morphine and Intestinal-Neoplasms

Extracts of the human intestinal tumor cell line SW1116 were able to stimulate the incorporation of (14C) fucose from GDP-(14C) fucose into organically soluble glycolipid. The reaction required a purified glycolipid preparation from human meconium as lipid acceptor. The active glycolipid co-migrated with standard globoside on high performance thin-layer chromatography (HPTLC) and had molecular species (M + H) under fast-atom bombardment mass spectrometry of 1199, 1245 and 1269. Globoside itself was inactive and asialo GM1b had low activity. The radioactive products co-purified with Lewis a and Lewis b and co-migrated principally (60-90%) with Lewis b monoclonal antibody binding cellular glycolipids on HPTLC. Analysis of fucosidase digests suggested the presence of two different fucosyl-hexose linkages one of which was susceptible to cleavage. We conclude that the data are consistent with fucosylation of lactotetraosyl ceramide to Lewis a and Lewis b antigenic glycolipids.

Topics: Antibodies, Monoclonal; Cell Line; Cell-Free System; Chromatography, High Pressure Liquid; Fucose; G(M1) Ganglioside; Globosides; Glycolipids; Glycosphingolipids; Humans; Intestinal Neoplasms; Lewis Blood Group Antigens; Mass Spectrometry; Meconium; Molecular Weight; Taurocholic Acid

Antigen of human fetal bowels with a relative electrophoretic mobility matching that of beta 1-globulins was identified using organ-specific rabbit antisera. It was designated as beta 1- meconial antigen (beta 1-MA). beta 1MA is thermolabile, precipitated with chloric acid and phenol, and has a molecular weight of ca. 2 x 10(6) dalton . It was identified by immunodiffusion methods in tissues of definitive and fetal intestine, a third of specimens of fetal stomach, meconium, and all tumors of the large intestine studied. The antigen was not found either in tumors of other sites, or in definitive and fetal organs and tissues other than ones mentioned above.

Topics: Adult; Antigens; Antigens, Neoplasm; Epitopes; Fetus; Gestational Age; Humans; Immunodiffusion; Immunoelectrophoresis, Two-Dimensional; Infant, Newborn; Intestinal Neoplasms; Intestines; Meconium

Human gastrointestinal glycoproteins (mucins), isolated by pepsin digestion from foetal stomachs and meconia, and from paired tumour and non-neoplastic mucosal samples of patients with gastric and colorectal carcinomas, were tested for precipitating reactions with peanut lectin (PNL) and four anti-carbohydrate antibodies (two anti-I, Ma and Low, and two anti-i, Den and Galli). There was remarkable correlation between reactivities with PNL and anti-I (Ma): both reagents reacted with non-neoplastic gastric glycoproteins of "non-secretors", but not with those of "secretors", and also with the majority of gastric tumour and meconium extracts regardless of secretor status. Colorectal tissue extracts (with the exception of one tumour extract) reacted with neither reagent. The various precipitating activities, and results of mild acid hydrolysis and affinity chromatography experiments, enable certain inferences to be made regarding the oligosaccharide moieties of gastrointestinal glycoproteins: (a) expression of PNL and anti-I (Ma) determinants in gastric glycoproteins is dependent on secretor status; (b) extracts reacting with PNL and anti-I (Ma) are mixtures of macromolecules: minor populations react with both reagents, or with PNL only; the major population lacks both determinants, or they are masked by other substitutions; (c) determinants reactive with anti-Ii sera other than anti-I (Ma) are less frequently expressed; and (d) colonic glycoproteins in their lack of PNL and Ii determinants. This suggests that there are structural differences in the oligosaccharide backbones of the two types of glycoprotein.

Topics: Antibodies, Monoclonal; Antigens, Neoplasm; Blood Group Antigens; Carbohydrate Sequence; Epitopes; Gastric Mucosa; Humans; Hydrolysis; I Blood-Group System; Intestinal Mucosa; Intestinal Neoplasms; Lectins; Meconium; Mucins; Oligosaccharides; Peanut Agglutinin; Stomach Neoplasms; Structure-Activity Relationship