Prostaglandin H2 (PGH2) accelerates formation of amyloid β1-42 oligomers

被引:54
作者
Boutaud, O [1 ]
Ou, JJ
Chaurand, P
Caprioli, RM
Montine, TJ
Oates, JA
机构
[1] Vanderbilt Univ, Dept Pharmacol, Nashville, TN 37203 USA
[2] Vanderbilt Univ, Ctr Mol Neurosci, Nashville, TN USA
[3] Vanderbilt Univ, Dept Biochem, Nashville, TN 37232 USA
[4] Vanderbilt Univ, Mass Spectrometry Res Ctr, Dept Pathol, Nashville, TN USA
[5] Vanderbilt Univ, Mass Spectrometry Res Ctr, Dept Med, Nashville, TN USA
关键词
Alzheimer; amyloid; cyclooxygenase; levuglandin; oligomer;
D O I
10.1046/j.1471-4159.2002.01064.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Epidemiologic evidence implicates cyclooxygenase activity in the pathogenesis of Alzheimer's disease, in which amyloid plaques have been found to contain increased levels of dimers and higher multimers of the amyloid beta peptide. The product of the oxygenation of arachidonic acid by the cyclooxygenases, prostaglandin H-2 (PGH(2) ), rearranges non-enzymatically to several prostaglandins, including the highly reactive gamma-keto aldehydes, levuglandins E-2 and D-2 . We demonstrate that PGH(2) markedly accelerates the formation of dimers and higher oligomers of amyloid beta(1-42) . This is associated with the formation of levuglandin adducts of the peptide. These findings provide the molecular basis for a hypothesis linking cyclooxygenase activity to the formation of oligomers of amyloid beta.
引用
收藏
页码:1003 / 1006
页数:4
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