Fischer J, Klein P J, Uhlenbruck G
Department of Pathology, University Medical School of Pécs, Hungary.
Acta Histochem Suppl. 1988;36:191-207.
Labelled lectins were used for the histochemical distinction of glycolipids with various terminal hexoses in different storage diseases as well as for the demonstration of differences in the composition of cell surface and intercellular glycoproteins in tissues at various stages of differentiation, in malignancy and in functional subsets of cells. Thereby the detection of some glycoproteins (i.e. in primary sensory neurones, in parietal cells or in polymorphonuclear leukocytes), which were invisible by formerly used methods, was also possible. In malignant tissues lectin binding was either altered or the intracellular localization of the lectin binding sites was changed. These differences did not represent tumour specific markers, rather they were found to reflect glycoprotein structures characteristic for an activated functional state or for an earlier grade of differentiation. Some of such glycoproteins were isolated by lectin affinity chromatography and their structures were further analysed by means of biochemical methods. In malignancy a reduced molecular weight and changes in the monosaccharide composition of surface or intracellular glycoproteins were found to be the main differences. Antibodies produced against the lectin affinity isolated glycoproteins allowed the demonstration of structural relationship of glycoproteins with identical or diverse lectin binding pattern. They proved to be also useful for diagnostic purposes, especially for the differential diagnosis of anaplastic tumours.
标记的凝集素用于不同储存疾病中具有各种末端己糖的糖脂的组织化学鉴别，以及用于证明在分化的各个阶段、恶性肿瘤和细胞功能亚群中组织的细胞表面和细胞间糖蛋白组成的差异。由此，还能够检测到一些以前使用的方法无法检测到的糖蛋白（如在初级感觉神经元、壁细胞或多形核白细胞中）。在恶性组织中，凝集素结合要么发生改变，要么凝集素结合位点的细胞内定位发生变化。这些差异并不代表肿瘤特异性标志物，相反，它们被发现反映了激活功能状态或早期分化阶段特有的糖蛋白结构。通过凝集素亲和层析分离出其中一些糖蛋白，并通过生化方法进一步分析其结构。在恶性肿瘤中，发现表面或细胞内糖蛋白的分子量降低和单糖组成变化是主要差异。针对凝集素亲和分离的糖蛋白产生的抗体能够证明具有相同或不同凝集素结合模式的糖蛋白之间的结构关系。它们还被证明对诊断有用，特别是对间变性肿瘤的鉴别诊断。
