In this work, we investigated the cell death termed apoptosis, in two tumor-cell lines, U937 and T98G, thus induced by the tumor necrosis factor (TNF)-alpha. The cell death involved lysosomal destabilization and the release of cathepsins into the cytosol. However, the blockage of cysteine cathepsins with a broad-spectrum inhibitor, E64d, or a more specific cathepsin B inhibitor, CA-074Me, had no effect on the progression of apoptosis in neither cell line, thus suggesting that TNF-alpha apoptosis is not critically dependent on cysteine cathepsins in these cellular models.
COBISS.SI-ID: 22717479
We investigated the mechanism of protein oligomerization using a yellow fluorescent protein (YFP) and GST fusion proteins containing more than 20 alanine repeats. These fusion proteins having 23 polyalanine residues sedimented in sucrose density gradients, suggesting instability and confirming protein oligomerization. Afterwards, the GST fusion proteins were resistant to trypsin digestion. In conclusion, the oligomerized artificial proteins containing long polyalanine repeats may represent a suitable model to study polyalanine-related diseases, among other neurodegenerative disorders.
COBISS.SI-ID: 22527783