Source:http://linkedlifedata.com/resource/pubmed/id/11134126
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2001-2-2
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pubmed:abstractText |
Autoantibodies against the smaller isoform of glutamic acid decarboxylase (GAD) are markers for Type 1 diabetes. GAD65 autoantibody (GAD65Ab)-positive individuals in the general population are, however, mostly at low risk of developing Type 1 diabetes, suggesting that GAD65Ab phenotypes may be associated with different underlying pathogenic processes. The aim of this study was to test the hypothesis that Type 1 diabetes patients (n = 243; group I), GAD65Ab-positive healthy individuals (n = 28; group II), and healthy first-degree relatives of Type 1 diabetes patients (n = 41; group III) have antibody phenotypes that recognize different GAD65 epitopes. Sera from groups I-III were tested for their binding to GAD65 and GAD67, as well as six different GAD65/67 fusion proteins. Regardless of group, sera reactive to both GAD65 and GAD67 showed broader epitope reactivity than GAD65-specific sera. Furthermore, Type 1 diabetes patients showed a more restricted epitope binding than healthy individuals and first-degree relatives, demonstrating significantly less binding to the N-terminal part of GAD65 and to GAD67. Our analysis demonstrates that the N-terminal part is essential for full antibody binding to GAD65, in particular, to the middle epitope. It is suggested that Type 1 diabetes is associated with restricted GAD65Ab epitope specificity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate decarboxylase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-972X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4671-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11134126-Adolescent,
pubmed-meshheading:11134126-Adult,
pubmed-meshheading:11134126-Antibody Specificity,
pubmed-meshheading:11134126-Autoantibodies,
pubmed-meshheading:11134126-Child,
pubmed-meshheading:11134126-Child, Preschool,
pubmed-meshheading:11134126-Diabetes Mellitus, Type 1,
pubmed-meshheading:11134126-Epitopes,
pubmed-meshheading:11134126-Female,
pubmed-meshheading:11134126-Glutamate Decarboxylase,
pubmed-meshheading:11134126-Humans,
pubmed-meshheading:11134126-Infant,
pubmed-meshheading:11134126-Isoenzymes,
pubmed-meshheading:11134126-Male,
pubmed-meshheading:11134126-Phenotype,
pubmed-meshheading:11134126-Radioimmunoassay,
pubmed-meshheading:11134126-Recombinant Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Recognition of glutamic acid decarboxylase (GAD) by autoantibodies from different GAD antibody-positive phenotypes.
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pubmed:affiliation |
Department of Medicine, University of Washington, Seattle, Washington 98195, USA. champe@u.washington.edu
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pubmed:publicationType |
Journal Article,
Clinical Trial,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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