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

被引：45

作者：

VLASE, H

GRAVES, PN

MAGNUSSON, RP

DAVIES, TF

机构：

[1] CUNY MT SINAI SCH MED, DEPT MED, DIV ENDOCRINOL & METAB, NEW YORK, NY 10029 USA

[2] CUNY MT SINAI SCH MED, DEPT PHARMACOL, NEW YORK, NY 10029 USA

来源：

JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM | 1995年 / 80卷 / 01期

关键词：

D O I：

10.1210/jc.80.1.46

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

To examine the heterogeneity of autoantibodies to the human TSH receptor (hTSHR), we evaluated 20 sera from patients with Graves' disease for their recognition of prokaryotic (unglycosylated) and eukaryotic (insect cell glycosylated) recombinant hTSHR extracellular domain (ecd) in an unfolded (linear) and a folded (nonlinear) state. With the prokaryotic antigen, 12 (60%) bound folded hTSHR ecd monomer, 8 (40%) bound to the unfolded monomer, and 3 (15%) bound to a tetrameric species. Such 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.

引用

页码：46 / 53

页数：8

共 23 条

[21] PROKARYOTIC EXPRESSION OF THE THYROTROPIN RECEPTOR AND IDENTIFICATION OF AN IMMUNOGENIC REGION OF THE PROTEIN USING SYNTHETIC PEPTIDES [J].