Electrospun nanofibers were coated with lung extracts from fibrotic or non-fibrotic mice and used to determine effects on bone marrow cells from naive mice. Varying moduli nanofibers were also employed to determine matrix stiffness effects on these cells. At structured time points, bone marrow cell morphology was recorded and changes in fibrotic gene expression Crenigacestat purchase determined by real-time

PCR. Cells plated on extracts isolated from fibrotic murine lungs secreted larger amounts of extracellular matrix, adopted a fibroblastic morphology, and exhibited increased myofibroblast gene expression after 8 and 14 days; cells plated on extracts from non-fibrotic lungs did not. Similar results were observed when the nanofiber modulus was increased. This ex vivo system appears to recapitulate the three-dimensional fibrotic lung microenvironment. (C) 2010 Published by Elsevier Ltd”
“SummaryBackground\n\nGlycoprotein VI (GPVI), 60-65 kDa, is a major collagen receptor on platelet membranes involved in adhesive and signaling responses. Mice lacking https://www.selleckchem.com/products/MK-1775.html GPVI have impaired platelet response to collagen and defective primary adhesion and subsequent thrombus formation. Complete or partial deficiency of GPVI in humans is a rare condition presenting

as a mild bleeding disorder. The defect in most of the reported patients is acquired and associated with LY3039478 other diseases. To date, only two patients have been characterized at the molecular level who carry different compound heterozygous mutations in the GP6 gene.\n\nObjective\n\nTo report four unrelated patients from non-consanguineous families who presented with mucocutaneous bleeding. They

had absent platelet aggregation and C-14-5-HT secretion with collagen, convulxin and collagen-related peptide.\n\nResults\n\nFlow cytometry and immunofluorescence-confocal microscopy showed an absence of GPVI in non-permeabilized platelets. All the patients had an adenine insertion in exon 6 (c.711_712insA), changing the reading frame and generating a premature ‘stop codon’ in site 242 of the protein. The mutation predicts the synthesis of the truncated protein before the trans-membrane domain, corresponding to a band of approximate to 49 kDa observed in western blots and in permeabilized platelets by immunofluorescence. Platelet mRNA from all the patients was sequenced and contained the corresponding adenine insertion. Heterozygous relatives had no pathological bleeding, normal response to collagen and convulxin and intermediate membrane expression of GPVI.\n\nConclusions\n\nThe identification of four unrelated homozygous patients with an identical defect suggests that inherited GPVI deficiency is more frequent than previously suspected, at least in Chile.”
“Birth weight may be influenced by environmental and socio-economic factors that could interact.