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Differential expression of brain proteins in glycogen synthase kinase‐3 transgenic mice: A proteomics point of view
Author(s) -
Tilleman Kelly,
Stevens Ilse,
Spittaels Kurt,
Haute Chris Van den,
Clerens Stefan,
Van den Bergh Gert,
Geerts Hugo,
Van Leuven Fred,
Vandesande Frans,
Moens Luc
Publication year - 2002
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200201)2:1<94::aid-prot94>3.0.co;2-w
Subject(s) - proteomics , gsk 3 , transgene , genetically modified mouse , biology , glycogen synthase , gsk3b , microbiology and biotechnology , biochemistry , kinase , enzyme , computational biology , gene
One of the landmarks of Alzheimer’s disease are neurofibrillary tangles (NFT) in the brain. NFT mainly consist of a hyperphosphorylated form of the protein tau, which is responsible for stabilisation of the neuronal cytoskeleton by microtubule binding and is unable to function properly in its hyperphosphorylated form. Glycogen synthase kinase‐3β (GSK3β) is able to phosphorylate tau in a cellular context which could play a role in the formation of these NFT. In order to learn more about the effect of GSK‐3β in the brain, two‐dimensional electrophoresis patterns of cerebrum extracts of GSK3β[S9A] transgenic mice and wild type mice were compared quantitatively. Fifty‐one spots were identified as being different in integrated intensity by at least a factor 1.5. The spots were subsequently identified by mass spectrometry. Identification of several proteins linked to signal transduction pathways in which GSK3β plays a role, indicates that our population of identified proteins includes some down stream proteins of GSK3β. This study may contribute to filling the gaps between GSK3β, its substrates and finally the phosphorylation of tau.