Модернизация технологического процесса сбора и утилизации газа на установках подготовки нефти на месторождениях Западной Сибири

Объектом исследования является технологический процесс подготовки скважинной продукции и осушки газа на установке подготовки нефти (УПН) п. Пионерный Катыльгинского нефтяного месторождения компании АО "Томскнефть" ВНК, а также технология компримирования газа на дожимной контейнерной компрессорной станции (ДККС). Целью данной работы является компримирование попутного нефтяного газа добытого на второй ступени сепарации на объекте УПН "Пионерный" и доказательство эффективности использования ДККС. В процессе исследования проведен анализ эффективности работы дожимной контейнерной компрессорной станции. В результате исследования была доказана эффективность внедрения ДККС в технологический процесс объекта УПН "Пионерный", путем снижения количества вредных выбросов в атмосферу.The object of the study is the technological process of well production preparation and gas dehydration at the oil treatment unit (OTP) of the Pionerny settlement of the Katylginsky oil field of the JSC Tomskneft VNK, as well as the technology of gas compression at the booster container compressor station (DCKS). The purpose of this work is to compress associated petroleum gas produced at the second stage of separation at the Pioneer OTF facility and to prove the efficiency of using the DCS. In the course of the study, the analysis of the efficiency of the booster container compressor station was carried out

Nachweis der Sekretion eines Kälteschockproteins und Aufklärung zugrundeliegender Exportmechanismen

The cold shock protein Y-box (YB) protein-1 posseses DNA- as well as RNA-binding capacities and plays a crucial role in both, gene transcription and mRNA processing. Very recently, our group demonstrated a diffuse staining pattern for YB-1 in inflammatory glomerular diseases without strict adherence to cell boundaries suggesting a secretion and extracellular functions of YB-1. We set out to analyze extracelluar occurrence of YB-1 in two model systems: mesangial cells (MC) with stable expression of a hemagglutinin-tagged YB-1 protein and monocytes (MonoMac6, MM6 cells). YB-1 and protein fragments thereof were detected in the cell culture medium of MCs within one and four hours upon challenge with various proinflammatory cytokines (platelet-derived growth factor (PDGF)-BB, transforming growth factor (TGF)-ß). Furthermore, we observed a comparable secretory YB-1 response in MM6 cells that showed high similarity to the secretion of macrophage-inhibitory factor (MIF) with a tight dose- and time-dependency within a narrow LPS concentration range between 1 to 7.5 ng/ml. Kinetic experiments (at a fixed concentration of 5 ng/ml LPS over a period of 24 h) revealed a “constitutive” YB-1 secretion in the first four hours and elevated secretion in the subsequent 20 hours. We extended our studies to primary human monocytes that have been isolated from healthy donors and observed a similar secretion mode following LPS stimulation. By sequential centrifugation of supernatants, secreted YB-1 was enriched in vesicle preparations. To elucidate the molecular mechanism underlying YB-1 secretion we utilized various inhibitors of well-established secretion pathways. Reserpine (inhibitor of ATP-dependent uptake of bioamines into vesicular structures) potently inhibits constitutive as well as LPS-dependent YB-1 secretion. Ionomycine (a ionophore that induces degranulation in distinct cell types) was found to have a stimulatory effect on the LPS-induced secretion of YB-1. Taken together, these results strongly support our hypothesis of a vesicle-mediated YB-1 secretion. YB-1 protein lacks a typical N-terminal signal peptide that may direct the protein to the endoplasmatic reticulum (ER) which suggests a non-classical secretion mode. Specific inhibition of the classical secretion pathway by brefeldin A and monensin results in “super-induction” of LPS-dependent YB-1 release, whereas inhibitors of ABC transporters (glyburid, probenecid) abrogated this response. We provide evidence that secreted YB-1 is not N-glycosylated and secretion was induced by elevated extracellular ATP levels. The export of YB-1 was reduced by tubulozol and paclitaxel, both inhibitors of tubulin depolymerisation, suggesting that YB-1 secretion requires an intact tubulin network. These results are in line with ABC-transporter-dependent enrichment of YB-1 in vesicles and non-classical secretion bypassing the ER. Finally we set out to elucidate potential extracellular propensities of secreted YB-1. To this goal, we added recombinant YB-1 protein to cultured MCs and human tubular cells and observed an increased rate of DNA synthesis that was abrogated by adding a “neutralizing” anti-YB-1 antibody. In summary, the presented studies provide new insights into the secretion mode of YB-1 protein via a non-classical pathway following challenge with various inflammatory stimuli. Extracellular YB-1 may exert mitogenic effects on renal cells

