In vitro activation of pro-cathepsin B by three serine proteinases: leucocyte elastase, cathepsin G, and the urokinase-type plasminogen activator

• Published in: FEBS letters Vol. 332; no. 3; pp. 251 - 254
• Main Authors: Dalet-Fumeron, Veronique, Guinec, Nathalie, Pagano, Maurice
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 18.10.1993; Elsevier
• Subjects: Activation; Analytical, structural and metabolic biochemistry; Ascites - enzymology; Biological and medical sciences; Cathepsin B - isolation & purification; Cathepsin B - metabolism; cathepsin B, EC 3.4.22.1; Cathepsin G; cathepsin G, EC 3.4.21.20; Cathepsins - metabolism; DTE, dithioerythritol; EDTA, ethylene diamine tetraacetate, disodium salt; Elastase; elastase, EC 3.4.21.11; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Precursors - metabolism; Enzymes and enzyme inhibitors; Female; Fundamental and applied biological sciences. Psychology; Humans; Hydrolases; Kinetics; Leukocyte Elastase; Molecular Weight; NH-Mec, 4 methyl-7-coumarylamide; Ovarian Neoplasms - enzymology; Pancreatic Elastase - metabolism; PBS, phosphate buffer saline; Pro-cathepsin B; Processing; Serine Endopeptidases - metabolism; Spectrometry, Fluorescence; Urokinase; urokinase, uPA, EC 3.4.21.31; Urokinase-Type Plasminogen Activator - metabolism; Z, benzyloxycarbonyl; EDTA, ethylene diamine tetraacetate, disodium salt; cathepsin G, EC 3.4.21.20; Pro-cathepsin B; Cathepsin G; Activation; urokinase, uPA, EC 3.4.21.31; Processing; Urokinase; PBS, phosphate buffer saline; cathepsin B, EC 3.4.22.1; elastase, EC 3.4.21.11; DTE, dithioerythritol; Z, benzyloxycarbonyl; Elastase; NH-Mec, 4 methyl-7-coumarylamide; Serine endopeptidases; Enzyme; Gel electrophoresis; Cysteine endopeptidases; Cell cell interaction; Malignant tumor; Fluorescence spectrometry; Enzymatic activity; Cathepsin B; Immunoblotting assay; Hydrolases; Proteinases
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)80643-9

In vitro activation of pro-cathepsin B purified from ascitic fluid of ovarian carcinomas by serine proteinases was studied. Both elastase and cathepsin G from human leucocytes were found to be activators, on the basis of generation of cathepsin B activity and processing of the precursor. These results represent a new cooperative pathway between cancer cells and host cells. The urokinase-type plasminogen activator activated pro-cathepsin B faster than leucocyte proteinases. A new relationship is emerging between the cysteine proteinases and the plasmin-activation system. Both pathways suggest an important role of cathepsin B in the proteolytic cascade associated with tumour invasion.