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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1994-7-28
|
| pubmed:databankReference | |
| pubmed:abstractText |
Electron transfer flavoprotein (ETF) is a heterodimeric enzyme composed of an alpha-subunit and a beta-subunit and contains a single equivalent of FAD per dimer. ETF deficiency can be demonstrated in individuals affected by a severe metabolic disorder, glutaric acidemia type II (GAII). In this study, we have investigated for the first time the molecular basis of beta-ETF deficiency in three GAII patients: two Japanese brothers, P411 and P412, and a third unrelated patient, P485. Molecular analysis of the beta-ETF gene in P411 and P412 demonstrated that both these patients are compound heterozygotes. One allele is carrying a G to A transition at nucleotide 518, causing a missense mutation at codon 164. This point mutation is maternally derived and is not detected in 42 unrelated controls. The other allele carries a G to C transversion at the first nucleotide of the intron donor site, downstream of an exon that is skipped during the splicing event. The sequence analysis of the beta-ETF coding sequence in P485 showed only a C to T transition at nucleotide 488 that causes a Thr154 to Met substitution and the elimination of a HgaI restriction site. HgaI restriction analysis on 63 unrelated controls' genomic DNA demonstrated that the C488T transition identifies a polymorphic site. Finally, transfection of wild-type beta-ETF cDNA into P411 fibroblasts suggests that wild-type beta-ETF cDNA complements the genetic defect and restores the beta-oxidation flux to normal levels.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CTGCAG-specific type II...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA modification methylase HgaI,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Cytosine Methylases,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, Type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Electron-Transferring Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutarates,
http://linkedlifedata.com/resource/pubmed/chemical/glutaric acid
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0964-6906
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
429-35
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:7912128-Amino Acid Metabolism, Inborn Errors,
pubmed-meshheading:7912128-Base Sequence,
pubmed-meshheading:7912128-Blotting, Western,
pubmed-meshheading:7912128-Cells, Cultured,
pubmed-meshheading:7912128-DNA,
pubmed-meshheading:7912128-DNA-Cytosine Methylases,
pubmed-meshheading:7912128-Deoxyribonucleases, Type II Site-Specific,
pubmed-meshheading:7912128-Electron-Transferring Flavoproteins,
pubmed-meshheading:7912128-Fibroblasts,
pubmed-meshheading:7912128-Flavoproteins,
pubmed-meshheading:7912128-Glutarates,
pubmed-meshheading:7912128-Humans,
pubmed-meshheading:7912128-Molecular Sequence Data,
pubmed-meshheading:7912128-Mutation,
pubmed-meshheading:7912128-Oxidation-Reduction,
pubmed-meshheading:7912128-Polymerase Chain Reaction,
pubmed-meshheading:7912128-Polymorphism, Restriction Fragment Length,
pubmed-meshheading:7912128-Sequence Deletion,
pubmed-meshheading:7912128-Transfection
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Mutations and polymorphisms of the gene encoding the beta-subunit of the electron transfer flavoprotein in three patients with glutaric acidemia type II.
|
| pubmed:affiliation |
Istituto di Fisiologia Generale e Chimica Biologica, Facoltà di Farmacia, Università degli Studi di Milano, Italy.
|
| pubmed:publicationType |
Journal Article
|