@article{f870db3f761f4f2e8f47df6fbecd27af,
title = "Characterization of a chemotactic and cytotoxic proteinase from human skin",
abstract = "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.",
author = "Hatcher, {Victor B.} and Lazarus, {Gerald S.} and Norman Levine and Burk, {Peter G.} and {J. Yost Jr.}, Fred",
note = "Funding Information: Dr. Charlotte Thomas participated actively in the latter stages of this project. The authors wish to acknowledge Dr. Peter Harpel, Department of Medicine, Division of Hematology, New York Hospital, Cornell Medical Center, New York, N.Y. for the preparations of a2-macroglobulin, a~-antitrypsin and C1-inactivator. Dr. James Powers, Georgia Institute of Technology, Atlanta, Ga. who provided the alanine ester inhibitors; Dr. Allen Barrett of the Strangeways Research Laboratories, Cambridge, England who provided the pepstatin; and Dr. Olga Blumenfeld performed the amino acid analysis. Ms. Deborah Cleary and Ms. Alyce Miller provided expert technical assistance. G.S.L. is a Senior Investigator of the Arthritis Foundation. This work was supported by a grant from the National Institute of Arthritis, Metabolic and Digestive Diseases (7 R01 AM17370-01) and the National Institute of Heart and Lung (HL 16387).",
year = "1977",
month = jul,
day = "8",
doi = "10.1016/0005-2744(77)90018-3",
language = "English (US)",
volume = "483",
pages = "160--171",
journal = "BBA - Enzymology",
issn = "0005-2744",
publisher = "Elsevier BV",
number = "1",
}