Degradation of collagen by a human granulocyte collagenolytic system.
This report suggests a mechanism for collagen degradation mediated by human granulocytic leukocytes. A specific collagenase, which is extractable from human granulocytes, has been partially purified by DEAE chromatography. This collagenolytic enzyme is operative at physiological pH and is inhibited by EDTA, cysteine, and reduced glutathione but not by human serum. The enzyme cleaves the collagen molecule into two specific products, without loss of helical conformation. Electron micrographs of segment long spacing aggregates indicate that the cleavage occurs one-quarter of the length from the carboxy terminal end of the molecule. Experiments with crude extracts from granulocytes suggest that the specific products of granulocyte collagenase activity are then degraded by other proteases present in the human granulocyte.
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- Microscopy, Electron
- Microbial Collagenase
- Leukocytes
- Immunology
- Hydrogen-Ion Concentration
- Humans
- Hot Temperature
- Glutathione
- Electrophoresis
- Edetic Acid
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Microscopy, Electron
- Microbial Collagenase
- Leukocytes
- Immunology
- Hydrogen-Ion Concentration
- Humans
- Hot Temperature
- Glutathione
- Electrophoresis
- Edetic Acid