Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0085693 (acute appendicitis)
 3,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a glycohistochemical analysis of human appendix vermiformis we report the assessment of lectin binding in cells of the Gut Associated Lymphoid Tissue of normal samples and in acute appendicitis using a panel of plant, invertebrate and mammalian lectins with specificity for alpha-L-Fuc (UEA-I), alpha-D-Gluc and alpha-D-Man (Con A), alpha-D-GalNAc (DBA), GalNAc (SBA, HPA), beta-Gal (RCA-I, 14 kDa = galectin-1) and alpha-, beta-Gal (VAA). Moreover, we initiate the study of expression of carbohydrate-binding sites in this tissue and in colonic mucosa, employing several types of carrier-immobilized carbohydrate ligands as suitable probes for this purpose. Within the three populations of macrophages intra-/subepithelial macrophages of the dome region, the lamina propria of the intercryptal region and the follicle-associated epithelium were apparently reactive with most of the lectins and also with mannose and fucose residues of the tested neoglycoproteins. Distinguishing features of germinal center macrophages in relation to intra-/subepithelial phagocytes were the lack of binding of UEA-I and DBA. In comparison to all other types of phagocytes, macrophages of the T-region displayed a rather restricted binding capacity only to Con A and RCA-I. Labeling of macrophages with SBA, HPA and VAA in this location was only rarely found. With respect to dendritic cells no consistently positive reaction was seen for follicular cells, whereas interdigitating cells of the T-region bound Con A, HPA and RCA-I, and, less frequently, SBA. Lymphocytes in all anatomical subsites of the Gut Associated Lymphoid Tissue, centrocytes, centroblasts and plasma cells had binding sites for Con A and RCA-I in common. Notably, a small number of lymphocytes mostly in the T-region but also in B-cell-rich areas expressed intranuclear binding sites for fucose and mannose residues. Intraepithelial lymphocytes and lymphatic cells of the T-region differed from lymphocytes in other regions by a more frequent expression of VAA-binding sites. The epithelium of appendix vermiformis and colonic mucosa not only presents lectin binding sites, but also has the capacity to bind carbohydrate structures, as shown by labeled glycoligand-exposing neoglycoproteins. In normal mucosa the extent of binding appeared to be associated with maturation of cells, the surface epithelium showing the most intense staining reaction. This pattern is not detectable in colonic adenoma which reveal increased intensity, when compared to normal mucosa. In contrast to development of hyperplasia, acute inflammation in appendicitis caused no detectable changes of neoglycoprotein binding. Taking our previous assessment on lectin binding in appendicitis into account, we conclude that glycosylation of goblet cell mucus, but not the capacity to bind certain sugar epitopes responds to inflammatory processes, whereas tumorigenesis of colonic adenoma can also affect the binding of neoglycoproteins.
 ...
PMID:Histochemical study of expression of lectin-reactive carbohydrate epitopes and glycoligand-binding sites in normal human appendix vermiformis, colonic mucosa, acute appendicitis and colonic adenoma. 893 Jun 36

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.
 ...
PMID:Detection of inflammation- and neoplasia-associated alterations in human large intestine using plant/invertebrate lectins, galectin-1 and neoglycoproteins. 978 Mar 61