Source:http://linkedlifedata.com/resource/pubmed/id/14680977
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2003-12-18
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| pubmed:abstractText |
Fabry disease, an X-linked recessive lysosomal storage disease, results from the deficient activity of the exogalactosidase, alpha-galactosidase A (alpha-Gal A). To date, over 270 disease-causing mutations have been identified; however, no coding sequence variants have been reported. In the course of enzyme diagnostic testing, a normal female control had low plasma and leukocyte alpha-Gal A activities. Sequencing her alpha-Gal A gene revealed the D313Y substitution (GAT to TAT at cDNA nucleotide 937). alpha-Gal A mutation and enzyme analyses of family members revealed X-linked transmission and leukocyte alpha-Gal A enzymatic activities in females, consistent with Lyonization. Since D313Y was reported in a classically affected male who had the double mutation, D313Y and G411D, efforts were undertaken to characterize these lesions. Expression of D313Y, G411D, and the doubly mutated construct, D313Y/G411D, resulted in alpha-Gal A levels of 76, 2.9, and 1.7% of mean expressed wild-type activity, respectively. Biosynthetic studies revealed essentially normal processing of the D313Y subunit, but the absence of the mature subunit encoded by the G411D and D313Y/G411D constructs. Thus, G411D is the disease-causing mutation, while D313Y is the first coding sequence variant identified in the human alpha-Gal A gene.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
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| pubmed:issn |
1096-7192
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
80
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
307-14
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14680977-Adult,
pubmed-meshheading:14680977-Animals,
pubmed-meshheading:14680977-Blotting, Southern,
pubmed-meshheading:14680977-COS Cells,
pubmed-meshheading:14680977-Cercopithecus aethiops,
pubmed-meshheading:14680977-DNA Primers,
pubmed-meshheading:14680977-Dosage Compensation, Genetic,
pubmed-meshheading:14680977-Fabry Disease,
pubmed-meshheading:14680977-Female,
pubmed-meshheading:14680977-Gene Expression,
pubmed-meshheading:14680977-Glycosphingolipids,
pubmed-meshheading:14680977-Haplotypes,
pubmed-meshheading:14680977-Humans,
pubmed-meshheading:14680977-Male,
pubmed-meshheading:14680977-Middle Aged,
pubmed-meshheading:14680977-Mutagenesis, Site-Directed,
pubmed-meshheading:14680977-Mutation, Missense,
pubmed-meshheading:14680977-Pedigree,
pubmed-meshheading:14680977-Precipitin Tests,
pubmed-meshheading:14680977-Sequence Analysis, DNA,
pubmed-meshheading:14680977-Transfection,
pubmed-meshheading:14680977-alpha-Galactosidase
|
| pubmed:year |
2003
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| pubmed:articleTitle |
Fabry disease: D313Y is an alpha-galactosidase A sequence variant that causes pseudodeficient activity in plasma.
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| pubmed:affiliation |
Laboratoire de Biochimie Pédiatrique, Hôpital Debrousse, Lyon, France.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|