Activation of glycogen synthase kinase-3 beta mediates β-amyloid induced neuritic damage in Alzheimer's disease

  title={Activation of glycogen synthase kinase-3 beta mediates β-amyloid induced neuritic damage in Alzheimer's disease},
  author={B. DaRocha-Souto and M. Coma and B. Perez-Nievas and T. C. Scotton and T. G{\'o}mez-Isla},
  journal={Neurobiology of Disease},
  • B. DaRocha-Souto, M. Coma, +2 authors T. Gómez-Isla
  • Published 2012
  • Biology, Medicine
  • Neurobiology of Disease
  • β-Amyloid (Aβ) plaques in Alzheimer (AD) brains are surrounded by severe dendritic and axonal changes, including local spine loss, axonal swellings and distorted neurite trajectories. Whether and how plaques induce these neuropil abnormalities remains unknown. We tested the hypothesis that oligomeric assemblies of Aβ, seen in the periphery of plaques, mediate the neurodegenerative phenotype of AD by triggering activation of the enzyme GSK-3β, which in turn appears to inhibit a transcriptional… CONTINUE READING
    113 Citations
    RPS23RG1 reduces Aβ oligomer-induced synaptic and cognitive deficits
    • 7
    • PDF
    Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: implications for synaptic dysfunction and neuronal damage.
    • P. Reddy
    • Biology, Medicine
    • Biochimica et biophysica acta
    • 2013
    • 74
    • Highly Influenced
    CREB expression mediates amyloid β-induced basal BDNF downregulation
    • 51
    • Highly Influenced
    Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis.
    • 77


    Distribution, Levels, and Activity of Glycogen Synthase Kinase‐3 in the Alzheimer Disease Brain
    • 303
    • PDF
    Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • 2,072
    • PDF
    GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • 967
    Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain
    • 153
    • Highly Influential
    • PDF