Premium
Prostaglandin H 2 (PGH 2 ) accelerates formation of amyloid β 1−42 oligomers
Author(s) -
Boutaud Olivier,
Ou Joyce J.,
Chaurand Pierre,
Caprioli Richard M.,
Montine Thomas J.,
Oates John A.
Publication year - 2002
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2002.01064.x
Subject(s) - arachidonic acid , cyclooxygenase , chemistry , pathogenesis , amyloid (mycology) , prostaglandin , peptide , alzheimer's disease , biochemistry , prostaglandin e , medicine , enzyme , disease , inorganic chemistry
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 β 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 γ‐keto aldehydes, levuglandins E 2 and D 2 . We demonstrate that PGH 2 markedly accelerates the formation of dimers and higher oligomers of amyloid β 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 β.