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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0003241,
umls-concept:C0003316,
umls-concept:C0019409,
umls-concept:C0030705,
umls-concept:C0030956,
umls-concept:C0034844,
umls-concept:C0040139,
umls-concept:C0085862,
umls-concept:C0150312,
umls-concept:C0185125,
umls-concept:C0205147,
umls-concept:C0229671,
umls-concept:C0237401,
umls-concept:C0332120,
umls-concept:C0524637,
umls-concept:C0567416,
umls-concept:C1299583,
umls-concept:C1529966,
umls-concept:C1549571,
umls-concept:C1608386,
umls-concept:C1883254
|
| pubmed:issue |
3
|
| pubmed:dateCreated |
1995-11-30
|
| pubmed:abstractText |
To define the epitope(s) of stimulating thyrotropin receptor antibody (TSH-R-Sab), we synthesized 19 oligopeptides covering almost all amino acids of the extracellular domain of the human TSH-R and studied these effects on the inhibition of one TSH-R-Sab activity. Four of the 19 peptides encompassing residues 31-50 (P31-20), 91-119 (P91-29), 287-304 (P287-18) and 354-367 (P354-14) were found to show significant TSH-R-Sab inhibition and to have similar effects on the other three Graves' immunoglobulins. When these peptides were applied in combination with P354-14 only P287-18 revealed additional effects but the other two combinations did not. Furthermore, sequential addition of these peptide pairs confirmed the additional effects of P287-18 and P354-14. Sequential peptide-affinity gel studies were then performed. Most of the TSH-R-Sab activity in the unabsorbed fraction from P287-18 gel was absorbed to a subsequent P354-14 gel and the eluted fraction from P287-18 mostly remained unabsorbed by the P354-14 gel. On the other hand, most of the unabsorbed fraction from P91-29 gel remained unabsorbed even by the subsequent P354-14 gel. When a P354-14 affinity gel-purified TSH-R-Sab immunoglobulin was labeled and evaluated for its binding to FRTL-5 cells, additions of original immunoglobulin, P354-14 and P91-29 resulted in significant inhibition of the binding but P287-18 did not affect either. From these results, it was concluded that most of the individual Graves' immunoglobulins contain at least two heterogeneous moieties with TSH-R-Sab activity, one of which binds P354-14 and the other binds P287-18. Further, P354-14 and P91-29 were indicated to bind the same molecule of TSH-R-Sab immunoglobulin.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0804-4643
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
133
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
283-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7581943-Absorption,
pubmed-meshheading:7581943-Amino Acid Sequence,
pubmed-meshheading:7581943-Animals,
pubmed-meshheading:7581943-Antibody Specificity,
pubmed-meshheading:7581943-Cell Line,
pubmed-meshheading:7581943-Chromatography, Affinity,
pubmed-meshheading:7581943-Epitopes,
pubmed-meshheading:7581943-Graves Disease,
pubmed-meshheading:7581943-Humans,
pubmed-meshheading:7581943-Immunoglobulins, Thyroid-Stimulating,
pubmed-meshheading:7581943-Molecular Sequence Data,
pubmed-meshheading:7581943-Peptide Fragments,
pubmed-meshheading:7581943-Rats,
pubmed-meshheading:7581943-Receptors, Thyrotropin,
pubmed-meshheading:7581943-Thyroid Gland
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Presence of heterogeneous thyroid-stimulating antibodies in sera from individual Graves' patients as shown by synthesized thyrotropin receptor peptide application: evidence showing two independent epitopes and a possible recognition of two epitopic regions by one antibody molecule.
|
| pubmed:affiliation |
Department of Laboratory Medicine, Kyoto University, School of Medicine, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|