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N Strömberg

Publications and source records attributed to N Strömberg.

47 records · Page 3Linked to original sources
PubMed1986

An antigen present in rat adenocarcinoma and normal colon non-epithelial stroma is a novel Forssman-like glycolipid based on isoglobotetraosylceramide.

A glycolipid with blood group A activity detected in the non-epithelial stroma of normal rat colon but not in epithelial cells (Hansson, G.C., Karlsson, K.-A., and Thurin, J. (1984) Biochim. Biophys. Acta 792, 281-292), was purified to homogeneity from normal rat colon and rat colon adenocarcinoma. Mass spectrometry and 1H-NMR spectroscopy of the intact permethylated derivative and gas chromatography after degradation revealed the structure GalNAc alpha 1----3GAINAc beta 1----3Gal alpha 1----3Gal beta 1----4Glc beta 1----1Cer, with the predominant ceramide containing sphingosine and non-hydroxylated 24:0 fatty acid. This identifies this glycolipid as a novel Forssman-like glycolipid, which is a tumor-associated antigen by definition, since it is not present in the normal rat large intestinal epithelium cells but in rat adenocarcinoma derived from these cells.

Acetaminophen↗
PubMed1986

A novel sulfoglycosphingolipid of mouse small intestine, IV3-sulfogangliotetraosylceramide, demonstrated by negative ion fast atom bombardment mass spectrometry.

In a comparative study of acidic glycosphingolipids in the small intestine of several species it was found that the mouse contained a complex sulfoglycolipid as a major component (Breimer, M.E., Hansson, G.C., Karlsson, K.-A., and Leffler, H. (1983) J. Biochem. (Tokyo) 93, 1473-1485). Fast atom bombardment negative ion mass spectrometry proved the presence and location of the sulfate group and also showed the saccharide sequence and ceramide composition. Combined with NMR spectroscopy of the intact structure and degradative studies the structure was shown to be -O3SO----3Galp beta 1----3GalNAcp beta 1----4Galp beta 1----4Glcp beta 1----1Cer. The sulfoglycolipid was enriched in epithelial cells of mouse small intestine where it constituted at least 90% of the acidic glycolipids and 4-8 mol% of the total glycosphingolipids.

Animals↗
PubMed1986

Production of oligosaccharide-binding monoclonal antibodies of diverse specificities by immunization with purified tumor-associated glycolipids inserted into liposomes with lipid A.

Two species of neutral glycosphingolipids purified from rat colon carcinoma tissue, isoglobotetraosylceramide [GalNAc(beta 1----3)Gal(alpha 1----3)Gal(beta 1----3)Glc(beta 1----1)Cer] and a related 6-sugar "analogue" were inserted into liposomes together with lipid A (from bacterial lipopolysaccharide) and used for immunization of mice and monoclonal antibody production. The yield of hybridomas producing glycolipid-specific antibody was 5-10% using a high-dose booster schedule with liposome-inserted glycolipid. In contrast the frequency was below 0.1% (no glycolipid-binding antibodies were found) when using the previously described method of immunizing with glycolipid coated on the surface of acid-treated S. minnesota. Monoclonal antibodies were screened on the purified glycolipids used for immunization and selected for differential reactivity to the two glycolipids. A diversity of specificities was demonstrated by binding to the purified antigens, in a thin-layer chromatogram binding assay and in binding tests to tumor and normal target cells.

Adenocarcinoma↗
PubMed1985

Mouse monoclonal antibodies with specificity for the melanoma-associated ganglioside disialyllactosylceramide (GD3) also react with the structural analogue disialylparagloboside.

A mouse monoclonal IgM antibody, 4.2, has previously been shown to bind preferentially to the surface of human malignant melanoma cells and to have specificity for the GD3 ganglioside (NeuAc alpha 2----8NeuAc alpha 2----3Gal beta 1----4GlcCer). Using overlay of antibodies on thin-layer chromatograms with glycolipids of various sources, it was shown that antibody 4.2, a further IgM and two IgG3 mouse monoclonal antibodies, selected on the basis of reactivity with GD3, also bound with similar strength to the structural analogue NeuAc alpha 2----8NeuAc alpha 2----3Gal beta 1----4GlcNac beta 1----3Gal beta 1----4GlcCer or disialylparagloboside. The SK-MEL 28 melanoma cell line used for immunization was shown to contain a large amount of GD3 but to lack disialylparagloboside. The demonstrated cross-reactivity may be of importance when considering the use of these antibodies for biochemical and medical purposes.

Animals↗
PubMed1985

Proton NMR and fast-atom bombardment mass spectrometry analysis of the melanoma-associated ganglioside 9-O-acetyl-GD3.

