Enhanced oligomerization of full-length RAGE by synergy of the interaction of its domains.

The pattern recognition receptor RAGE (receptor for advanced glycation end-products) transmits proinflammatory signals in several inflammation-related pathological states, including vascular diseases, cancer, neurodegeneration and diabetes. Its oligomerization is believed to be important in signal transduction, but RAGE oligomeric structures and stoichiometries remain unclear. Different oligomerization modes have been proposed in studies involving different truncated versions of the extracellular parts of RAGE. Here, we provide basic characterization of the oligomerization patterns of full-length RAGE (including the transmembrane (TM) and cytosolic regions) and compare the results with oligomerization modes of its four truncated fragments. For this purpose, we used native mass spectrometry, analytical ultracentrifugation, and size-exclusion chromatography coupled with multi-angle light scattering. Our results confirm known oligomerization tendencies of separate domains and highlight the enhanced oligomerization properties of full-length RAGE. Mutational analyses within the GxxxG motif of the TM region show sensitivity of oligomeric distributions to the TM sequence. Using hydrogen-deuterium exchange, we mapped regions involved in TM-dependent RAGE oligomerization. Our data provide experimental evidence for the major role of the C2 and TM domains in oligomerization, underscoring synergy among different oligomerization contact regions along the RAGE sequence. These results also explain the variability of obtained oligomerization modes in RAGE fragments

Influence of modified porous aggregates on the efficiency of treatment by trickling filter systems

Złoża biologiczne stają się obecnie coraz bardzie popularne jako małe oczyszczalnie. Wzrost ich popularności jest spowodowany stosowaniem materiałów o dużej powierzchni, ale jednocześnie lekkich. W badaniach porównano pracę dwóch modelowych zanurzonych złóż biologicznych z kruszywem ceramicznym oraz kruszywem ceramicznym modyfikowanym. Efektywność procesu określona na podstawie szybkości powstawania biofilmu, ilości biomasy oraz jakości oczyszczonych ścieków (ChZT, BZT5, OWO, związki biogenne). Badania wykazały większą przydatność złoża modyfikowanego do hodowli błony biologicznej, a tym samym do oczyszczania ścieków.Biological beds are now becoming more and more popular as small wastewater treatment plant. Increase their popularity is due to the use of materials with large surface and light. In the study compares the work of two model biological beds with using ceramic aggregates and modified ceramic aggregates. The efficiency of the biodegradation process determined on the basis of the biofilm formation, biomass growth and quality of treated wastewater (COD, BOD5, TOC, biogenic compounds). Research showed that modified porous aggregates are more suitable for the growth of biofilm and thus to wastewater treatment

Targeted Quantitative Screening of Chromosome 18 Encoded Proteome in Plasma Samples of Astronaut Candidates

This work was aimed at estimating the concentrations of proteins encoded by human chromosome 18 (Chr 18) in plasma samples of 54 healthy male volunteers (aged 20–47). These young persons have been certified by the medical evaluation board as healthy subjects ready for space flight training. Over 260 stable isotope-labeled peptide standards (SIS) were synthesized to perform the measurements of proteins encoded by Chr 18. Selected reaction monitoring (SRM) with SIS allowed an estimate of the levels of 84 of 276 proteins encoded by Chr 18. These proteins were quantified in whole and depleted plasma samples. Concentration of the proteins detected varied from 10^–6 M (transthyretin, P02766) to 10^–11 M (P4-ATPase, O43861). A minor part of the proteins (mostly representing intracellular proteins) was characterized by extremely high inter individual variations. The results provide a background for studies of a potential biomarker in plasma among proteins encoded by Chr 18. The SRM raw data are available in ProteomeXchange repository (PXD004374)