Letter | Published:

Release of Lysosomal Enzymes by Alveolar Mononuclear Cells

Naturevolume 247pages475477 (1974) | Download Citation



THE finding that individuals severely deficient in the circulating enzyme inhibitor α1-antitrypsin usually contract panlobular emphysema at an early age suggested that proteolytic enzymes were involved in the connective tissue destruction characteristic of pulmonary emphysema1. This idea was strengthened by reports that intratracheal administration of the relatively nonspecific enzyme, papain, or the more specific enzymes, elastase or collagenase, led to the development of emphysema-like lesions in a variety of animal species2,3. The origin of such proteolytic enzymes in vivo, and their mode of release has been the subject of much speculation, and two cell types, the polymorphonuclear (PMN) leukocyte and the alveolar macrophage are implicated. Evidence favouring the PMNs include their sequestration in the basilar portions of the lung in the non-diseased person, their containing large numbers of lysosomes, and the high incidence of concurrent infection (with resultant leukocyte infiltration) associated with non α1-antitrypsin related emphysema. In addition human PMNs release approximately 25% of their lysosomal enzymes during phagocytosis of various particles such as zymosan, latex, and immune complexes4.

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  1. Department of Pharmacology, Pfizer Central Research, Groton, Connecticut, 06340

    •  & JAMES R. BEEBE


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