Cummings Richard D., Chiffoleau Elise, van Kooyk Yvette, McEver Rodger P.
C-type lectins (CTLs) are Ca-dependent glycan-binding proteins (GBPs) that share primary and secondary structural homology in their carbohydrate-recognition domains (CRDs). The CRD of CTLs is more generally defined as the CTL domain (CTLD), because not all proteins with this domain bind either glycans or Ca. CTLs include collectins, selectins, endocytic receptors, and proteoglycans, some of which are secreted and others are transmembrane proteins. They often oligomerize, which increases their avidity for multivalent ligands and enhance recognition of pattern recognition receptor (PRRs). CTLs differ significantly in the types of ligands that they recognize with high affinity (e.g., glycans, proteins, lipids, and inorganic compounds). These proteins that recognize pathogens or self-expressed ligands function as adhesion, phagocytic, and signaling receptors in many pathways, including homeostasis and innate and adaptive immunity, and are crucial in inflammatory responses, leukocyte and platelet trafficking, and tissue remodeling.
C型凝集素(CTLs)是依赖钙离子的聚糖结合蛋白(GBPs),它们在碳水化合物识别结构域(CRDs)中具有一级和二级结构同源性。CTLs的CRD更普遍地被定义为CTL结构域(CTLD),因为并非所有具有该结构域的蛋白质都能结合聚糖或钙离子。CTLs包括凝集素、选择素、内吞受体和蛋白聚糖,其中一些是分泌型的,另一些是跨膜蛋白。它们常常寡聚化,这增加了它们对多价配体的亲和力,并增强了对模式识别受体(PRRs)的识别。CTLs在它们高亲和力识别的配体类型(如聚糖、蛋白质、脂质和无机化合物)上有显著差异。这些识别病原体或自身表达配体的蛋白质在许多途径中作为黏附、吞噬和信号受体发挥作用,包括体内平衡以及固有免疫和适应性免疫,并且在炎症反应、白细胞和血小板运输以及组织重塑中至关重要。