Thi paper is dedicated to Nobel laureate Christian de Duve (who visited our laboratory 1978, three years after the discovery of the lysosome). In this discovery, the important role played also aspartic protease cathepsin D. This discovery was crucial for the enormous progress in the field of proteolysis and various proteases including cysteine cathepsins, cathepsin E and others. In this paper, is indicated the role of aspartic protease cathepsin D at the process of cystatins degradation, thus regulating the activity of cysteine cathepsins.
COBISS.SI-ID: 25347623
Cathepsin E splice variant 2 appears in a number of gastric carcinoma. Here, we report detecting this variant in HeLa cells using polyclonal antibodies and biotinylated inhibitor pepstatin A. Overexpression of GFP fusion proteins of cathepsin E and its splice variant within HEK-293T cells showed that both proteins are colocalized. Both proteins were expressed with and without the propeptide in E.coli. After refolding it was found that full-length cathepsin E variant1 is activated at acid pH, while the splice variant remains inactive. A comparative structure model of splice variant 2 was computed based on its alignment to the known structure of cathepsin E intermediate (Protein Data Bank code 1TZS), and used to rationalize its conformational properties and loss of activity.
COBISS.SI-ID: 25585959