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“Please cite this paper as: Bruns, Watanpour, Gebhard, Flechtenmacher, Galli, Schulze-Bergkamen, Zorn, Büchler and Schemmer (2011).

Glycine and Taurine Equally Prevent Fatty Livers from Kupffer Cell-Dependent Injury: An In Vivo Microscopy Study. Microcirculation 18(3), 205–213. Background:  IRI still is a major problem in liver surgery due to warm ischemia and organ manipulation. Steatosis is not only induced by diabetes, hyperalimentation, alcohol and toxins, but also chemotherapy given before resection. Since steatotic livers are prone to Kupffer cell-dependent IRI, protection of steatotic livers is of special interest. This study was designed to compare the effect of taurine and glycine on IRI in steatotic

livers. Materials and Methods:  Steatosis was induced with ethanol Selleckchem Osimertinib (7 g/kg b.w.; p.o.) in female SD rats. Ten minutes after inactivation of Kupffer cells with taurine or glycine (300 mM; i.v.), left liver lobes underwent 60 minutes of warm ischemia. Controls received the same volume of valine (300 mM; i.v.) or normal saline. After reperfusion, white Small molecule library blood cell-endothelial interactions and latex-bead phagocytosis by Kupffer cells were investigated. Liver enzymes were measured to estimate injury. For statistical analysis, ANOVA and Student’s t-test were used. Results:  Glycine and taurine significantly decreased leukocyte- and platelet-endothelium interactions and latex-bead phagocytosis

(p < 0.05). Liver enzymes were significantly lower after glycine and taurine (p < 0.05). Conclusions:  This study shows that preconditioning with taurine or glycine is equally effective in preventing injury to fatty livers most likely via Kupffer cell-dependent mechanisms. "
“Angiogenesis is a multistep process that requires intricate changes in cell shape to generate new blood vessels. IF are a large family of proteins that play an important structural and functional role in forming and regulating the cytoskeleton. Vimentin, a major type III intermediate filament protein is expressed in endothelial and other mesenchymal cells. The structure of vimentin is conserved in mammals and shows dynamic expression profiles in various cell types and different developmental stages. Although initial studies with vimentin-deficient Clostridium perfringens alpha toxin mice demonstrated a virtually normal phenotype, subsequent studies have revealed several defects in cell attachment, migration, signaling, neurite extension, and vascularization. Regulation of vimentin is highly complex and is driven by posttranslational modifications such as phosphorylation and cleavage by intracellular proteases. This review discusses various novel functions which are now known to be mediated by vimentin, summarizing structure, regulation and roles of vimentin in cell adhesion, migration, angiogenesis, neurite extension, and cancer.