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  • Title: Role of the carboxyl-terminal half of the extracellular domain of the human thyrotropin receptor in signal transduction.
    Author: Nagayama Y, Rapoport B.
    Journal: Endocrinology; 1992 Aug; 131(2):548-52. PubMed ID: 1322272.
    Abstract:
    We studied the role of the carboxyl-terminus of the extracellular region of the human TSH receptor in signal transduction (cAMP generation). For this purpose, we introduced homologous substitutions of smaller segments within amino acids 261-418 (domains D and E) of the TSH receptor with the corresponding amino acids of the rat LH/CG receptor. Amino acids 317-366 were not investigated in view of previous data indicating their noninvolvement. Mutant TSH receptor cDNAs, in a eukaryotic expression vector, were stably transfected into Chinese hamster ovary cells. Eight of nine plasmid constructs expressed TSH receptors that could be detected by radiolabeled TSH binding; six of these were of high affinity similar to the wild-type receptor and, therefore, provided informative data on signal transduction. Despite high affinity TSH binding, five of six TSH receptor mutants displayed a diminished cAMP response to TSH stimulation, suggesting the involvement of broad segments of domains DE in signal transduction. Amino acids 270-278 and 287-297 were particularly important in this respect. The conformation conferred by these segments of the TSH receptor, therefore, appears to be involved in transducing a signal from the extracellular to the intracellular region of the receptor.
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