In vitro activation of pro-cathepsin B by three serine proteinases: leucocyte elastase, cathepsin G, and the urokinase-type plasminogen activator.
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.
Dalet-Fumeron
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V
Laboratoire de biochimie, équipe associée à l'Ura 1460 CNRS, Faculté de Médecine Broussais Hotel-Dieu, Université Pierre et Marie Curie, Paris, France.
Guinec
N
N
Pagano
M
M
D001201:Ascites / Q000201:enzymology; D002401:Cathepsin B / Q000302:isolation & purification / Q000378:metabolism*; D056649:Cathepsin G; D002403:Cathepsins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D019272:Leukocyte Elastase; D008970:Molecular Weight; D010051:Ovarian Neoplasms / Q000201:enzymology; D010196:Pancreatic Elastase / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D004792:Enzyme Precursors; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase; D014568:Urokinase-Type Plasminogen Activator; C057832:procathepsin B; D002401:Cathepsin B