1.

Intracellular aggregation of human stefin B : confocal and electron microscopy study

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

2.

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 substrates such as transcription factors from its proteolytic processing.

COBISS.SI-ID: 23338023

3.

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. Despite the increased expression of cathepsin L in the nuclei of classically activated macrophages, no cathepsin activity was detected. 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

4.

Activity-based probes as a tool for functonal proteomic analysis of proteases.

Proteases are known for their multilayered post-translational activity regulation that can lead to a significant difference between protease abundance levels and their enzyme activity. In this article, we present structural features of activity-based probes for proteases and discuss their applications in proteomic profiling of various catalytic classes of proteases

COBISS.SI-ID: 22136615

5.

Activity based probes for proteases : applications to biomarker discovery, molecular imaging and drug screening

In this article, we describe the development and applications of activity based probes (ABPs) to study proteases and their role in pathological processes. Specifically we focus on application of this technique for biomarker discovery, in vivo imaging and drug screening

COBISS.SI-ID: 20499751