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p38 Kinase Is Activated in the Alzheimer's Disease Brain
Author(s) -
Hensley Kenneth,
Floyd Robert A.,
Zheng NaiYing,
Nael Raha,
Robinson Kent A.,
Nguyen Xuan,
Pye Quentin N.,
Stewart Charles A.,
Geddes James,
Markesbery William R.,
Patel Ela,
Johnson Gail V. W.,
Bing Guoying
Publication year - 1999
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.1471-4159.1999.0722053.x
Subject(s) - p38 mitogen activated protein kinases , phosphorylation , tangle , senile plaques , kinase , protein kinase a , neuropil , microbiology and biotechnology , neuroscience , alzheimer's disease , tau protein , neurofibrillary tangle , signal transduction , biology , cytoskeleton , cyclin dependent kinase 5 , chemistry , pathology , medicine , biochemistry , cell , disease , mitogen activated protein kinase kinase , central nervous system , mathematics , pure mathematics
The p38 mitogen‐activated protein kinase is a stress‐activated enzyme responsible for transducing inflammatory signals and initiating apoptosis. In the Alzheimer's disease (AD) brain, increased levels of phosphorylated (active) p38 were detected relative to age‐matched normal brain. Intense phospho‐p38 immunoreactivity was associated with neuritic plaques, neuropil threads, and neurofibrillary tangle‐bearing neurons. The antibody against phosphorylated p38 recognized many of the same structures as an antibody against aberrantly phosphorylated, paired helical filament (PHF) tau, although PHF‐positive tau did not cross‐react with the phospho‐p38 antibody. These findings suggest a neuroinflammatory mechanism in the AD brain, in which aberrant protein phosphorylation affects signal transduction elements, including the p38 kinase cascade, as well as cytoskeletal components.