Publications by authors named "Veronica Ramberg"
Aggregation of amyloid beta (Aβ) peptides and the subsequent neural plaque formation is a central aspect of Alzheimer's disease. Various strategies to reduce Aβ load in the brain are therefore intensely pursued. It has been hypothesized that reducing Aβ peptides in the periphery, that is in organs outside the brain, would be a way to diminish Aβ levels and plaque load in the brain.
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- Recent research highlights local caspase activity in neuronal structures during development and in conditions like Alzheimer's disease, implicating soluble amyloid-β as a significant factor.
- The study utilizes fluorescence resonance energy transfer (FRET)-based sensors linked to tau protein to monitor caspase activation in human neuroblastoma cells, revealing unique patterns of activation in both neurites and cell bodies.
- Findings suggest that specific amyloid-β exposure causes a widespread activation of caspases, primarily caspase-3 and -6, which contributes to neuronal degeneration.
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- C/EBP transcription factors α, β, and δ regulate inflammatory genes in the brain, with C/EBPα typically down-regulated and C/EBPβ and δ up-regulated during inflammation.
- Research in Alzheimer's disease highlights chronic neuroinflammation linked to amyloid-β (Aβ) deposits, complicating the understanding of their effects which can be both beneficial and harmful.
- In studies, exposure to fibrillar Aβ was found to inhibit C/EBPδ expression in glial cultures, while C/EBPα was down-regulated and C/EBPβ was up-regulated in aged transgenic mice, showing variations in expression based on brain regions affected by Aβ.
Alzheimer amyloid-beta peptides block the activation of C/EBPbeta and C/EBPdelta in glial cells.
Biochem Biophys Res Commun
June 2008
Members of the CCAAT/enhancer binding protein (C/EBP) family of transcription factors have been reported to be up-regulated in Alzheimer's disease. In the present study, we have investigated the effects of amyloid-beta (Abeta) peptides on C/EBPbeta and C/EBPdelta, previously shown to be induced by inflammatory stimuli in glial cells. Surprisingly, electrophoretic mobility shift assay showed that both Abeta(1-42) and Abeta(25-35) blocked C/EBP activation induced by the inflammatory cytokine interleukin-1beta (IL-1beta) or lipopolysaccharide (LPS) in mixed primary glial cell cultures from rat.
View Article and Find Full Text PDFInhibition of nuclear factor (NF)-kappaB has emerged as an important strategy for design of anti-inflammatory therapies. In neurodegenerative disorders like Alzheimer's disease, inflammatory reactions mediated by glial cells are believed to promote disease progression. Here, we report that uptake of a double-stranded oligonucleotide NF-kappaB decoy in rat primary glial cells is clearly facilitated by noncovalent binding to a cell-penetrating peptide, transportan 10, via a complementary peptide nucleic acid (PNA) sequence.
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