Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1993-12-23
|
| pubmed:abstractText |
The cause of neuronal death in amyotrophic lateral sclerosis (ALS) is unknown. Recently, it was found that some patients with autosomal-dominant familial ALS (FALS) have point mutations in the gene that encodes Cu/Zn superoxide dismutase (SOD1). In this study of postmortem brain tissue, we examined SOD activity and quantified protein carbonyl groups, a marker of oxidative damage, in samples of frontal cortex (Brodmann area 6) from 10 control patients, three FALS patients with known SOD1 mutations (FALS-1), one autosomal-dominant FALS patient with no identifiable SOD1 mutations (FALS-O), and 11 sporadic ALS (SALS) patients. Also, we determined the activities of components of the electron transport chain (complexes I, II-III, and IV) in these samples. The cytosolic SOD activity, which is primarily SOD1 activity, was reduced by 38.8% (p < 0.05) in the FALS-1 patients and not significantly altered in the SALS patients or the FALS-O patient relative to the control patients. The mitochondrial SOD activity, which is primarily SOD2 activity, was not significantly altered in the FALS-1, FALS-O, or SALS patients. The protein carbonyl content was elevated by 84.8% (p < 0.01) in the SALS patients relative to the control patients. Finally, the complex I activity was increased by 55.3% (p < 0.001) in the FALS-1 patients relative to the control patients. These results from cortical tissue demonstrate that SOD1 activity is reduced and complex I activity is increased in FALS-1 patients and that oxidative damage to proteins is increased in SALS patients.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
61
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2322-5
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8245985-Adult,
pubmed-meshheading:8245985-Amyotrophic Lateral Sclerosis,
pubmed-meshheading:8245985-Autopsy,
pubmed-meshheading:8245985-Brain,
pubmed-meshheading:8245985-Citrate (si)-Synthase,
pubmed-meshheading:8245985-Electron Transport,
pubmed-meshheading:8245985-Energy Metabolism,
pubmed-meshheading:8245985-Family,
pubmed-meshheading:8245985-Female,
pubmed-meshheading:8245985-Genes, Dominant,
pubmed-meshheading:8245985-Humans,
pubmed-meshheading:8245985-Male,
pubmed-meshheading:8245985-Middle Aged,
pubmed-meshheading:8245985-Mitochondria,
pubmed-meshheading:8245985-Mutation,
pubmed-meshheading:8245985-Oxidative Phosphorylation,
pubmed-meshheading:8245985-Reference Values,
pubmed-meshheading:8245985-Superoxide Dismutase
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis.
|
| pubmed:affiliation |
Neurochemistry Laboratory, Massachusetts General Hospital, Boston 02114.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|