Characterization of a chemotactic and cytotoxic proteinase from human skin.
A proteinase (EC 3.4.-.-) active at physiological pH has been isolated from human skin utilizing gel filtration and affinity chromatography techniques. The proteinase has a molecular weight of approx. 28 000 and it is inhibited by alpha 2-macroglobulin, alpha 1-antitrypsin, C-1 inactivatory, soybean trypsin inhibitor and diisopropyl fluorophosphate. 2njection of 1 ng of purified proteinase into rabbit skin induces polymorphonuclear leukocyte infiltration of the cutis. Inhibition of enzyme activity with diisopropyl fluorophosphate inhibits the chemotactic effect. Addition of 0.2 microgram/ml of purified proteinase to fibroblast cultures kills the cells within minutes. This proteinase may play a significant role in modulating the inflammatory response after cellular injury.
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- alpha-Macroglobulins
- Trypsin Inhibitors
- Skin
- Rabbits
- Protein Biosynthesis
- Protease Inhibitors
- Peptide Hydrolases
- Molecular Weight
- Leucine
- Isoflurophate
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- alpha-Macroglobulins
- Trypsin Inhibitors
- Skin
- Rabbits
- Protein Biosynthesis
- Protease Inhibitors
- Peptide Hydrolases
- Molecular Weight
- Leucine
- Isoflurophate