Possible difference in glycosylation of the thyrotropin receptor among species.
Residue 113 of the thyrotropin receptor (TSHR) is a possible asparagine-linked glycosylation site in the human TSHR, but not in rat or dog TSHR. Russo et al. (Mol Endocrinol 5:29-33) reported that mutation of this residue in the human TSHR diminished TSH binding activity after transfection. To investigate the difference in the role of residue 113 of the TSHR among species, we created a mutant at residue 113 in the rat TSHR, transfected Cos-7 cells with the mutant DNA and measured TSH binding and TSH- and Graves' IgG-stimulated cAMP and phosphoinositide signals. No difference was found in the activities of the mutant transfectant from the wild type receptor transfectant. These results might suggest a real difference in glycosylation of the TSHR among species.
Kosugi
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S
Department of Laboratory Medicine, Kyoto University School of Medicine, Japan.
Akamizu
T
T
Mori
T
T
D000818:Animals; D004285:Dogs; D006031:Glycosylation; D006111:Graves Disease / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D051379:Mice; D016297:Mutagenesis, Site-Directed; D051381:Rats; D011989:Receptors, Thyrotropin / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012756:Sheep; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013552:Swine; D013972:Thyrotropin / Q000378:metabolism
D008562:Membrane Glycoproteins; D011989:Receptors, Thyrotropin; D011994:Recombinant Proteins; D013972:Thyrotropin