Nachweis der Sekretion eines Kälteschockproteins und Aufklärung zugrundeliegender Exportmechanismen

The cold shock protein Y-box (YB) protein-1 posseses DNA- as well as RNA-binding capacities and plays a crucial role in both, gene transcription and mRNA processing. Very recently, our group demonstrated a diffuse staining pattern for YB-1 in inflammatory glomerular diseases without strict adherence to cell boundaries suggesting a secretion and extracellular functions of YB-1. We set out to analyze extracelluar occurrence of YB-1 in two model systems: mesangial cells (MC) with stable expression of a hemagglutinin-tagged YB-1 protein and monocytes (MonoMac6, MM6 cells). YB-1 and protein fragments thereof were detected in the cell culture medium of MCs within one and four hours upon challenge with various proinflammatory cytokines (platelet-derived growth factor (PDGF)-BB, transforming growth factor (TGF)-ß). Furthermore, we observed a comparable secretory YB-1 response in MM6 cells that showed high similarity to the secretion of macrophage-inhibitory factor (MIF) with a tight dose- and time-dependency within a narrow LPS concentration range between 1 to 7.5 ng/ml. Kinetic experiments (at a fixed concentration of 5 ng/ml LPS over a period of 24 h) revealed a “constitutive” YB-1 secretion in the first four hours and elevated secretion in the subsequent 20 hours. We extended our studies to primary human monocytes that have been isolated from healthy donors and observed a similar secretion mode following LPS stimulation. By sequential centrifugation of supernatants, secreted YB-1 was enriched in vesicle preparations. To elucidate the molecular mechanism underlying YB-1 secretion we utilized various inhibitors of well-established secretion pathways. Reserpine (inhibitor of ATP-dependent uptake of bioamines into vesicular structures) potently inhibits constitutive as well as LPS-dependent YB-1 secretion. Ionomycine (a ionophore that induces degranulation in distinct cell types) was found to have a stimulatory effect on the LPS-induced secretion of YB-1. Taken together, these results strongly support our hypothesis of a vesicle-mediated YB-1 secretion. YB-1 protein lacks a typical N-terminal signal peptide that may direct the protein to the endoplasmatic reticulum (ER) which suggests a non-classical secretion mode. Specific inhibition of the classical secretion pathway by brefeldin A and monensin results in “super-induction” of LPS-dependent YB-1 release, whereas inhibitors of ABC transporters (glyburid, probenecid) abrogated this response. We provide evidence that secreted YB-1 is not N-glycosylated and secretion was induced by elevated extracellular ATP levels. The export of YB-1 was reduced by tubulozol and paclitaxel, both inhibitors of tubulin depolymerisation, suggesting that YB-1 secretion requires an intact tubulin network. These results are in line with ABC-transporter-dependent enrichment of YB-1 in vesicles and non-classical secretion bypassing the ER. Finally we set out to elucidate potential extracellular propensities of secreted YB-1. To this goal, we added recombinant YB-1 protein to cultured MCs and human tubular cells and observed an increased rate of DNA synthesis that was abrogated by adding a “neutralizing” anti-YB-1 antibody. In summary, the presented studies provide new insights into the secretion mode of YB-1 protein via a non-classical pathway following challenge with various inflammatory stimuli. Extracellular YB-1 may exert mitogenic effects on renal cells