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-? (A?) peptide has been implicated in the pathology of Alzheimer's disease (AD). Using an antisense peptide approach a novel interaction between A? and the human cdc2 kinase was identified. The A? 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 A? (pSA?) was found in extracts from NT-2 neurons and AD brain. In NT-2 neurons the levels of pSA? were increased in the presence of exogenous A? and this increase was prevented by a cdc2 protein kinase inhibitor, olomoucine, that also prevented A? cytotoxicity. The results from this study suggest that A? phosphorylation by cdc2 could play a role in the brain pathology of AD.

Item Type: Article
Subjects: University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)
Depositing User: Miss Nina Watts
Date Deposited: 26 Jan 2010 15:49
Last Modified: 26 Jan 2010 15:49
URI: http://westminsterresearch.wmin.ac.uk/id/eprint/7382

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