Source:http://linkedlifedata.com/resource/pubmed/id/11444797
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2001-7-10
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pubmed:abstractText |
A reactive intermediate generated by lipid peroxidation, 4-hydroxy-2-nonenal (HNE), has received considerable attention as a potential effector of oxidative damage and Abeta peptide-mediated neurotoxicity in Alzheimer disease (AD). However, little is known about aldo-keto oxidoreductases, a group of enzymes that constitute a major detoxifying pathway for HNE and related reactive aldehydes in human brain. We have determined the regional, cellular, and class distribution in human brain of the 4 major aldo-keto oxidoreductases that detoxify HNE: aldehyde dehydrogenase (ALDH): aldose reductase; aldehyde reductase: and alcohol dehydrogenase (ADH). Of these 4 enzymes, only ALDH and aldose reductase were expressed in cerebral cortex. hippocampus, basal ganglia, and midbrain: all 4 enzymes were present in cerebellum. In cerebrum and hippocampus, aldose reductase was localized to pyramidal neurons and mitochondrial class 2 ALDH was localized to glia and senile plaques. ALDH, but not aldose reductase, activity was significantly increased in temporal cortex from patients with AD compared to age-matched controls. These results suggest that in brain regions involved in AD, neurons and glia utilize different mechanisms to detoxify HNE, and that increased ALDH activity is a protective response of cerebral cortex to AD.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxy-2-nonenal,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehydes
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-3069
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
686-95
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11444797-Alcohol Dehydrogenase,
pubmed-meshheading:11444797-Aldehyde Dehydrogenase,
pubmed-meshheading:11444797-Aldehyde Reductase,
pubmed-meshheading:11444797-Aldehydes,
pubmed-meshheading:11444797-Alzheimer Disease,
pubmed-meshheading:11444797-Animals,
pubmed-meshheading:11444797-Antibody Specificity,
pubmed-meshheading:11444797-Brain,
pubmed-meshheading:11444797-Enzyme Activation,
pubmed-meshheading:11444797-Humans,
pubmed-meshheading:11444797-Immunoblotting,
pubmed-meshheading:11444797-Male,
pubmed-meshheading:11444797-Mice,
pubmed-meshheading:11444797-Mice, Inbred C57BL,
pubmed-meshheading:11444797-Neuroglia,
pubmed-meshheading:11444797-Organ Specificity,
pubmed-meshheading:11444797-Pyramidal Cells
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pubmed:year |
2001
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pubmed:articleTitle |
Expression and activities of aldo-keto oxidoreductases in Alzheimer disease.
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pubmed:affiliation |
Department of Pathology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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