What question did this study set out to answer?

To determine whether thyroid hormone autoantibodies from Graves' disease patients and a cross-reactive murine monoclonal antibody recognize specific hormonogenic peptide sequences of human thyroglobulin.

January 1, 1993Endocrine JournalOpen Access

Immune Recognition of Hormonogenic Sites of Human Thyroglobulin: Studies of Graves' Sera and A Murine Monoclonal Antibody with Thyroid Hormone Antibody Activity.

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Authors

SSShigeki SakataMayo Clinic MMMasafumi MatsudaInstitute for Advanced Study HTHiroshi TakunoKihoku hospital

Discussion

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Overview

In vitro study reveals distinct epitope binding between monoclonal antibodies and Graves' autoantibodies, indicating iodine dependence in human thyroid autoimmunity.

Key Points

To determine whether thyroid hormone autoantibodies from Graves' disease patients and a cross-reactive murine monoclonal antibody recognize specific hormonogenic peptide sequences of human thyroglobulin.
Synthesized six peptides (HTg-1 to HTg-6) corresponding to hormonogenic regions of human thyroglobulin with or without hormonogenic acceptor tyrosine residues, labeled with 127I or 125I.
Tested peptides for direct binding and competitive displacement of 125I-T4 binding to autoantibodies from two patients with Graves' disease and an anti-thyroglobulin murine monoclonal antibody.
Assessed displacement of 125I-T4 binding using normal human thyroglobulin versus iodine-poor thyroglobulin derived from a Hürthle cell adenoma.
None of the synthetic iodinated peptides displaced 125I-T4 binding to thyroid hormone autoantibodies or the monoclonal antibody, nor did they show direct binding.
Normal thyroglobulin completely displaced 125I-T4 binding in patient serum, whereas iodine-deficient thyroglobulin displaced 125I-T4 binding by only 2% in Case 1 and 5% in Case 2.
Monoclonal antibody binding to 125I-T4 was displaced equally by both normal and iodine-deficient thyroglobulin.

Cite This Study

Sakata et al. (1993) studied this question.

synapsesocial.com/papers/6a87a90e6239aa4041f2fecd https://doi.org/10.1507/endocrj.40.393

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January 1, 1993Endocrine JournalOpen Access

Immune Recognition of Hormonogenic Sites of Human Thyroglobulin: Studies of Graves' Sera and A Murine Monoclonal Antibody with Thyroid Hormone Antibody Activity.

View Full Paper

Ask AI

Bookmark

Authors

SSShigeki SakataMayo Clinic MMMasafumi MatsudaInstitute for Advanced Study HTHiroshi TakunoKihoku hospital

Discussion

Member takes

Overview

In vitro study reveals distinct epitope binding between monoclonal antibodies and Graves' autoantibodies, indicating iodine dependence in human thyroid autoimmunity.

Key Points

To determine whether thyroid hormone autoantibodies from Graves' disease patients and a cross-reactive murine monoclonal antibody recognize specific hormonogenic peptide sequences of human thyroglobulin.
Synthesized six peptides (HTg-1 to HTg-6) corresponding to hormonogenic regions of human thyroglobulin with or without hormonogenic acceptor tyrosine residues, labeled with 127I or 125I.
Tested peptides for direct binding and competitive displacement of 125I-T4 binding to autoantibodies from two patients with Graves' disease and an anti-thyroglobulin murine monoclonal antibody.
Assessed displacement of 125I-T4 binding using normal human thyroglobulin versus iodine-poor thyroglobulin derived from a Hürthle cell adenoma.
None of the synthetic iodinated peptides displaced 125I-T4 binding to thyroid hormone autoantibodies or the monoclonal antibody, nor did they show direct binding.
Normal thyroglobulin completely displaced 125I-T4 binding in patient serum, whereas iodine-deficient thyroglobulin displaced 125I-T4 binding by only 2% in Case 1 and 5% in Case 2.
Monoclonal antibody binding to 125I-T4 was displaced equally by both normal and iodine-deficient thyroglobulin.

Cite This Study

Sakata et al. (1993) studied this question.

synapsesocial.com/papers/6a87a90e6239aa4041f2fecd https://doi.org/10.1507/endocrj.40.393

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