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J Biol Chem, Vol. 274, Issue 22, 15493-15499, May 28, 1999
-Amyloid Activates the O
2 Forming NADPH Oxidase in
Microglia, Monocytes, and Neutrophils
,,,
From the The deposition of Institute of General Pathology and the
§ Chair of Histology and Embryology, University of Verona,
37134 Verona, Italy
-amyloid in the brain is the
key pathogenetic event in Alzheimer's disease. Among the various
mechanisms proposed to explain the neurotoxicity of -amyloid
deposits, a new one, recently identified in our and other laboratories,
suggests that -amyloid is indirectly neurotoxic by activating
microglia to produce toxic inflammatory mediators such as cytokines,
nitric oxide, and oxygen free radicals. Three findings presented here support this mechanism, showing that -amyloid peptides (25-35), (1-39), and (1-42) activated the classical NADPH oxidase in rat primary culture of microglial cells and human phagocytes: 1) The exposure of the cells to -amyloid peptides stimulates the production of reactive oxygen intermediates; 2) the stimulation is associated with
the assembly of the cytosolic components of NADPH oxidase on the plasma
membrane, the process that corresponds to the activation of the enzyme;
3) neutrophils and monocytes of chronic granulomatous disease patients
do not respond to -amyloid peptides with the stimulation of reactive
oxygen intermediate production. Data are also presented that the
activation of NADPH oxidase requires that -amyloid peptides be in
fibrillary state, is inhibited by inhibitors of tyrosine kinases or
phosphatidylinositol 3-kinase and by dibutyryl cyclic AMP, and is
potentiated by interferon-
or tumor necrosis factor-
.
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