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

Norman Levine, Victor B. Hatcher, Gerald Sylvan Lazarus

Research output: Contribution to journalArticle

Abstract

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 KCl 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.

Original languageEnglish (US)
Pages (from-to)458-467
Number of pages10
JournalBBA - Enzymology
Volume452
Issue number2
DOIs
StatePublished - Dec 8 1976
Externally publishedYes

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Leukocyte Chemotaxis
fluorophosphate
Epidermis
Neutrophils
Peptide Hydrolases
Molecular Weight
Enzymes
Cathepsin D
Octoxynol
Serine Proteases
Sodium Dodecyl Sulfate
Chromatography
Polyacrylamide Gel Electrophoresis
Edema
Rabbits
Skin
Injections

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis. / Levine, Norman; Hatcher, Victor B.; Lazarus, Gerald Sylvan.

In: BBA - Enzymology, Vol. 452, No. 2, 08.12.1976, p. 458-467.

Research output: Contribution to journalArticle

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