Graves' IgG recognizes linear epitopes in the human thyrotropin receptor

Endre V. Nagy; Henry B. Burch; Karen Mahoney; Yvonne G. Lukes; John C. Morris; Kenneth D. Burman

doi:10.1016/0006-291X(92)92345-X

Graves' IgG recognizes linear epitopes in the human thyrotropin receptor

Endre V. Nagy, Henry B. Burch, Karen Mahoney, Yvonne G. Lukes, John C. Morris, Kenneth D. Burman

Endocrinology, Diabetes, Metabolism, and Nutrition

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

Abstract

Twenty-nine peptides covering the full extracellular domain of the human thyrotropin receptor have been synthesized and tested for reactivity with Graves' patients' and normal sera in ELISA. Two peptides, amino acids 331-350 and the second extracellular loop of the transmembrane segment, bound IgG-s from 5 and 4 of 10 Graves' disease patients' sera, respectively. Neither of these two peptides showed enhanced binding to normal IgG. There were no apparent differences between the Graves' disease and normal group with respect to the other 27 peptides. We conclude that peptide 331-350 and the second extracellular loop carry important linear epitopes which may contribute to the disease process in selected Graves' patients.

Original language	English (US)
Pages (from-to)	28-33
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	188
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(92)92345-X
State	Published - Oct 15 1992

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(92)92345-X

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title = "Graves' IgG recognizes linear epitopes in the human thyrotropin receptor",

abstract = "Twenty-nine peptides covering the full extracellular domain of the human thyrotropin receptor have been synthesized and tested for reactivity with Graves' patients' and normal sera in ELISA. Two peptides, amino acids 331-350 and the second extracellular loop of the transmembrane segment, bound IgG-s from 5 and 4 of 10 Graves' disease patients' sera, respectively. Neither of these two peptides showed enhanced binding to normal IgG. There were no apparent differences between the Graves' disease and normal group with respect to the other 27 peptides. We conclude that peptide 331-350 and the second extracellular loop carry important linear epitopes which may contribute to the disease process in selected Graves' patients.",

author = "Nagy, {Endre V.} and Burch, {Henry B.} and Karen Mahoney and Lukes, {Yvonne G.} and Morris, {John C.} and Burman, {Kenneth D.}",

note = "Funding Information: Acknowledoments The authors wish to thank Ms. Alice Jacobson for assistance in preparation of the manuscript. Dr. Nagy is the recipient of an NIH Fogarty International Research Fellowship 1 F05 TW04412-02.",

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T1 - Graves' IgG recognizes linear epitopes in the human thyrotropin receptor

AU - Nagy, Endre V.

AU - Burch, Henry B.

AU - Mahoney, Karen

AU - Lukes, Yvonne G.

AU - Morris, John C.

AU - Burman, Kenneth D.

N1 - Funding Information: Acknowledoments The authors wish to thank Ms. Alice Jacobson for assistance in preparation of the manuscript. Dr. Nagy is the recipient of an NIH Fogarty International Research Fellowship 1 F05 TW04412-02.

PY - 1992/10/15

Y1 - 1992/10/15

N2 - Twenty-nine peptides covering the full extracellular domain of the human thyrotropin receptor have been synthesized and tested for reactivity with Graves' patients' and normal sera in ELISA. Two peptides, amino acids 331-350 and the second extracellular loop of the transmembrane segment, bound IgG-s from 5 and 4 of 10 Graves' disease patients' sera, respectively. Neither of these two peptides showed enhanced binding to normal IgG. There were no apparent differences between the Graves' disease and normal group with respect to the other 27 peptides. We conclude that peptide 331-350 and the second extracellular loop carry important linear epitopes which may contribute to the disease process in selected Graves' patients.

AB - Twenty-nine peptides covering the full extracellular domain of the human thyrotropin receptor have been synthesized and tested for reactivity with Graves' patients' and normal sera in ELISA. Two peptides, amino acids 331-350 and the second extracellular loop of the transmembrane segment, bound IgG-s from 5 and 4 of 10 Graves' disease patients' sera, respectively. Neither of these two peptides showed enhanced binding to normal IgG. There were no apparent differences between the Graves' disease and normal group with respect to the other 27 peptides. We conclude that peptide 331-350 and the second extracellular loop carry important linear epitopes which may contribute to the disease process in selected Graves' patients.

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Graves' IgG recognizes linear epitopes in the human thyrotropin receptor

Abstract

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