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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1985-8-30
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pubmed:abstractText |
The microsomal/microvillar antigen of the human thyroid gland which provokes thyroid autoimmunity was characterised by immunoprecipitation studies. Sera from patients with Hashimoto's thyroiditis, primary myxoedema or Graves' disease containing autoanti-microsomal antibody specifically precipitated a component, which under reducing conditions migrates with a mol. wt of 105,000 on SDS-polyacrylamide gel electrophoresis. This protein was absent in auto- or xeno-anti-thyroglobulin precipitates, which under reducing conditions display four polypeptides of Mr 260,000, 230,000, 180,000 and 142,000. Under non-reducing conditions, the microsomal/microvillar antigen displayed a small shift in mobility to a mol. wt of 117,000 suggesting the presence of intrachain disulphide bonds. In contrast, under these conditions, anti-thyroglobulin precipitated components displaying polypeptides of approx. mol. wts in the region of 240,000-260,000, 170,000-180,000 and 140,000. Absorption of thyroiditis sera on thyroglobulin-Sepharose followed by immunoprecipitation abolished the anti-thyroglobulin components without affecting the binding of the 105,000-dalton polypeptide, if the sera contained antimicrosomal antibody. No comparable material was identified in microsomal membrane preparations prepared from the stomach which is also commonly involved in organ-specific autoimmunity. The 105,000-dalton component does not bind to a Lens culinaris lectin affinity column. We conclude that the epitopes of the microsomal/microvillar antigen are presented on a poorly glycosylated peptide of mol. wt 105,000, which is probably stabilised by intrachain disulphide bonds and which does not share serological reactivity with membrane-bound thyroglobulin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
629-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:4022016-Antigens,
pubmed-meshheading:4022016-Autoantigens,
pubmed-meshheading:4022016-Autoimmune Diseases,
pubmed-meshheading:4022016-Chromatography, Affinity,
pubmed-meshheading:4022016-Chromatography, High Pressure Liquid,
pubmed-meshheading:4022016-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:4022016-Humans,
pubmed-meshheading:4022016-Intracellular Membranes,
pubmed-meshheading:4022016-Membrane Proteins,
pubmed-meshheading:4022016-Microsomes,
pubmed-meshheading:4022016-Microvilli,
pubmed-meshheading:4022016-Molecular Weight,
pubmed-meshheading:4022016-Organ Specificity,
pubmed-meshheading:4022016-Radioimmunoassay,
pubmed-meshheading:4022016-Thyroglobulin,
pubmed-meshheading:4022016-Thyroid Diseases,
pubmed-meshheading:4022016-Thyroid Gland
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pubmed:year |
1985
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pubmed:articleTitle |
Structural features of the autoantigens involved in thyroid autoimmune disease: the thyroid microsomal/microvillar antigen.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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