Characterization of a chemotactic and cytotoxic proteinase from human skin.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Hatcher, VB; Lazarus, GS; Levine, N; Burk, PG; Yost, FJ
Published Date
- July 8, 1977
Published In
Volume / Issue
- 483 / 1
Start / End Page
- 160 - 171
PubMed ID
- 69444
International Standard Serial Number (ISSN)
- 0006-3002
Digital Object Identifier (DOI)
- 10.1016/0005-2744(77)90018-3
Language
- eng
Conference Location
- Netherlands