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Rösler, R.

Publications and source records attributed to Rösler, R..

2 recordsLinked to original sources

Pathophysiological response in experimental trauma-related acute kidney injury

BackgroundTrauma and shock often severely affect the kidneys. This can lead to trauma-related acute kidney injury (TRAKI), which significantly increases the risk of adverse outcomes. MethodsTo study the pathophysiology of TRAKI, we developed a murine model of combined blunt thoracic trauma and pressure-controlled hemorrhage that induces mild transient TRAKI. ResultsThe mice showed early and transient increased plasma creatinine, urea, NGAL, and urine albumin, resolving 5 days after TRAKI induction. Despite normal kidney morphology, significant damage to proximal tubular cells and a loss of the brush border was observed. This included kidney stress responses, e.g., with induced heme oxygenase-1 expression in tubules. The upregulation of inflammatory mediators and kidney injury markers was followed by elevated leukocyte numbers, mainly consisting of monocytes/macrophages. Proteomic analyses revealed a distinct time course of intrarenal processes after trauma. 3D x-ray-based whole-organ histology by contrast-enhanced microcomputed tomography showed significant impairment of capillary blood flow, especially during the first day post THS, which was partly resolved by day 5. ConclusionsOur novel model of murine TRAKI has revealed previously unknown aspects of the complex temporal pathophysiological response of the kidney along the nephron after trauma and hemorrhage, which may provide mechanistic starting points for future therapeutic approaches.

pathology↗

An interaction network of the human SEPT9 established by quantitative mass spectrometry reveals an interplay with myosin motors

SummaryPhenotypic variations of an organism or a single cell often arise from alterations of protein interaction networks. We provide here an interaction network of the human SEPT9, an important component of the human septin cytoskeleton.\n\nAbstractExperimentally deciphering and understanding the interaction network of a particular protein provides often evidence for so far unknown functions. For the septins, a class of cytoskeletal proteins, targeted high-throughput approaches that aim at systematically deciphering interaction partners have not yet been performed. Septins regulate the organization of the acin cytoskeleton, vesicle transport and fusion, chromosome alignment-and segregation, and cytokinesis. SEPT9 is part of the core septin hetero-octamer in human cells which is composed of SEPT2, SEPT6, SEPT7, and SEPT9. SEPT9 has been linked to a variety of intracellular functions as well as to diseases and diverse types of cancer. We applied a quantitative proteomics approach to establish an interactome of SEPT9 in human fibroblast cells. We identified among others so far unknown interaction partners from the myosin family and could provide evidence that SEPT9 participates in vesicle transport from and to the plasma membrane as well as in the attachment of actin stress fibers to cellular adhesions.

cell biology↗