par Hanger, Diane;Hughes, K;Woodgett, James R;Brion, Jean Pierre ;Anderton, Brian
Référence Neuroscience letters, 147, 1, page (58-62)
Publication Publié, 1992-11
Référence Neuroscience letters, 147, 1, page (58-62)
Publication Publié, 1992-11
Article révisé par les pairs
Résumé : | Glycogen synthase kinase-3 (GSK-3) reduced the mobility of human tau on SDS-PAGE, prevented binding of the monoclonal antibody (mAb), Tau.1, and induced binding of the mAb 8D8. Recombinant tau phosphorylated by GSK-3 aligned on SDS-PAGE with the abnormally phosphorylated tau (PHF-tau) associated with the paired helical filaments in Alzheimer's disease brain. Phosphorylated serine396 (numbering of the largest human brain tau isoform) was identified as a binding site on tau for mAb 8D8. The localisation of GSK-3 within granular structures in pyramidal cells indicates that GSK-3 alpha and GSK-3 beta may have a role in the production of PHF-tau in Alzheimer's disease. |