g(m1)-ganglioside and Nasal-Polyps

This study is intended to demonstrate the versatility and feasibility of custom-made oligosaccharide-exposing neoglycoconjugates including histo-blood group epitopes in various human lesions, including nasal polyps. The binding of the biotinylated probes was determined on formalin-fixed paraffin-embedded sections from archive materials. The general aspects of our results may be interpreted as follows: the neoglycoconjugates used here can readily detect differences in the ability of cells to bind glycan residues in tissue sections, thereby enabling the extent of the binding capacity of various types of human lesions to be compared. Furthermore, the reactivity to glycan may reflect characteristics of the cells and their environment. The investigation into pathological disorders with respect to the binding capacity of these carrier-immobilized mono- or oligosaccharide structures derived from custom-made synthesis or biochemical purification is based on the prospect of translating progress in this field into the establishment of potentially beneficial procedures for medical diagnosis and pathological classification.

Topics: Adenocarcinoma; Binding Sites; Blood Group Antigens; Brain Neoplasms; Breast Neoplasms; Carcinoma, Ductal, Breast; Carcinoma, Transitional Cell; Colonic Neoplasms; Feasibility Studies; Female; Fibroadenoma; G(M1) Ganglioside; Glioblastoma; Glycoconjugates; Histocytochemistry; Humans; Hyaluronic Acid; Male; Melanoma; Nasal Polyps; Neoplasms; Prostatic Hyperplasia; Skin Neoplasms; Trisaccharides; Urinary Bladder Neoplasms

The basis for the unique association of Pseudomonas aeruginosa and the cystic fibrosis (CF) lung has remained obscure despite major advances in the understanding of the molecular genetic cause of this disease. There is evidence to suggest that abnormalities in CF transmembrane conductance regulator function result in alterations in the glycosylation of epithelial components. The number of asialoGM1 residues, as representative of a class of glycolipids which contain a GalNAc beta 1-4Gal sequence for P. aeruginosa attachment, was quantified by flow cytometric studies of respiratory epithelial cells in primary culture from both CF patients and normal subjects. Superficial asialoGM1 was detected on 12% of the CF cells as compared with 2.9% of the cells from normal control subjects (P = 0.03, chi 2 = 4.73), and more asialoGM1 residues were exposed on CF cells after modification by P. aeruginosa exoproducts. AsialoGM1, but not the sialylated glycolipid GM1, was demonstrated to be a receptor for 125I-labeled P. aeruginosa pilin, a major adhesin for this organism, and exogenous asialoGM1 was found to competitively inhibit P. aeruginosa adherence to epithelial cells, thus, confirming the biological role of the asialoGM1 receptor. Quantitative and qualitative differences in the sialylation of superficial glycolipids in CF epithelial cells may directly contribute to the colonization of the CF lung by P. aeruginosa.

Topics: Bacterial Adhesion; Binding, Competitive; Carbohydrate Conformation; Carbohydrate Sequence; Cell Membrane; Cells, Cultured; Cholera Toxin; Chromatography, Thin Layer; Cystic Fibrosis; Epithelium; Fimbriae, Bacterial; Flow Cytometry; G(M1) Ganglioside; Glycolipids; Humans; Molecular Sequence Data; Nasal Polyps; Pseudomonas aeruginosa; Reference Values