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.
COBISS.SI-ID: 23338023
Increased nucleolar localization of SpiA3G in classically but not alternatively activated macrophages. A serpin A3G (SpiA3G) is highly up regulated in classically activated macrophages. We show increased localization of SpiA3G in the nucleolus and co-localization with cathepsin L, upon classical, but not alternative activation of macrophages. Since only pro-inflammatory, but not anti-inflammatory stimuli induce increased nucleolar localization of SpiA3G, we conclude that SpiA3g translocation into the nucleolus is important in host defense against pathogens.
COBISS.SI-ID: 23524135
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 (the peptide accumulating in AD). 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.
COBISS.SI-ID: 2152783
We have shown that endogenous stefin B formed smaller, occasional cytoplasmic aggregates and inhibition of the proteasome led to an increase in the amount of the endogenous protein within the cells and also increased its aggregation. Stefin B aggregates also co-localized with LC3 and the p62, markers of autophagy. Stefin B -positive cytoplasmic aggregates were partially co-localized with ubiquitin, proteasome subunits S20 and S26 and components of cytoskeleton using confocal microscopy.
COBISS.SI-ID: 23321639
In this paper we have shown which conformation of stefin B is toxic to cells. These are native-like intermediate and molten globule state (similar toxicity within error) and they both are oligomeric. The finding is more general as there is a report that prion protein in the molten globule is also toxic.
COBISS.SI-ID: 21386023