Premium
In vitro activation of pro‐cathepsin B by three serine proteinases: leucocyte elastase, cathepsin G, and the urokinase‐type plasminogen activator
Author(s) -
Dalet-Fumeron Veronique,
Guinec Nathalie,
Pagano Maurice
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80643-9
Subject(s) - plasmin , urokinase , cathepsin b , plasminogen activator , chemistry , elastase , cathepsin o , cathepsin g , cathepsin , cathepsin l1 , biochemistry , microbiology and biotechnology , in vitro , serine , cathepsin h , enzyme , biology , endocrinology , genetics
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.