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. 1980 Dec 1;152(6):1563-70.
doi: 10.1084/jem.152.6.1563.

Limited proteolysis by macrophage elastase inactivates human alpha 1-proteinase inhibitor

M J Banda, E J Clark, Z Werb

Limited proteolysis by macrophage elastase inactivates human alpha 1-proteinase inhibitor

M J Banda et al. J Exp Med. .

Abstract

Inflammatory mouse peritoneal macrophages secrete a metalloproteinase that is not inhibited by alpha 1-proteinase inhibitor. This proteinase, macrophage elastase, recognizes alpha 1-proteinase inhibitor with macrophage elastase does not involve a stable proteinase-inhibitor complex and results in the proteolytic removal of a peptide of apparent molecular weight 4,000-5,000 from the inhibitor. After degradation by macrophage elastase, alpha 1-proteinase inhibitor is no longer able to inhibit human granulocyte elastase, a serine proteinase implicated in the pathogenesis of emphysema. Macrophage elastase apparently does not degrade human granulocyte elastase-alpha 1-proteinase inhibitor complexes or release active granulocyte elastase from these complexes. The ability of macrophage elastase to degrade alpha 1-proteinase inhibitor is inhibited by EDTA and alpha 2-macroglobulin.

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