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作 者:王巍 高春芳 Wang Wei;Gao Chunfang(Clinical Research Center for Laboratory Medicine,Yueyang Hospital of Integrated Traditional Chinese and Western Medicine,Shanghai University of Traditional Chinese Medicine,Shanghai 200437,China)
机构地区:[1]上海中医药大学附属岳阳中西医结合医院临床检验实验医学中心,上海200437
出 处:《中华检验医学杂志》2022年第4期327-331,共5页Chinese Journal of Laboratory Medicine
摘 要:糖基化修饰是免疫球蛋白G(IgG)结构和功能的一部分,唾液酸位于IgG N-糖链的最末端,通过调节IgG与可结晶片段γ受体及补体的结合而调控IgG抗炎和促炎活性,与自身免疫疾病的发生发展及转归密切相关,在疾病诊断、监测及治疗领域都显示出了巨大潜能,有望成为自身免疫疾病新型标志物和治疗靶点。Glycosylation is a part of the structure and function of immunoglobulin G(IgG).Sialic acid is located at the end of IgG N-glycan and regulates IgG anti-inflammatory and pro-inflammatory activities by changing the binding of IgG with fragment crystallizable gamma receptors(FcγRs)and complements.Low IgG sialylation is closely related to the occurrence,development and prognosis of autoimmune diseases and shows great potential in the field of diagnosis,monitoring and treatment,and may function as a new biomarker and therapeutic target for autoimmune diseases.
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