Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis.

Journal Article (Journal Article)

Three neutral proteinases (EC 3.4.--.--) and cathepsin D have been identified in human epidermis utilizing a highly sensitive radioactive method. The proteinases were extracted in 1.0 M KC1 and 0.1% Triton X-100 and separated by Sephadex G-75 chromatography. The neutral proteinase peaks were all inhibited by diisopropyl fluorophosphate and thus were serine proteinases. Incubation of the enzyme fractions with [3H] diisopropyl fluorophosphate followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that the two larger molecular weight proteinases were enzyme mixtures. The small molecular weight [3H] diisopropyl fluorophosphate proteinase migrated as a single band. Injection of the small molecular weight neutral proteinase into rabbit skin produced a polymorphonuclear leukocyte infiltration and edema. The reaction was not observed with the diisopropyl fluorophosphate-inhibited enzyme fraction. The release of neutral proteinases may be one of the signal events in the epidermal inflammatory response.

Full Text

Duke Authors

Cited Authors

  • Levine, N; Hatcher, VB; Lazarus, GS

Published Date

  • December 8, 1976

Published In

Volume / Issue

  • 452 / 2

Start / End Page

  • 458 - 467

PubMed ID

  • 1009122

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/0005-2744(76)90196-0


  • eng

Conference Location

  • Netherlands