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Title: Localization and synthesis of the hormone-binding regions of the human thyrotropin receptor

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
;  [1];  [2]
  1. Baylor Coll. of Medicine, Houston, TX (United States)
  2. Gifu Univ. School of Medicine (Japan)

Two regions of human thyrotropin (thyroid-stimulating hormone, TSH) receptor (TSHR) were selected on the basis that they exhibit no sequence resemblance to luteinizing hormone/chorionic gonadotropin receptor. Five synthetic overlapping peptides (12-30, 24-44, 308-328, 324-344, and 339-364) were studied for their ability to bind {sup 125}I-labeled human TSH (hTSH), its isolated {alpha} and {beta} subunits, bovine TSH, ovine TSH, human luteinizing hormone, and human follicle-stimulating hormone. The human TSHR peptides 12-30 and 324-344 exhibited remarkable binding activity to human, bovine, and ovine TSH and to the {beta} chain of hTSH. Lower binding activity resided in the adjacent overlapping peptides, probably due to the contribution of the shared overlap to the binding. The specificity of TSH binding to these peptides was confirmed by their inability to bind human luteinizing hormone, human follicle-stimulating hormone, and the {alpha} chain of hTSH. Thyrotropins did not bind to bovine serum albumin or to peptide controls unrelated to the TSHR system. It is concluded that the binding of TSH to its receptor involves extensive contacts and that the TSHR peptides 12-30 and 324-344 contain specific binding regions for TSH that might be either independent sites or two faces (subsites) within a large binding site.

OSTI ID:
6096348
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:9; ISSN 0027-8424
Country of Publication:
United States
Language:
English

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