Determination of Carbohydrate-Binding Preferences of Human Galectins with Carbohydrate Microarrays
Determination of Carbohydrate-Binding Preferences of Human Galectins with Carbohydrate Microarrays
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DOI：
10.1002/cbic.201000020
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发表时间：
2010-07-26
期刊：
影响因子：
3.2
通讯作者：
Seeberger, Peter H.
中科院分区：
文献类型：
--
作者：
Horlacher, Tim;Oberli, Matthias A.;Seeberger, Peter H.
半乳糖凝集素是一类碳水化合物结合蛋白，因其对半乳糖结合的偏好而得名，并参与从生物体内平衡到免疫反应的一系列过程。作为将不同凝集素的碳水化合物结合偏好与其生物学功能相关联的第一步，我们借助碳水化合物微阵列确定了凝集素的碳水化合物识别精细特异性。通过化学合成制备了一组被认为与凝集素相关的低聚糖。确定了半乳糖凝集素-糖相互作用的结构-活性关系，通过比较结合偏好，这些关系有助于建立冗余和特异性的半乳糖凝集素作用。基本乳糖基基上不同的糖基化被证明是调节凝集素结合的关键——因此，凝集素的作用——要么产生高亲和力的配体，要么结合被阻断。高亲和力配体，如血型抗原，可能介导特定功能被确定。
Galectins are a class of carbohydrate-binding proteins named for their galactose-binding preference and are involved in a host of processes ranging from homeostasis of organisms to immune responses. As a first step towards correlating the carbohydrate-binding preferences of the different galectins with their biological functions, we determined carbohydrate recognition fine-specificities of galectins with the aid of carbohydrate microarrays. A focused set of oligosaccharides considered relevant to galectins was prepared by chemical synthesis. Structure-activity relationships for galectin-sugar interactions were determined, and these helped in the establishment of redundant and specific galectin actions by comparison of binding preferences. Distinct glycosylations on the basic lactosyl motifs proved to be key to galectin binding regulation-and therefore galectin action-as either high-affinity ligands are produced or binding is blocked. High-affinity ligands such as the blood group antigens that presumably mediate particular functions were identified.