IgG4 glycosylation contributes to the pathogenesis of IgG4 Hashimoto's thyroiditis via the complement pathway.

ABSTRACT:

Background

To explore whether IgG4 is involved in the pathogenesis of IgG4 HT.

Methods

Serum TgAb IgG4 and TPOAb IgG4 were measured in IgG4 HT and non-IgG4 HT. C1q, mannose-binding lectin (MBL), Bb, C3d, C4d, and membrane attack complex (MAC) in thyroid tissues from IgG4 HT, non-IgG4 HT, and controls were examined by immunohistochemistry. We assessed IgG4 and MAC deposition in mouse thyroid by immunohistochemistry after injecting purified IgG4 into mice. The glycosylation patterns of TgAb IgG4 from IgG4 HT were identified by MALDI-TOF-MS. The ability of IgG4 to bind to MBL before and after deglycosylation was assessed by ELISA. MBL and MAC fluorescence were detected in thyrocytes after the addition of IgG4 or deglycosylated IgG4.

Results

Serum TgAb IgG4 and TPOAb IgG4

SUBMITTER: Zhao C 

PROVIDER: S-EPMC11558973 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature