免疫球蛋白G糖基化的表观遗传学。

Q2 Medicine
Marija Klasić, Vlatka Zoldoš
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引用次数: 3

摘要

免疫球蛋白G (IgG)的选择性糖基化影响其在免疫应答中的效应功能。IgG糖基化在许多疾病中发生改变,但在个体的健康生活中也会发生改变。目前,对健康状态下改变IgG糖基化的因素以及与病理生理相关的特异性IgG糖基化模式相关的因素的了解有限。遗传背景起着重要作用,但表观遗传机制也有助于健康生活和疾病中IgG糖基化模式的改变。众所周知,许多糖基转移酶的表达受DNA甲基化和microRNA (miRNA)分子的调节,但其他表观遗传机制,如组蛋白修饰,在糖基化相关基因(糖基因)的调节中的作用仍然知之甚少。最近的研究已经确定了几个与IgG糖基化相关的差异甲基化位点,但涉及特异性IgG糖基化模式形成的机制仍然知之甚少。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Epigenetics of Immunoglobulin G Glycosylation.

Alternative glycosylation of immunoglobulin G (IgG) affects its effector functions during the immune response. IgG glycosylation is altered in many diseases, but also during a healthy life of an individual. Currently, there is limited knowledge of factors that alter IgG glycosylation in the healthy state and factors involved in specific IgG glycosylation patterns associated with pathophysiology. Genetic background plays an important role, but epigenetic mechanisms also contribute to the alteration of IgG glycosylation patterns in healthy life and in disease. It is known that the expression of many glycosyltransferases is regulated by DNA methylation and by microRNA (miRNA) molecules, but the involvement of other epigenetic mechanisms, such as histone modifications, in the regulation of glycosylation-related genes (glycogenes) is still poorly understood. Recent studies have identified several differentially methylated loci associated with IgG glycosylation, but the mechanisms involved in the formation of specific IgG glycosylation patterns remain poorly understood.

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来源期刊
Experientia supplementum (2012)
Experientia supplementum (2012) Medicine-Medicine (all)
CiteScore
3.30
自引率
0.00%
发文量
24
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