Glycoconj J-IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease

      2013年6月20日，SCI期刊Glycoconj J杂志（SCI 1.882）在线发表了医科院动研所病毒室薛婧博士撰写的论文，题目为“IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease.”。

全文网址：http://link.springer.com/content/pdf/10.1007%2Fs10719-013-9481-y.pdf

英文摘要：

      Glycoconj J. 2013 Nov;30(8):735-745. Epub 2013 Jun 20.

IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease.

Xue J, Zhu LP, Wei Q.

Source

      Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences (CAMS) and Comparative Medicine Center, Peking Union Medical College (PUMC), Key Laboratory of Human Disease Comparative Medicine, No 5 Panjiayuan Nanli, Chaoyang District, Beijing, 100021, China.

Abstract

      Immunoglobulins (Igs) are the major molecules secreted by B lymphocytes during an adaptive immune response. They are glycoproteins with distinctive glycosylation patterns, resulting in wide variations in the number, type and location of their oligosaccharides in each isotype and subclass. The sugars play specific structural roles, maintaining and modulating effector functions of Igs. Aberrant glycosylation might contribute to disease pathogenesis. This review will focus on the glycosylation of IgG and IgA because they have been studied more extensively than other immunoglobulins. Rheumatoid arthritis and IgA nephritis are used to describe the association of glycosylation aberration and disease pathogenesis.