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

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3839-3844
Number of pages6
JournalNeuroReport
Volume12
Issue number17
DOIs
Publication statusPublished - 4 Dec 2001
Externally publishedYes

Keywords

  • Amyloid-β
  • Antisense peptide
  • Cdc2
  • Cyclin
  • Olomoucine
  • Phosphorylation

Fingerprint

Dive into the research topics of 'Phosphorylation of amyloid-β at the serine 26 residue by human cdc2 kinase'. Together they form a unique fingerprint.

Cite this