The amyloid-? peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity

Milton, Nathaniel G.N. (2002) The amyloid-? peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity. Neuroscience Letters, 322 (2). pp. 131-133. ISSN 0304-3940

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/S0304-3940(02)00081-2

Abstract

The pathological features of Alzheimer's disease include deposition of amyloid-? (A?) containing plaques and increases in the expression of cyclin-dependent kinase (CDK) enzymes. Chemical inhibition of CDKs prevents the neurotoxicity of the A? peptide. The activity of these kinases requires the binding of a cyclin component to the catalytic enzyme component. This study characterizes direct interactions between A? and cyclin B1. A? fragments containing the cytotoxic 31–35 region could inhibit biotinylated A? binding to cyclin B1. The same cytotoxic A? fragments all increased CDK-1 phosphorylation of known substrates in a cell free system. The CDK-1 inhibitor olomoucine prevented the cytotoxicity of A? 31–35 containing peptides in differentiated human teratocarcinoma cell line, Ntera 2/cl-D1 (NT-2) neurons. These direct interactions between cyclin B1 and A? provide potential mechanisms for the cytotoxicity of the A? peptide.

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 15:33
Last Modified: 26 Jan 2010 15:33
URI: http://westminsterresearch.wmin.ac.uk/id/eprint/7379

Actions (login required)

Edit Item (Repository staff only) Edit Item (Repository staff only)