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PMID: 7952653 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Elastolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease.

American journal of respiratory and critical care medicine ·Vol. 150 ·No. 6 Pt 2 ·1994-12-00 ·Pages S160-4

Shapiro SD

Abstract

Mononuclear phagocytes have the capacity to produce an array of MMPs. Several of these proteinases are capable of degrading insoluble elastin, an important component for the structural stability of the lung. Matrilysin is a low molecular weight proteinase with a broad substrate specificity produced at highest levels in in vitro differentiated monocytes. The 92-kD gelatinase is a major product of human alveolar macrophages that is also an elastase. The most newly described member of the MMP family is human macrophage metalloelastase. This enzyme is also expressed in alveolar macrophages derived from cigarette smokers. Determining the contribution of these and other elastolytic proteinases to the pathogenesis of emphysema is a focus of ongoing research.

MeSH Terms
Animals Elastin/metabolism Extracellular Matrix/enzymology Humans Lung Diseases/enzymology Macrophages, Alveolar/enzymology Matrix Metalloproteinase 7 Metalloendopeptidases/physiology Monocytes/enzymology Pancreatic Elastase/metabolism
Chemicals
Elastin Pancreatic Elastase Metalloendopeptidases Matrix Metalloproteinase 7
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Shapiro S D
Department of Medicine, Washington University Medical Center at Jewish Hospital, St. Louis, Missouri 63110.
Article Info
Journal
American journal of respiratory and critical care medicine
Abbr.
Am J Respir Crit Care Med
ISSN
1073-449X
Published
1994-12-00
Pages
S160-4
Language
English
Region
United States
NLM ID
9421642
Subset
IM
Grants
PHS HHS · AL29594 · United States
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