Linked Life Data

12626432

Source:http://linkedlifedata.com/resource/pubmed/id/12626432

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2003-5-1
pubmed:abstractText
Amyotrophic lateral sclerosis (ALS) involves the progressive degeneration of motor neurons in the spinal cord and motor cortex. It has been shown that 15-20% of patients with familial ALS (FALS) have defects in the Sod1 gene that encodes Cu, Zn-superoxide dismutase (SOD). To elucidate the pathological role of mutated Cu, Zn-SODs in FALS, the susceptibility of mutants to glycation was examined. Mutated Cu, Zn-SODs (G37R, G93A, and I113T) related to FALS and wild type were produced in a baculovirus/insect cell expression system. Glycated and nonglycated proteins were separated on a boronate column, and the nonglycated fraction was then incubated with glucose. The mutated Cu, Zn-SODs were found to be highly susceptible to glycation compared with the wild-type enzyme as estimated by Western blot analysis using an anti-hexitol lysine antibody. The mutated Cu, Zn-SOD incubated with glucose generated higher levels of hydrogen peroxide than the wild-type enzyme. Mutated Cu, Zn-SODs were also shown to be highly susceptible to fructation, and the fructated mutant also produced higher levels of hydrogen peroxide than the wild type. These results suggest that high susceptibility of mutated Cu, Zn-SODs to glycation could be the origin of the oxidative stress associated with neuronal dysfunction in FALS.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1530-6860
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
938-40
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Glycation proceeds faster in mutated Cu, Zn-superoxide dismutases related to familial amyotrophic lateral sclerosis.
pubmed:affiliation
Department of Biochemistry, Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
pubmed:publicationType
Journal Article