Abstract
PROTEOLYSIS and its biological control in the pathogenesis of disease states involving inflammation and tissue injury have become areas of intensive study1,2. Because of their probable involvement in the pathogenesis of emphysema, the elastolytic enzymes derived from neutrophils have received particular attention3–6. Among the principal protease inhibitors in blood, α1 antitrypsin (α1-AT) serves as the main inhibitor controlling the activity of elastase and other serine proteinases, whereas α2-macroglobulin (α2-M) is believed to function primarily as a means of removing elastase and other proteinases from the circulatory system via the reticuloendothelial system7,8. During studies of the interaction of various inhibitors with elastase isolated from purulent sputum9, it was noted that the activity of this enzyme towards certain synthetic substrates was markedly enhanced in the presence of α2-M. We present here a study of this activation. It is possible that activation of elastase by α2-M may be of physiological significance, particularly under those conditions where a deficiency of antitrypsin is known to be a predisposing factor towards chronic obstructive pulmonary disease10.
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TWUMASI, D., LIENER, I., GALDSTON, M. et al. Activation of human leukocyte elastase by human α2-macroglobulin. Nature 267, 61–63 (1977). https://doi.org/10.1038/267061a0
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DOI: https://doi.org/10.1038/267061a0
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