Model of material and financial flows in the forest industry cluster of the Tomsk region

The main objective of the paper is the modeling of the timber industry complex in the Tomsk region from circular economy and sustainable development point of view. On the basis of the value chain process and the formation of threats along the whole chain nature (forest) - economy - society (consumer) the modeling of products and waste creation has been developed. The large amount of unused waste requires the development of a special regional forestry cluster model using circular economy approach in order to propose best solutions for recycling

Subzelluläre Lokalisation des Y-box-Proteins-1 (YB-1) in Mesangialzellen und Charakterisierung der dafür verantwortlichen Proteindomänen

As a DNA- and RNA binding protein the cold-shock protein YB-1 serves multiple functions in the nucleus and cytoplasm, e.g. regulating transcription, RNA-processing, -translation and –storage. In the present study we examined the expression and localisation pattern of YB-1 in various models of glomerular diseases. Furthermore we determined protein regions involved in the regulation of YB-1 localisation. In glomeruli of healthy rat kidneys YB-1 is detected exclusively in the nucleus by means of immunohistochemistry with two different antibodies against YB-1. In the course of the Ant-Thy 1.1- nephritis YB-1 changes its localisation and expression pattern. Within one day YB-1 localizes to the perinuclear region of cells within all glomeruli . In the course of the disease the strongest cytoplasmic YB-1 signal coincided with the peak mesangial cell activation/proliferation between days 4 and 6 and was detected in a mesangial distribution pattern. With resolution of the disease at day 31 with complete morphological restitution was associated with YB-1 relocalisation to the nucleus. In the course of different other models of rat glomerular disease YB-1 remained nuclear. In the second part of the study we examined YB-1 localisation in the in vitro model of proliferating rat mesangial cells, which are activated in cell culture conditions. In these cells endogenous YB-1 as well as transfected GFP-YB-1-proteins was detected in the cytoplasm. Using cell cycle inhibitors we tried to arrest the rat mesangial cells. Only after treatment with roscovitine, a specific CDK- inhibitor, YB-1 translocated into the nucleus. Cloning various deletion construct of YB-1 with a fluorescent tag we identified three nuclear localisation signals (NLS: AS 185-194, AS 149-156, AS 276-292) and two cytoplasmic localisation signals or nuclear export signals ( ZLS: AS 1-57, AS 52-146). Experiments using leptomycin B as an inhibitor of the CRM1 dependent nuclear export could reveal a CRM-1 independent export of YB-1. In summary these results document an increased expression and translocation of YB-1 in mesangial cells in the course of glomerulonephritis, therefore YB-1 has pivotal role coordinating inflammatory processes in glomerular disease

Subzelluläre Lokalisation des Y-box-Proteins-1 (YB-1) in Mesangialzellen und Charakterisierung der dafür verantwortlichen Proteindomänen

As a DNA- and RNA binding protein the cold-shock protein YB-1 serves multiple functions in the nucleus and cytoplasm, e.g. regulating transcription, RNA-processing, -translation and –storage. In the present study we examined the expression and localisation pattern of YB-1 in various models of glomerular diseases. Furthermore we determined protein regions involved in the regulation of YB-1 localisation. In glomeruli of healthy rat kidneys YB-1 is detected exclusively in the nucleus by means of immunohistochemistry with two different antibodies against YB-1. In the course of the Ant-Thy 1.1- nephritis YB-1 changes its localisation and expression pattern. Within one day YB-1 localizes to the perinuclear region of cells within all glomeruli . In the course of the disease the strongest cytoplasmic YB-1 signal coincided with the peak mesangial cell activation/proliferation between days 4 and 6 and was detected in a mesangial distribution pattern. With resolution of the disease at day 31 with complete morphological restitution was associated with YB-1 relocalisation to the nucleus. In the course of different other models of rat glomerular disease YB-1 remained nuclear. In the second part of the study we examined YB-1 localisation in the in vitro model of proliferating rat mesangial cells, which are activated in cell culture conditions. In these cells endogenous YB-1 as well as transfected GFP-YB-1-proteins was detected in the cytoplasm. Using cell cycle inhibitors we tried to arrest the rat mesangial cells. Only after treatment with roscovitine, a specific CDK- inhibitor, YB-1 translocated into the nucleus. Cloning various deletion construct of YB-1 with a fluorescent tag we identified three nuclear localisation signals (NLS: AS 185-194, AS 149-156, AS 276-292) and two cytoplasmic localisation signals or nuclear export signals ( ZLS: AS 1-57, AS 52-146). Experiments using leptomycin B as an inhibitor of the CRM1 dependent nuclear export could reveal a CRM-1 independent export of YB-1. In summary these results document an increased expression and translocation of YB-1 in mesangial cells in the course of glomerulonephritis, therefore YB-1 has pivotal role coordinating inflammatory processes in glomerular disease

Cold shock Y-box protein-1 proteolysis autoregulates its transcriptional activities

Background: The Y-box protein-1 (YB-1) fulfills pleiotropic functions relating to gene transcription, mRNA processing, and translation. It remains elusive how YB-1 shuttling into the nuclear and cytoplasmic compartments is regulated and whether limited proteolysis by the 20S proteasome releases fragments with distinct function(s) and subcellular distribution(s). Results: To address these questions, mapping of domains responsible for subcellular targeting was performed. Three nuclear localization signals (NLS) were identified. NLS-1 (aa 149-156) and NLS-2 (aa 185-194) correspond to residues with unknown function(s), whereas NLS-3 (aa 276-292) matches with a designated multimerization domain. Nuclear export signal(s) were not identified. Endoproteolytic processing by the 20S proteasome before glycine 220 releases a carboxy-terminal fragment (CTF), which localized to the nucleus, indicating that NLS-3 is operative. Genotoxic stress induced proteolytic cleavage and nuclear translocation of the CTF. Co-expression of the CTF and full-length YB-1 resulted in an abrogated transcriptional activation of the MMP-2 promoter, indicating an autoregulatory inhibitory loop, whereas it fulfilled similar trans-repressive effects on the collagen type I promoter. Conclusion: Compartmentalization of YB-1 protein derivatives is controlled by distinct NLS, one of which targets a proteolytic cleavage product to the nucleus. We propose a model for an autoregulatory negative feedback loop that halts unlimited transcriptional activation.Medicine, Faculty ofPediatrics, Department ofReviewedFacult