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- W1997201199 abstract "Pulmonary emphysema and periodontal disease are each characterized by the uncontrolled proteolysis of connective tissue proteins by proteinases derived from human neutrophils. Although these diseases would not appear to be related in terms of the initial insult to individual tissues, the ultimate result in each disease is the accumulation and degranulation of neutrophils at inflammatory sites, apparently as a result of frustrated phagocytosis and specific activation of these phagocytic cells. This result is easily recognized in the case of emphysema, where there is clear evidence that the primary cause of the disease is the accumulation of foreign materials in the lung (e.g., smoke condensate), followed by the recruitment of neutrophils to the organ and the release of oxidative and hydrolytic enzymes. In periodontitis, however, the problem begins with the accumulation of plaque at the base of the teeth, followed by the growth of opportunistic anaerobic bacteria below the gum line. These parasitic microbes, which are resistant to killing by both monocytes and granulocytes, secrete proteinases that can activate the kallikrein-kinin pathway, degrade clotting factors, and release the potent neutrophil chemotactic factor, C5a, from complement. It is under such conditions that neutrophils are recruited to infected sites within the periodontium. After the neutrophil-recruitment stage, the two diseases become similar in that degranulation of neutrophils occurs during attempted phagocytosis of either cigarette smoke components (emphysema) or bacteria (periodontitis), followed by inactivation of tissue proteinase inhibitors and degradation of connective tissue proteins, the ultimate result being the destruction of the alveolus or gingiva, respectively." @default.
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- W1997201199 date "1994-12-01" @default.
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- W1997201199 title "The Role of Proteolytic Enzymes in the Development of Pulmonary Emphysema and Periodontal Disease" @default.
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- W1997201199 doi "https://doi.org/10.1164/ajrccm/150.6_pt_2.s143" @default.
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