This investigation is concerned with assignments of Lewis(a) (Le(a)) and Le(x) analogs on linear and branched di- to hexasaccharide backbones as components of the recognition motifs for E-selectin. The influence of the location of fucose residue(s) was investigated using 14 structurally defined and variously fucosylated oligosaccharides in biotinylated form or as neoglycolipids in static binding assays, in microwells, and on thin-layer chromatograms. Results of the two assay systems were in agreement overall and showed that the recognition motifs for E-selectin include 4-fucosyl-lacto (Le(a)) and 3-fucosyl-neo-lacto (Le(x)) sequences strictly at capping positions and not Le(x) at an internal position as a part of VIM-2 antigen sequence. There is greater potency of the Le(a) over the Le(x) series. Additional fucose residues alpha1-2-linked to neighboring galactoses or alpha1-3-linked to inner N-acetyglucosamines or to reducing-terminal glucose residues of the tetrasaccharide backbone had little or no effect on the selectin binding. E-selectin binding to the Le(a) or Le(x )capping motif on a 3-linked branch was equivalent to the binding on the corresponding linear backbone. A lack of E-selectin binding to the Le(x) motif capping a 6-linked branch and to the Le(x) trisaccharide linked to biotin via a nine-carbon spacer indicates that the -GlcNAcbeta1-3Gal- sequence on the oligosaccharide backbone adjoining the Le(x) is a part of recognition motif for E-selectin. These findings contribute to understanding the molecular basis of E-selectin recognition and could influence future designs of selectin antagonists as possible therapeutic substances.

中文翻译：

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E-选择素与血型家族岩藻寡糖相互作用的研究。

这项研究与线性和支链二糖至六糖骨架上的Lewis（a）（Le（a））和Le（x）类似物的分配有关，作为E-选择素识别基序的组成部分。在生物结合中，在微孔中以及在薄层色谱图上，使用14种生物素化形式或作为新糖脂的结构上定义的和各种岩藻糖基化的寡糖，研究了岩藻糖残基位置的影响。两种测定系统的结果总体一致，表明E-选择素的识别基序包括严格在加帽时的4-岩藻糖基内酯（Le（a））和3-岩藻糖基-新内酯（Le（x））序列。内部位置而不是Le（x）作为VIM-2抗原序列的一部分。Le（a）的强度比Le（x）级数更大。与相邻的半乳糖连接的其他岩藻糖残基或与内部N-乙酰氨基葡糖或四糖骨架的还原末端葡萄糖残基的alpha1-2连接的对选择素结合的影响很小或没有影响。E-选择蛋白结合到3-连接的分支上的Le（a）或Le（x）的封端基序等同于在相应的线性主链上的结合。缺乏E-选择素与通过6碳间隔基团连接至生物素的Le（x）基序和Le（x）三糖结合，表明寡糖主链上的-GlcNAcbeta1-3Gal-序列Le（x）相邻是E-选择素识别基序的一部分。这些发现有助于理解E-选择素识别的分子基础，并可能影响选择素拮抗剂作为可能的治疗物质的未来设计。