Case Western Reserve University, School of Medicine, Department of Pathology, Cleveland, OH 44106, United States.
Cell Immunol. 2018 Nov;333:58-64. doi: 10.1016/j.cellimm.2018.03.014. Epub 2018 Mar 31.
ST6Gal1 is a critical sialyltransferase enzyme that controls the addition of α2,6-linked sialic acids to the termini of glycans. Attachment of sialic acids to glycoproteins as a posttranslational modification influences cellular responses, and is a well-known modifier of immune cell behavior. ST6Gal1 activity impacts processes such as: effector functions of immunoglobulin G via Fc sialylation, hematopoietic capacity by hematopoietic stem and progenitor cell surface sialylation, and lymphocyte activation thresholds though CD22 engagement and inhibition of galectins. This review summarizes recent studies that suggest α2,6 sialylation by ST6Gal1 has an immunoregulatory effect on immune reactions.
ST6Gal1 是一种关键的唾液酸转移酶，可控制糖链末端α2,6 连接的唾液酸的添加。糖蛋白上唾液酸的附着作为一种翻译后修饰，影响细胞反应，是免疫细胞行为的已知调节剂。ST6Gal1 的活性影响以下过程：通过 Fc 唾液酸化影响免疫球蛋白 G 的效应功能，通过造血干细胞和祖细胞表面唾液酸化影响造血能力，通过 CD22 结合和半乳糖凝集素抑制影响淋巴细胞激活阈值。这篇综述总结了最近的研究，表明 ST6Gal1 的α2,6 唾液酸化对免疫反应具有免疫调节作用。
