HUMAN AUTOANTIBODIES TO THE THYROTROPIN RECEPTOR - RECOGNITION OF LINEAR, FOLDED, AND GLYCOSYLATED RECOMBINANT EXTRACELLULAR DOMAIN

Authors
VLASE H GRAVES PN MAGNUSSON RP DAVIES TF
Citation
H. Vlase et al., HUMAN AUTOANTIBODIES TO THE THYROTROPIN RECEPTOR - RECOGNITION OF LINEAR, FOLDED, AND GLYCOSYLATED RECOMBINANT EXTRACELLULAR DOMAIN, The Journal of clinical endocrinology and metabolism, 80(1), 1995, pp. 46-53
Citations number
23
Categorie Soggetti
Endocrynology & Metabolism
Journal title
The Journal of clinical endocrinology and metabolism → ACNP
ISSN journal
0021972X
Volume
80
Issue
1
Year of publication
1995
Pages
46 - 53
Database
ISI
SICI code
0021-972X(1995)80:1<46:HATTTR>2.0.ZU;2-N
Abstract
To examine the heterogeneity of autoantibodies to the human TSH recept or (hTSHR), we evaluated 20 sera from patients with Graves' disease fo r their recognition of prokaryotic (unglycosylated) and eukaryotic (in sect cell glycosylated) recombinant hTSHR extracellular domain (ecd) i n an unfolded (linear) and a folded (nonlinear) state. With the prokar yotic antigen, 12 (60%) bound folded hTSHR ecd monomer, 8 (40%) bound to the unfolded monomer, and 3 (15%) bound to a tetrameric species. Su ch binding to different hTSHR antigens was not mutually exclusive. In addition, 7 (35%) sera showed an apparently higher reactivity for the folded than the unfolded monomer.