Phosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase

Milton, N.G.N. 2001. Phosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase. NeuroReport. 12 (17), pp. 3839-3844.

TitlePhosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase
AuthorsMilton, N.G.N.
Abstract

The amyloid-β (Aβ) peptide has been implicated in the pathology of Alzheimer's disease (AD). Using an antisense peptide approach a novel interaction between Aβ and the human cdc2 kinase was identified. The Aβ 1-42, 1-40 and 25-35 peptides were shown to be substrates for the cdc2 kinase and phosphorylated on the Serine 26 residue. Phosphorylated Aβ (pSAβ) was found in extracts from NT-2 neurons and AD brain. In NT-2 neurons the levels of pSAβ were increased in the presence of exogenous Aβ and this increase was prevented by a cdc2 protein kinase inhibitor, olomoucine, that also prevented Aβ cytotoxicity. The results from this study suggest that Aβ phosphorylation by cdc2 could play a role in the brain pathology of AD.

JournalNeuroReport
Journal citation12 (17), pp. 3839-3844
ISSN0959-4965
Year04 Dec 2001
PublisherLippincott Williams & Wilkins
Publication dates
Published04 Dec 2001

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