Proteolytic enzymes and plasminogen activator in melanoma.
Proteolytic activities were measured in extracts of human skin melanoma, lymphatic metastasis and in nonmalignant naevi by using various proteinase substrates as well as plasminogen activator assay. pH-optima for hydrolysis of various proteinase substrates by these tumors were found to be essentially the same as in healthy human skin. Melanoma extracts were found to especially readily hydrolyze N-alpha-benzoyl-DL-arginine beta-naphthylamine (BANA) at pH 5.8 in the presence of 1 mmol/l dithiothreitol and EDTA (cathepsin B1-like enzyme) as well as histones and p-tosyl-L-arginine methyl ester (TAME) at pH 7.5, and showed increased capacity to activate plasminogen when compared to nonmalignant naevus. The possible role of proteinases in malignant melanoma is discussed.
D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008207:Lymphatic Metastasis; D008545:Melanoma / Q000201:enzymology*; D009506:Nevus / Q000201:enzymology; D010447:Peptide Hydrolases / Q000378:metabolism*; D010960:Plasminogen Activators / Q000378:metabolism*; D012878:Skin Neoplasms / Q000201:enzymology*
D010447:Peptide Hydrolases; D010960:Plasminogen Activators