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 (/sup 3/H)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 (/sup 3/H)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 diisopropul fluorophosphate-inhibited enzyme fraction. The release of neutral proteinases may be one of the signal events in the epidermal inflammatory response.
Levine, N;
Hatcher, V B;
Lazarus, G S;
[1]
Montefiore Hospital, New York (USA);
Duke Univ., Durham, N.C. (USA))
- Albert Einstein Coll. of Medicine, Bronx, N.Y. (USA)
Citation Formats
Levine, N, Hatcher, V B, Lazarus, G S, Montefiore Hospital, New York (USA), and Duke Univ., Durham, N.C. (USA)).
Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis.
Netherlands: N. p.,
1976.
Web.
Levine, N, Hatcher, V B, Lazarus, G S, Montefiore Hospital, New York (USA), & Duke Univ., Durham, N.C. (USA)).
Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis.
Netherlands.
Levine, N, Hatcher, V B, Lazarus, G S, Montefiore Hospital, New York (USA), and Duke Univ., Durham, N.C. (USA)).
1976.
"Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis."
Netherlands.
@misc{etde_7314581,
title = {Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis}
author = {Levine, N, Hatcher, V B, Lazarus, G S, Montefiore Hospital, New York (USA), and Duke Univ., Durham, N.C. (USA))}
abstractNote = {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 (/sup 3/H)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 (/sup 3/H)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 diisopropul fluorophosphate-inhibited enzyme fraction. The release of neutral proteinases may be one of the signal events in the epidermal inflammatory response.}
journal = []
volume = {452:2}
journal type = {AC}
place = {Netherlands}
year = {1976}
month = {Dec}
}
title = {Proteinases of human epidermis; a possible mechanism for polymorphonuclear leukocyte chemotaxis}
author = {Levine, N, Hatcher, V B, Lazarus, G S, Montefiore Hospital, New York (USA), and Duke Univ., Durham, N.C. (USA))}
abstractNote = {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 (/sup 3/H)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 (/sup 3/H)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 diisopropul fluorophosphate-inhibited enzyme fraction. The release of neutral proteinases may be one of the signal events in the epidermal inflammatory response.}
journal = []
volume = {452:2}
journal type = {AC}
place = {Netherlands}
year = {1976}
month = {Dec}
}