human lung elastin by neutrophil proteinases
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2013, Respiratory Physiology and NeurobiologyCitation Excerpt :This elastin-digesting enzyme is present in large quantities in neutrophils. There is evidence that cathepsin G may theoretically hydrolyze a critical position next to a desmosine cross-linking point in the elastin chain (Foster et al., 1976; Reilly and Travis, 1980). The contribution of neutrophil-released elastase to the development of chronic inflammatory lung diseases has been shown in animal and cell culture models (Quinn et al., 2010; Voynow et al., 2008).
The action of neutrophil serine proteases on elastin and its precursor
2012, BiochimieCitation Excerpt :This approach may aid in the development of directed therapies to treat elastin-degrading diseases. Only a few studies have thus far focused on the susceptibility of elastin to proteolysis by different NSPs such as HLE and CG, however, they have not provided any insights into the preferred cleavage sites on elastin or into its molecular-level structure [6,18–24]. Therefore, the aim of the present study was to comprehensively characterize and compare the cleavage behavior, in particular the cleavage site specificities, of HLE, PR3 and CG with two natural substrates, tropoelastin and insoluble elastin, using mass spectrometric (MS) techniques.
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