Gabius H J, Wosgien B, Brinck U, Schauer A
Max-Planck-Institut für experimentelle Medizin, Abteilung Chemie, Göttingen, FRG.
Pathol Res Pract. 1991 Sep;187(7):839-47. doi: 10.1016/s0344-0338(11)80580-7.
Protein-carbohydrate interactions constitute a system of molecular interaction with relevance to pathologic conditions. Carrier-immobilized carbohydrate structures enable the histochemical investigation of the protein part of this recognitive system. However, thorough systematic studies are inevitably required for standardized application of this relatively novel class of markers. Consequently, serial sections of 21 cases of malignant breast lesion were comparatively analyzed with three different types of probe, specific for beta-galactoside-binding lectins. In addition to the chemically lactosylated neoglycoprotein, human lectin-binding glycoproteins, purified by affinity chromatography on resins with an immobilized beta-galactoside-specific lectin, and a lectin-specific antibody were employed to answer the question whether differences occur in their capacity for lectin localization. The patterns of staining were qualitatively similar, the lectin-binding glycoproteins yielding the most intense reaction. Having assured the reliable applicability of the neoglycoprotein, structural alterations of the subterminal carbohydrate residue on the labelled carrier addressed the issue, whether selectivity of binding can be inferred histochemically, allowing rational synthetic tailoring. An N-acetylglucosamine residue in beta-1,3-linkage proved to be a less favorable extension than this type of sugar in beta-1,4-linkage or an N-acetylgalactosamine moiety in beta-1,3-linkage. Binding was clearly reduced in cells of normal breast tissue with this probe. In order to gain evidence on the expression of potential carbohydrate ligands for the glyco- and immunohistochemically localized binding activity, a labelled mammalian beta-galactoside-specific lectin was similarly used as histochemical tool. It effectively bound to accessible sites in the sections. The binding pattern was different to that of plant lectins with specificity to beta-galactosides. This result underscores that caution is necessary in the functional interpretation of results of studies with plant, not mammalian lectins.(ABSTRACT TRUNCATED AT 250 WORDS)
蛋白质 - 碳水化合物相互作用构成了一个与病理状况相关的分子相互作用系统。载体固定化的碳水化合物结构使得能够对该识别系统的蛋白质部分进行组织化学研究。然而，对于这类相对新颖的标志物的标准化应用，不可避免地需要进行全面系统的研究。因此，对21例恶性乳腺病变的连续切片用三种不同类型的针对β - 半乳糖苷结合凝集素的探针进行了比较分析。除了化学乳糖基化的新糖蛋白外，还使用了通过固定化β - 半乳糖苷特异性凝集素的树脂上的亲和色谱法纯化的人凝集素结合糖蛋白以及凝集素特异性抗体，以回答它们在凝集素定位能力上是否存在差异的问题。染色模式在质量上相似，凝集素结合糖蛋白产生的反应最为强烈。在确保新糖蛋白可靠适用性之后，标记载体上末端碳水化合物残基的结构改变引发了这样一个问题，即是否可以通过组织化学推断结合的选择性，从而进行合理的合成定制。事实证明，β - 1,3连接的N - 乙酰葡糖胺残基作为延伸部分不如β - 1,4连接的这种类型的糖或β - 1,3连接的N - 乙酰半乳糖胺部分有利。用该探针时，正常乳腺组织细胞中的结合明显减少。为了获得关于糖基化和免疫组织化学定位的结合活性的潜在碳水化合物配体表达的证据，一种标记的哺乳动物β - 半乳糖苷特异性凝集素同样被用作组织化学工具。它有效地结合到切片中的可及位点。这种结合模式与对β - 半乳糖苷具有特异性的植物凝集素不同。这一结果强调，在用植物而非哺乳动物凝集素进行研究的结果功能解释中需要谨慎。（摘要截短至250字）
