Linked Life Data

2337120

Source:http://linkedlifedata.com/resource/pubmed/id/2337120

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-6-12
pubmed:abstractText
The possible heterogeneity of TSH receptor antibodies in Graves' disease (GD) and Hashimoto's thyroiditis (HT) with respect to the binding site on the receptor and corresponding biological effect was studied. Employing an immunoprecipitation assay (IPA), the sera of 80% of the patients with GD (24 out of 30) and 76% of the patients with HT (16 out of 21) contained TSH receptor-binding antibodies, compared to none of the sera from 17 normal volunteers and 8 patients with nontoxic multinodular goiter. TSH inhibited immunoprecipitation by GD and HT sera. In HT sera (n = 9), but not in GD sera (n = 5), heterogeneity of the TSH-induced inhibition was observed. Four HT sera showed complete inhibition of immunoprecipitation at a saturating concentration (19.8 nM) of TSH. Five HT sera, like the 5 GD sera, showed partial inhibition of immunoprecipitation by 19.8 nM TSH. Thyroid stimulating immunoglobulins (TSI) were found in four of the five GD sera and in only one of the nine HT sera. The results suggest that different subpopulations of TSH receptor antibodies, characterized by other receptor binding sites or different affinities, are associated with autoimmune thyroid disease.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0002-9629
pubmed:author
pubmed:issnType
Print
pubmed:volume
299
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
291-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Heterogeneity of TSH receptor-binding antibodies in Hashimoto's thyroiditis and Graves' disease.
pubmed:affiliation
Department of Medicine, University of Massachusetts Medical Center, Worcester 01655.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.