title: Proteolytic enzymes and plasminogen activator in melanoma.
abstract: 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.
mesh_terms: 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*
chemical_list: D010447:Peptide Hydrolases; D010960:Plasminogen Activators