This review, containing some of our recent findings of centrally expressed SCT on water intake, focuses on the actions of SCT in influencing the physiological, neuroendocrine, and cardiovascular processes that subserve body fluid homeostasis. Kidney International (2011) 79, 280-287; doi:10.1038/ki.2010.397; published online 13 October 2010″
“C5a is thought to play a role during complement-activated neuronal apoptotic cell death in the central nervous system. The mechanisms

responsible are however not well-understood. As mitochondria play a key role during apoptosis, we investigated mitochondria as a potential target for C5a. Using PC12 cells, we demonstrated that exposure to C5a led to inhibition of mitochondrial respiration, dehydrogenase and Belnacasan manufacturer cytochrome AZD1208 solubility dmso c oxidase activities. Interestingly, an increase in expression of the mitochondrial stress protein chaperonin 60 was also observed, confirming a marked effect

of C5a on mitochondrial functions. These observations are the first documented intracellular effects noted for the complement molecule C5a in in-vitro cultured cells. NeuroReport 22:581-585 (C) 2011 Wolters Kluwer Health vertical bar Lippincott Williams & Wilkins.”
“In addition to skeletal muscle and the nervous system, alpha-dystroglycan is found in the podocyte basal membrane, stabilizing these cells on the glomerular basement membrane. Fukutin, named after the gene responsible for Fukuyama-type congenital muscular dystrophy, is a putative glycosyltransferase required for the post-translational modification of alpha-dystroglycan. Chimeric mice targeted for both alleles of fukutin develop severe muscular dystrophy; however, these mice do not have proteinuria. Despite the lack of a functional renal defect,

we evaluated glomerular structure and found minor abnormalities in the chimeric mice by light microscopy. Electron microscopy revealed flattening of podocyte foot processes, the number of which was significantly lower in the chimeric compared to wild-type mice. A monoclonal antibody against the laminin-binding carbohydrate residues of alpha-dystroglycan did not detect find more alpha-dystroglycan glycosylation in the glomeruli by immunoblotting or immunohistochemistry. In contrast, expression of the core alpha-dystroglycan protein was preserved. There was no statistical difference in dystroglycan mRNA expression or in the amount of nephrin and alpha 3-integrin protein in the chimeric compared to the wild-type mice as judged by immunohistochemistry and real-time RT-PCR. Thus, our results indicate that appropriate glycosylation of alpha-dystroglycan has an important role in the maintenance of podocyte architecture. Kidney International (2011) 79, 311-316; doi:10.1038/ki.2010.