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

FEBS Letters

Guinec, Nathalie¹  Dalet-Fumeron, Veronique¹  Pagano, Maurice¹ 

[1] Laboratoire de biochimie, équipe associée à l'Ura 1460 CNRS, Faculté de Médecine Broussais Hotel-Dieu, Université Pierre et Marie Curie, 15 rue de l'école de médecine, 75270 Paris cedex 06, France

关键词: Pro-cathepsin B;    Activation;    Processing;    Elastase;    Cathepsin G;    Urokinase;    cathepsin B;    EC 3.4.22.1;    elastase;    EC 3.4.21.11;    cathepsin G;    EC 3.4.21.20;    urokinase;    uPA;    EC 3.4.21.31;    Z;    benzyloxycarbonyl;    NH-Mec;    4 methyl-7-coumarylamide;    EDTA;    ethylene diamine tetraacetate;    disodium salt;    DTE;    dithioerythritol;    PBS;    phosphate buffer saline;   

DOI  :  10.1016/0014-5793(93)80643-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown