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


  • eng

Conference Location

  • Netherlands