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P1‐428: Phosphorylation of APP, TAU and PIN1 is regulated by JNK
Author(s) -
Forloni Gianluigi,
Colombo Alessio,
Borsello Tiziana
Publication year - 2008
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2008.05.1010
Subject(s) - pin1 , phosphorylation , senile plaques , amyloid precursor protein , microbiology and biotechnology , chemistry , prolyl isomerase , p3 peptide , intracellular , kinase , extracellular , mg132 , tau protein , neurodegeneration , proteasome , alzheimer's disease , biochemistry , biology , isomerase , proteasome inhibitor , medicine , enzyme , disease
both neuroblastoma cells as well as in primary neurons when compared to wild-type forms. In addition, we could identify specific glycine residues within the A 42 sequence that were responsible to inhibit LTP in rat hippocampal slices. Conclusions: In conclusion, GxxxG mutant peptides allowed dissecting toxicity from oligomerization processes of A . This leads to the following assumptions, (i) soluble A oligomers are not necessarily toxic and (ii) those oligomeric A species which are toxic can inhibit LTP. Thus, oligomerization is not sufficient for A to exert its toxic function. But A toxicity is linked to LTP inhibition. Taken together, GxxxG mutants are extremely useful tools to unravel the role of A in the pathogenesis.