Abstract
Chronic Obstructive Pulmonary Disease (COPD), comprised of chronic bronchitis and pulmonary emphysema, is a serious health problem in the world. In the USA, COPD caused more than 70,000 deaths in 1986 and more than 10,000,000 Americans suffered from the disease.1 The association between severe α1protease inhibitor (α1PI) deficiency and emphysema has led to the hypothesis that an elastase-antielastase imbalance causes emphysema.2,3 Human neutrophil elastase (HNE) is most likely the cause of emphysema in both smokers and non-smokers, although the evidence supporting the elastase-antielastase hypothesis is largely indirect in smokers with normal protective levels of α1PI. Homogenates of leucocytes as well as highly purified preparations of HNE produce emphysema in experimental animals and only elastolytic enzymes will induce experimental emphysema. In addition, neutrophils are increased 4–5 fold in the lungs of smokers and it is postulated that α1PI is inactivated by powerful oxidizing agents in the cigarette smoke and PMNs contributing to the elastase-antielastase imbalance. Other proteases including human proteinase 3 and macrophage elastase may also play a role in lung destruction in emphysema. Nevertheless, the majority of investigators in the field believe that a human neutrophil elastase-antielastase imbalance plays the major role in the pathogenesis of emphysema.
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Powers, J.C., Kam, CM., Hori, H., Oleksyszyn, J., Meyer, E.F. (1992). Synthetic Mechanism-Based and Transition-State Inhibitors for Human Neutrophil Elastase. In: Grassi, C., Travis, J., Casali, L., Luisetti, M. (eds) Biochemistry of Pulmonary Emphysema. Current Topics in Rehabilitation. Springer, London. https://doi.org/10.1007/978-1-4471-3771-9_10
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DOI: https://doi.org/10.1007/978-1-4471-3771-9_10
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