1.

Selective and sensitive monitoring of caspase-1 activity by a novel bioluminescent activity-based probe.

A new extremely selective bioluminescent caspase-1 activity-based probe was generated. The probe enablse sensitive detection of caspase-1 activity in cell lysates, but not in intact cells, as it is not cell permeable. This probe has substantialy improved properties as compared to all other known caspase-1 fluorescent substrates or probes, based on such substrates.

COBISS.SI-ID: 23985703

2.

Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells.

By using techniques SPR and ESI MS we were able to show that the tetramers of stefin B and domain-swapped dimers of stefin B (Y31 variant) interact with amyloid-beta. That interaction is specific to stefin B oligomers as compared to monomers is a new finding. Further, we have shown that oligomers of stefin B inhibit growth of amyloid fibrils by A-beta in vitro and co-localise with A-beta in vivo. Any such interaction and inhibition of A-beta fibril growth is of interest for eventual trials to obtain the therapy for AD, which brings huge economical burden to Western societies.

COBISS.SI-ID: 2152783

3.

Stefin B interacts with histones and cathepsin L in the nucleus.

We have identified an interaction between stefin B and the histones. Increased expression of stefin B in the nucleus influenced processing of CUX1 transcription factor, and as a consequence of diminished cleavage of CUX1, delayed cell cycle progression was determined. Interaction of stefin B with the truncated form of cathepsin L in the nucleus was confirmed by FRET experiments in the living cells. Stefin B could play an important role in regulating the proteolytic activity of cathepsin L in the nucleus, protecting nuclear substrates from proteolytic processing.

COBISS.SI-ID: 23338023

4.

Binding of amyloid peptides to domain-swapped dimers as opposed to monomers.

We performed additional studies of amyloid-beta binding to cystatins dimers as opposed to monomers and derive some more general conclusions about a possible chaperone-like activity of domain-swapped oligomers.

COBISS.SI-ID: 23983911

5.

Lysosomal-mitochondrial cross-talk during cell death.

In this review article we have critically evaluated current research in the field of cell death and the role of lysosomes in this process with the major empahsis on the cross-talk between lysosomes and mitochondria.

COBISS.SI-ID: 24130087