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

Milton, Nathaniel G.N. (2001) Phosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase. NeuroReport, 12 (17). pp. 3839-3844. ISSN 0959-4965

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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.

Item Type:Article
Research Community:University of Westminster > Life Sciences, School of
ID Code:7382
Deposited On:26 Jan 2010 15:49
Last Modified:26 Jan 2010 15:49

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