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PMID: 2454577 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Structure, function, and control of neutrophil proteinases.

The American journal of medicine ·Vol. 84 ·No. 6A ·1988-06-24 ·Pages 37-42

Travis J

Abstract

Elastase and cathepsin G are two of the major enzymes present in and secreted by human neutrophils. These proteinases can rapidly degrade connective tissue proteins. However, they also may be involved in other processes, including the activation or inactivation of protein hormones and the inactivation of plasma proteinase inhibitors. Neutrophil elastase has been implicated in the development of pulmonary emphysema, although a function for cathepsin G has not yet been elucidated. Both enzymes are normally tightly controlled by plasma proteinase inhibitors. However, this proteinase-proteinase inhibitor balance can be perturbed in favor of free enzyme by several methods, with resulting tissue damage. The use of inhibitors from several sources should be helpful in augmenting natural levels so that homeostasis can be maintained.

MeSH Terms
Blood Proteins/deficiency,physiology Cathepsin G Cathepsins/antagonists & inhibitors,blood,physiology Chymotrypsin/antagonists & inhibitors Humans Neutrophils/enzymology Pancreatic Elastase/antagonists & inhibitors,blood,physiology Pulmonary Emphysema/enzymology Serine Endopeptidases alpha 1-Antitrypsin alpha-Macroglobulins/physiology
Chemicals
Blood Proteins alpha 1-Antitrypsin alpha-Macroglobulins Cathepsins Serine Endopeptidases Chymotrypsin CTSG protein, human Cathepsin G Pancreatic Elastase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Travis J
Department of Biochemistry, University of Georgia, Athens 30602.
Article Info
Journal
The American journal of medicine
Abbr.
Am J Med
ISSN
0002-9343
Published
1988-06-24
Pages
37-42
Language
English
Region
United States
NLM ID
0267200
Subset
IM
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