Structure and biological roles of mucin-type O-glycans at the ocular surface.

Structure and biological roles of mucin-type O-glycans at the ocular surface.
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DOI:
10.1016/s1542-0124(12)70213-6
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发表时间:
2010-01
期刊:
影响因子:
6.4
通讯作者:
Argueeso, Pablo
Argueeso, Pablo
中科院分区:
医学2区
文献类型:
--
作者:
Guzman-Aranguez, Ana;Argueeso, Pablo

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黏液蛋白是湿表面上皮中黏液分泌物和顶端细胞膜的主要成分。在结构上,它们的特点是存在含有大量o糖基化丝氨酸和苏氨酸残基的串联重复结构域。o -聚糖有助于维持粘蛋白的高度延伸和刚性结构,赋予其特定的物理和生物特性,以实现其保护功能。在眼表上皮,黏液型o -聚糖链很短,主要是唾液化的,这可能反映了眼表的特殊需求。传统上,泪膜中分泌的粘蛋白及其o -聚糖参与清除眼表面的碎片和病原体。然而,新的证据表明,细胞表面糖萼上的o -聚糖在保护角膜和结膜上皮方面具有额外的生物学作用,如防止细菌粘附,促进边界润滑,并通过与半乳糖凝集素-3的相互作用维持上皮屏障功能。粘蛋白型o -糖基化异常在许多眼表稳定性受损的疾病中被发现。本文综述了近年来在眼表黏液型o -聚糖的结构、生物合成和功能及其在眼表疾病中的变化方面的研究进展。
Mucins are major components in mucus secretions and apical cell membranes on wet-surfaced epithelia. Structurally, they are characterized by the presence of tandem repeat domains containing heavily O-glycosylated serine and threonine residues. O-glycans contribute to maintaining the highly extended and rigid structure of mucins, conferring to them specific physical and biological properties essential for their protective functions. At the ocular surface epithelia, mucin-type O-glycan chains are short and predominantly sialylated, perhaps reflecting specific requirements of the ocular surface. Traditionally, secreted mucins and their O-glycans in the tear film have been involved in the clearance of debris and pathogens from the surface of the eye. New evidence, however, shows that O-glycans on the cell-surface glycocalyx have additional biological roles in the protection of corneal and conjunctival epithelia, such as preventing bacterial adhesion, promoting boundary lubrication, and maintaining the epithelial barrier function through their interaction with galectin-3. Abnormalities in mucin-type O-glycosylation have been identified in many disorders where the stability of the ocular surface is compromised. This review summarizes recent advances in understanding the structure, biosynthesis, and function of mucin-type O-glycans at the ocular surface and their alteration in ocular surface disease.
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