Characterization of a chemotactic and cytotoxic proteinase from human skin

Victor B. Hatcher, Gerald S. Lazarus, Norman Levine, Peter G. Burk, Fred J. Yost Jr.

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


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 α2-macroglobulin, α1-antitrypsin, C 1 ̄ inactivator, soybean trypsin inhibitor and diiosopropyl fluorophosphate. Injection 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 μg/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.

Original languageEnglish (US)
Pages (from-to)160-171
Number of pages12
JournalBBA - Enzymology
Issue number1
StatePublished - Jul 8 1977

ASJC Scopus subject areas

  • Medicine(all)


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