Thyrotropin Receptor Structure—In the Crystal New Horizons Shine

The thyrotropin receptor (TSHR) expressed on the surface of the thyrocytes plays a key role in thyroid physiology and is also an important autoantibody target in patients with thyroid autoimmunity. Just over 50 years ago in 1956, Adams and Purves made their milestone observation that the immunoglobu...

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Bibliographic Details
Published in:Endocrine practice Vol. 15; no. 1; pp. 56 - 60
Main Authors: Furmaniak, Jadwiga, Sanders, Jane, Smith, Bernard Rees
Format: Journal Article
Language:English
Published: United States Elsevier Limited 01.01.2009
Subjects:
Animals
Antibodies, Monoclonal - metabolism
Antibodies, Monoclonal - pharmacology
Antibodies, Monoclonal - therapeutic use
Disease Models, Animal
Graves Disease - drug therapy
Humans
Protein Binding
Receptors, Thyrotropin - chemistry
Receptors, Thyrotropin - drug effects
Receptors, Thyrotropin - metabolism
Thyroiditis, Autoimmune - drug therapy
Thyrotropin - metabolism
ISSN:1530-891X, 1934-2403, 1934-2403
Online Access:Get full text
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Summary:The thyrotropin receptor (TSHR) expressed on the surface of the thyrocytes plays a key role in thyroid physiology and is also an important autoantibody target in patients with thyroid autoimmunity. Just over 50 years ago in 1956, Adams and Purves made their milestone observation that the immunoglobulins from patients with Graves disease had the ability to stimulate the thyroid. Cloning of the TSHR complementary DNA sequence in 1989 was the next key development, which had considerable effect on studies of the TSHR. In particular, recombinant TSHRs could be expressed in different systems. The ability to produce recombinant TSHR enabled the development of animal antibodies to the TSHR that proved to be valuable tools for studying the structure and function of the receptor. After many years of efforts, the goal that was deemed by some as impossible was achieved when mouse and hamster thyroid-stimulating antibodies were produced.
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ISSN:1530-891X
1934-2403
1934-2403
DOI:10.4158/EP.15.1.56