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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2003-10-14
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pubmed:abstractText |
Disease-specific epitope profiles of glutamic acid decarboxylase (GAD)65 autoantibodies (GAD65Ab) were studied in slowly progressive type 1 (insulin-dependent) diabetes mellitus (SPIDDM) and acute onset type 1 (insulin-dependent) diabetes mellitus (AIDDM) using seven kinds of GAD65/67 chimeric molecules. Sera obtained from Japanese SPIDDM (n = 17) and AIDDM (n = 46) patients followed prospectively were analyzed by immunoprecipitation, ELISA, and Western blotting. GAD65Ab in all SPIDDM samples reacted specifically with an N-terminal linear epitope located on the membrane anchoring domain between amino acids 17-51 and C-terminal conformational epitope between amino acids 443-585 of GAD65. The binding of GAD65Ab with N-terminal 83 residues in SPIDDM inversely correlated with the period in which insulin was not required. GAD65Ab in AIDDM did not react with N-terminal epitope located between amino acids 1-83, irrespective of the titer of GAD65Ab. A novel epitope of GAD65Ab in AIDDM residing between amino acids 244-360 was identified in 17% (8 of 46) of patients whose age of onset was younger than other AIDDM patients. In conclusion, GADAb in SPIDDM has unique N-terminal linear epitopes that are located on the anchoring domain of GAD65 molecules. Association is suggested between GAD65Ab targeted to this region and slowly progressive beta-cell failure in SPIDDM.
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pubmed:language |
eng
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pubmed:journal |
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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/HLA-DQ Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQ alpha-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQ beta-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQA1 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DQB1 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoglycemic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate decarboxylase 1,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate decarboxylase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-972X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4768-75
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:14557453-Autoantibodies,
pubmed-meshheading:14557453-Binding Sites,
pubmed-meshheading:14557453-Diabetes Mellitus, Type 1,
pubmed-meshheading:14557453-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:14557453-Epitopes,
pubmed-meshheading:14557453-Glutamate Decarboxylase,
pubmed-meshheading:14557453-HLA-DQ Antigens,
pubmed-meshheading:14557453-HLA-DQ alpha-Chains,
pubmed-meshheading:14557453-HLA-DQ beta-Chains,
pubmed-meshheading:14557453-Haplotypes,
pubmed-meshheading:14557453-Humans,
pubmed-meshheading:14557453-Hypoglycemic Agents,
pubmed-meshheading:14557453-Insulin,
pubmed-meshheading:14557453-Isoenzymes,
pubmed-meshheading:14557453-Longitudinal Studies,
pubmed-meshheading:14557453-Protein Structure, Tertiary,
pubmed-meshheading:14557453-Pyridoxal Phosphate,
pubmed-meshheading:14557453-Recombinant Fusion Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Unique epitopes of glutamic acid decarboxylase autoantibodies in slowly progressive type 1 diabetes.
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pubmed:affiliation |
Third Department of Internal Medicine, Yamanashi Medical University, Tamaho, Yamanashi 409-3898, Japan. tetsurou@yamanashi.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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