Abstract:
:A soluble form of the amino-terminal extracellular (ecto-) domain of the human TSH receptor was generated. This protein was capable of binding TSH and autoimmune antibodies found in Graves' patients. A deletion mutant of the ectodomain lacking nine amino acids in the C-terminal region lost its ability to interact with TSH but retained binding to Graves' IgGs. In cells expressing recombinant TSH receptors, cotreatment with the mutant protein blocked the cAMP production induced by stimulating antibodies from all Graves' patients tested but was without effect on TSH action. The ability to dissociate the actions of TSH and Graves' IgGs provides a tool with which to study the mechanisms underlying Graves' disease and the possibility of neutralizing the undesirable effects of thyroid-stimulating antibodies without altering the normal responses to TSH.
journal_name
Endocrinologyjournal_title
Endocrinologyauthors
Osuga Y,Liang SG,Dallas JS,Wang C,Hsueh AJdoi
10.1210/endo.139.2.5748subject
Has Abstractpub_date
1998-02-01 00:00:00pages
671-6issue
2eissn
0013-7227issn
1945-7170journal_volume
139pub_type
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