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 HEK293T 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 fulllength 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
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
COBISS.SI-ID: 25347623
Endosomal/lysosomal system has numerous biological functions. In addition to cysteine cathepsins participate in apoptosis cathepsins D and E, as well.
COBISS.SI-ID: 22640935
Control of protease activity play a crucial role in a variety of physiological processes. Imbalances in their activities is critical in a number of pathologies. Recent studies showed, that the development of the modern technologies, such as proteomics contributed to the discovery of proteases as signalling molecules and not only as enzymes responsible for protein degradation. Among other proteases, play important role in these processes lysosomal cathepsin D and most probably cathepsin E.
COBISS.SI-ID: 25737767
In this work we present a detailed analysis of the dual role of lysosomes and lysosomal cathepsins in the two main pathways of cell death, namely, apoptosis and autophagy. Destabilization of the lysosomal membranes by lysosomotropic detergents seems to be a promising strategy as it would not only disable autophagy, but also promote apoptosis through the initiation of the lysosomal pathway. On the other side, the impaired autophagy and lysosomal degradation linked with the increased oxidative stress underlie degenerative changes in the aging neurons. Lizosomi ter lizosomalni katepsini pri celični smrti.
COBISS.SI-ID: 25347879