Characterization of a chemotactic and cytotoxic proteinase from human skin.
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 alpha 2-macroglobulin, alpha 1-antitrypsin, C-1 inactivatory, soybean trypsin inhibitor and diisopropyl fluorophosphate. 2njection 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 microgram/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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007249:Inflammation / Q000139:chemically induced; D007531:Isoflurophate / Q000494:pharmacology; D007930:Leucine / Q000378:metabolism; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors; D014176:Protein Biosynthesis; D011817:Rabbits; D012867:Skin / Q000201:enzymology* / Q000473:pathology; D014361:Trypsin Inhibitors / Q000494:pharmacology; D000511:alpha-Macroglobulins / Q000494:pharmacology
D000596:Amino Acids; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D000511:alpha-Macroglobulins; D007531:Isoflurophate; D010447:Peptide Hydrolases; D007930:Leucine