A glycolipid antigen, detected by a monoclonal antibody (ME 311) obtained by immunizing mice with a human metastatic melanoma cell line (WM 46), was isolated and structurally characterized. Using immunostaining on thin-layer chromatograms for monitoring, 1.0 mg of a pure alkali-labile disialoganglioside was obtained from 23 g of packed melanoma cells (WM 164). Fractionation of the lipid extract was done on DEAE-Sepharose columns into total disialogangliosides which were repeatedly separated by high-pressure liquid chromatography. On mild alkaline treatment, the ganglioside was converted to a slower migrating species identical with a ganglioside GD3 isolated from the same source (Neu5Ac alpha 2----8Neu5Ac alpha 2----3Gal beta 1----4Glc beta 1----1-cer-amide) and specifically detected by monoclonal antibody R24. Comparison of the two gangliosides by fast-atom bombardment mass spectrometry (revealing an acetyl group on the terminal sialic acid on the alkali-labile species) and by 1H NMR (indicating the position of the acetyl group) suggested the following structure: Neu5,9Ac2 alpha 2----8Neu5Ac alpha 2----3Gal beta 1----4Glc beta 1----1-ceramide. This is identical with a ganglioside proposed earlier to exist in melanoma cells (Cheresh, D. A., Varki, A. P., Varki, N. M., Stallcup, W. B., Levine, J., and Reisfeld, R. A. (1984) J. Biol. Chem. 259, 7453-7459). Immunostaining with ME 311 antibody of cell extracts on thin-layer chromatography chromatograms revealed only this ganglioside in the melanoma cells, while normal human brain was negative. However, in one of the total ganglioside extracts tested for presence of binding with antibody ME 311, three gangliosides were found to bind. No evidence was obtained for the presence of the antigenic epitope in mucins or glycoproteins of the melanoma cells.

Antibodies, Monoclonal↗
PubMed1985

Specificity of binding of a strain of uropathogenic Escherichia coli to Gal alpha 1----4Gal-containing glycosphingolipids.

A strain of Escherichia coli originally isolated from urine of a patient with acute pyelonephritis was studied in detail for binding to glycosphingolipids. Bacteria labeled metabolically with [14C]glucose were layered over a glycolipid chromatogram and bound bacteria were detected by autoradiography. The detection was down to a few ng of glycolipid (pmol level) under these assay conditions. At a test level of 500 ng all glycolipids (more than a dozen molecular species analyzed) with Gal alpha 1----4Gal as an internal or terminal part bound the bacteria strongly while glycolipids known to lack this sequence were negative. Conformational analysis using hard sphere calculations including the exo-anomeric effect showed a bend in the saccharide chain at this disaccharide with a largely hydrophobic surface of the convex side, probably being part of the binding epitope. Mixtures of glycolipids isolated from a human ureter scraping and from urinary sediments bound bacteria in the 2- to 7-sugar interval. Thus, this infectious strain of E. coli recognizes glycolipids being present in epithelial cells lining the urinary tract.

ABO Blood-Group System↗
PubMed1985

Carbohydrate-specific adhesion of bacteria to thin-layer chromatograms: a rationalized approach to the study of host cell glycolipid receptors.

Conditions have been adapted for the binding of intact bacteria to glycosphingolipids in a thin-layer chromatogram. Bacteria labeled externally with 125I or metabolically with other isotopes are layered on the plate and after repeated washing the bound bacteria are detected by autoradiography. Using this technique several kinds of bacteria have been shown to adhere to the plate in a carbohydrate-specific way with practically no background binding. Among the advantages of the method is the possible detection of a minor receptor component of a complex mixture extracted from a target cell, facilitating the isolation of the receptor for structural studies. In addition, the multivalent solid-phase presentation of the receptor candidate should also reveal low-affinity binding sites, which may escape detection in traditional inhibition experiments with soluble oligosaccharides.

Adhesiveness↗
PubMed1984

A novel approach to the study of glycolipid receptors for viruses. Binding of Sendai virus to thin-layer chromatograms.

A method for the binding of virus to a silica gel thin-layer chromatogram is presented. After development the chromatogram is overlayed with the 125I-labelled virus and the bound virus is autoradiographed. Alternatively, the unlabelled virus may be detected after exposure to monoclonal antibody and labelled anti-antibody. The Sendai virus strain used did not bind to brain gangliosides earlier proposed to be receptors, but bound to human erythrocyte gangliosides. This finding may be explained by the existence of Sendai virus variants with different receptor specificities.

Animals↗