Detection of inflammation- and neoplasia-associated alterations in human large intestine using plant/invertebrate lectins, galectin-1 and neoglycoproteins.

Acta anatomica Pub Date : 1998-01-01 DOI:10.1159/000046460
U Brinck, M Korabiowska, R Bosbach, H J Gabius
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引用次数: 29

Abstract

Commonly, plant and invertebrate lectins are accepted glycohistochemical tools for the analysis of normal and altered structures of glycans in histology and pathology. Mammalian lectins and neoglycoproteins are recent additions to this panel for the detection of lectin-reactive carbohydrate epitopes and glycoligand-binding sites. The binding profiles of these three types of probes were comparatively analyzed in normal, inflamed and neoplastic large intestine. In normal colonic mucosa the intracellular distribution of glycoconjugates and carbohydrate ligand-binding sites in enterocytes reveals a differential binding of lectins with different specificity and of neoglycoproteins to the Golgi apparatus, the rough and smooth endoplasmic reticulum and the apical cell surface. The accessible glycoligand-binding sites and the lectin-reactive carbohydrate epitopes detected by galectin-1 show the same pattern of intracellular location excluding the apical cell surface. Lectin-reactive carbohydrate epitopes detected by plant lectins of identical monosaccharide specificity as the endogenous lectin [Ricinus communis agglutinin-I (RCA-I), Viscum album agglutinin (VAA)], however, clearly differ with respect to their intracellular distribution. Maturation-associated differences and heterogeneity in glycohistochemical properties of epithelial cells and non-epithelial cells (macrophages, dendritic cells, lymphocytes) are found. Dissimilarities in the fine structural ligand recognition of lectins with nominal specificity to the same monosaccharide have been demonstrated for the galactoside-specific lectins RCA-I, VAA and galectin-1 as well as the N-acetylgalactosamine (GalNAc)-specific lectins Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA) and Helix pomatia agglutinin in normal mucosa and in acute appendicitis. Acute inflammation of the intestinal mucosa found in acute phlegmonous appendicitis is associated with selective changes of glycosylation of mucin in goblet cells mainly of lower and middle crypt segments resulting in an increase of DBA- and SBA-binding sites in the goblet cell population. Appendicitis causes no detectable alteration of neoglycoprotein binding. In contrast, tumorigenesis of colonic adenoma is characterized by increases in lectin-reactive galactose (Gal; Gal-beta1, 3-GalNAc), fucose and N-acetylglucosamine moieties and by enhanced presentation of respective carbohydrate ligand-binding capacity. This work reveals that endogenous lectins and neoglycoproteins are valuable glycohistochemical tools supplementing the well-known analytic capacities of plant lectins in the fields of gastrointestinal anatomy and gastroenteropathology.

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利用植物/无脊椎动物凝集素、半乳糖凝集素-1和新糖蛋白检测人大肠炎症和肿瘤相关改变
通常,植物和无脊椎动物凝集素是被接受的糖组织化学工具,用于分析正常和改变的组织和病理的聚糖结构。哺乳动物凝集素和新糖蛋白是最近添加到该面板的,用于检测凝集素反应性碳水化合物表位和糖配体结合位点。比较分析这三种探针在正常、炎症和肿瘤大肠中的结合谱。在正常的结肠粘膜中,肠细胞中糖缀合物和碳水化合物配体结合位点的细胞内分布表明,具有不同特异性的凝集素和新糖蛋白与高尔基体、粗糙和光滑的内质网和细胞顶端表面的结合存在差异。半乳糖凝集素-1检测到的可接近的糖配体结合位点和凝集素反应性碳水化合物表位在细胞内的定位模式相同,不包括细胞顶端表面。植物凝集素检测到的凝集素-活性碳水化合物表位与内源性凝集素具有相同的单糖特异性[Ricinus communis agglutinin- i (RCA-I), Viscum album agglutinin (VAA)],但它们在细胞内的分布明显不同。发现上皮细胞和非上皮细胞(巨噬细胞、树突状细胞、淋巴细胞)的糖组织化学特性的成熟相关差异和异质性。在正常粘膜和急性阑尾炎中,半乳糖苷特异性凝集素rca -1、VAA和半乳糖素-1以及n-乙酰半乳糖胺(GalNAc)特异性凝集素Dolichos biflorus凝集素(DBA)、大豆凝集素(SBA)和Helix pomatia凝集素对相同单糖的精细结构配体识别存在差异。急性痰性阑尾炎肠黏膜急性炎症与主要位于下、中隐窝节段的杯状细胞中粘蛋白糖基化的选择性改变有关,导致杯状细胞群中DBA和sba结合位点的增加。阑尾炎不引起可检测到的新糖蛋白结合改变。相反,结肠腺瘤的肿瘤发生以凝集素活性半乳糖(Gal;gal - β, 3-GalNAc),聚焦和n -乙酰氨基葡萄糖,并通过增强各自的碳水化合物配体结合能力。这项工作表明,内源性凝集素和新糖蛋白是有价值的糖组织化学工具,补充了众所周知的植物凝集素在胃肠道解剖学和胃肠病理学领域的分析能力。
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[The subarachnoid space]. Protein-carbohydrate interactions during fertilization. Applications of lectins and neoglycoconjugates in histology and pathology. Detection of inflammation- and neoplasia-associated alterations in human large intestine using plant/invertebrate lectins, galectin-1 and neoglycoproteins. Glycobiology of the olfactory system.
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