Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation.
Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation.
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Galectin-5 与游离糖和哺乳动物糖蛋白的相互作用概况：探讨其精细特异性和自然成簇配体呈递的效果。
作者：
A. M. Wu;T. Singh;June H. Wu;M. Lensch;S. André;H. Gabius
细胞表面聚糖是组织凝集素（例如半乳糖凝集素家族成员）的功能性对接位点。这种互动会引发各种各样的反应；因此，人们对定义其结构特征产生了浓厚的兴趣。为了实现这一目标，我们使用酶联凝集素吸附剂 (ELLSA) 和大鼠半乳糖凝集素原型 5 以及游离糖和复合糖组进行抑制测定。在测试凝集素结合的 45 种天然聚糖中，半乳糖凝集素 5 与糖蛋白 (gps) 的反应最好，呈现出高密度的 Galbeta1-3/4GlcNAc (I/II) 和具有 II 末端的多触角 N 聚糖。以纳克为单位计算，它们的反应活性分别比单体 Galbeta1-3/4GlcNAc (I/II)、三触角-II (Tri-II) 和 Gal 高 4.3 x 10(2)、3.2 x 10(2)、2.5 x 10(2) 和 1.7 x 10(4) 倍。 Galectin-5 还可与多种含有 B 型 (Galalpha1-3Gal) 和 A (GalNAcalpha1-3Gal) 血型的 gps 良好结合。它与肿瘤相关 Tn (GalNAcalpha1-Ser/Thr) 和唾液酸化 gps 反应较弱或根本不反应。在测试的单糖、二糖、寡糖和哺乳动物糖复合物中，血型 B 活性 II (Galalpha1-3Gal beta1-4GlcNAc)、B 活性 IIbeta1-3L (Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc) 和 Tri-II 是最好的。结论是：(1) Galbeta1-3/4GlcNAc 和其他具有 alpha1-3 延伸的 Galbeta1 相关寡糖对于结合至关重要，它们在细胞糖缀合物中的多价形式是 galectin-5 的关键识别力； (2)半乳糖凝集素-5的结合位点似乎是浅槽型，足够大以容纳取代的β-半乳糖苷，特别是在非还原端具有α-异头延伸（例如，人血型B-活性II和B-活性IIbeta1-3L）； (3) β-端基异构定位中的偏好是Galbeta1-4>或=Galbeta1-3>Galbeta1-6； (4)核心半乳糖单元附近的疏水相互作用可以增强结合。这些结果对于系统比较该粘附/生长调节效应物家族中的配体选择具有重要的医学应用潜力。
Cell-surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. Toward this aim, we have used enzyme-linked lectinosorbent (ELLSA) and inhibition assays with the prototype rat galectin-5 and panels of free saccharides and glycoconjugates. Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Galbeta1-3/4GlcNAc (I/II) and multiantennary N-glycans with II termini. Their reactivities, on a nanogram basis, were up to 4.3 x 10(2), 3.2 x 10(2), 2.5 x 10(2), and 1.7 x 10(4) times higher than monomeric Galbeta1-3/4GlcNAc (I/II), triantennary-II (Tri-II), and Gal, respectively. Galectin-5 also bound well to several blood group type B (Galalpha1-3Gal)- and A (GalNAcalpha1-3Gal)-containing gps. It reacted weakly or not at all with tumor-associated Tn (GalNAcalpha1-Ser/Thr) and sialylated gps. Among the mono-, di-, and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Galalpha1-3Gal beta1-4GlcNAc), B-active IIbeta1-3L (Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc), and Tri-II were the best. It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 > or = Galbeta1-3 > Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. These results are important for the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications.
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影响因子：
4.3
作者：
Wu,AM;Song,SC;Chang,SC;Wu,JH;Chang,KS;Kabat,EA
通讯作者：
Kabat,EA
影响因子：
4.3
作者：
Gupta, D;Kaltner, H;Brewer, CF
通讯作者：
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影响因子：
4.3
作者：
Wu,AM;Wu,JH;Chen,YY;Song,SC;Kabat,EA
通讯作者：
Kabat,EA
影响因子：
2.9
作者：
Dam, TK;Gabius, HJ;Brewer, CF
通讯作者：
Brewer, CF
三种可溶性大鼠 β-半乳糖苷结合凝集素。
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Cerra,RF;Gitt,MA;Barondes,SH
通讯作者：
Barondes,SH