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Träfflista för sökning "hsv:(MEDICIN OCH HÄLSOVETENSKAP) hsv:(Klinisk medicin) ;srt2:(1990-1999);pers:(Breimer Michael 1951)"

Sökning: hsv:(MEDICIN OCH HÄLSOVETENSKAP) hsv:(Klinisk medicin) > (1990-1999) > Breimer Michael 1951

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1.
  • Bäcker, Annika E., 1965, et al. (författare)
  • Biochemical and enzymatic characterization of blood group ABH and related histo-blood group glycosphingolipids in the epithelial cells of porcine small intestine.
  • 1997
  • Ingår i: Glycobiology. - : Oxford University Press (OUP). - 0959-6658 .- 1460-2423. ; 7:7, s. 943-53
  • Tidskriftsartikel (refereegranskat)abstract
    • Non-acid glycosphingolipids were isolated from small intestinal epithelial cells of a single blood group A pig. One very predominant blood group compound was obtained chemically pure upon HPLC fractionation. It was characterized by mass spectrometry and 1H NMR spectroscopy to be the type 1 chain blood group A hexaglycosylceramide. Support for the presence of minute amounts of additional A glycolipids was obtained by mass spectrometry and immunostaining of TLC plates with anti-A antibodies specific for A type 2 chain, A type 3 and 4 chain, and the ALe(b) determinant. Among precursor chains, globoside (type 4) and lactotetraosylceramide (type 1) were immunologically identified, whereas no neolactotetraosylceramide (type 2) and gangliotetraosylceramide reactivities were detected. We addressed the question whether the predominant expression of type 1 chain based A glycolipids reflects a restricted glycolipid precursor chain specificity of the alpha 1-2 fucosyl- and/or the alpha 1-3 N-acetylgalactosaminyltransferases, or if the biosynthesis of the precursor chains themselves is regulated. All precursor core saccharides, lacto- (type 1), neolacto-(type 2), and gangliotetraosylceramide as well as globopentaosylceramide (type 4), could serve as acceptors for fucose in vitro when a crude microsomal fraction obtained from mechanically released, porcine intestinal epithelial cells was used as an enzyme source. Under the same conditions an N-acetylgalactosamine residue could be transferred to the blood group H structures based on these core saccharide chains. Lactotriaosylceramide, but not gangliotriaosylceramide, could serve as an acceptor for UDP-galactose. When the product was digested with beta-galactosidase (EC 3.2.1.23) from S.pneumoniae, under conditions where it specifically cleaves Gal beta 1-4 residues, approximately 40% of the radioactivity was cleaved off, indicating that a substantial amount of neolactotetraosylceramide was made in vitro, as opposed to the predominance of lactotetraosylceramide-based structures found in vivo.
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2.
  • Rydberg, Lennart, 1944, et al. (författare)
  • An ELISA technique for quantitation of human xenoantibodies binding to pig cells: application in patients with pig kidneys extracorporeally connected to the circulation.
  • 1998
  • Ingår i: Xenotransplantation. - 0908-665X. ; 5:2, s. 105-10
  • Tidskriftsartikel (refereegranskat)abstract
    • A quantitative ELISA technique for determination of human anti-pig xenoantibody number in serum samples has been established using pig lymphocytes and pig/rabbit erythrocytes as target cells and a pool of serum from human blood group AB donors. The number of low affinity antibodies binding to the cells was determined by quantitation following the use of aqueous washing of the cells and separation of bound and unbound antibodies with the phthalate oil method. The efficiency of different soluble Gal(alpha)1-3Gal-terminating di- and tri-saccharides to inhibit antibody binding was tested and found to vary between 70-90% at a saccharide concentration of 10 mg/ml. The assay was used to evaluate the antibody changes in two patients who, after plasmapheresis treatments, had pig kidneys extracorporeally connected to their blood circulation. The number of anti-pig IgM/IgG antibodies bound to each pig lymphocyte were reduced from 5,600/13,200 to 1,300/3,100 in patient 1 and from 1,200/6,500 to 500/2,100 in patient 2 by three consecutive daily plasmapheresis treatments. Although the lymphocytotoxic titers were reduced to very low levels, the antibody numbers still present in the blood of patient 1 caused a hyperacute rejection of the pig kidney. However, the antibody levels in patient 2 did not cause rejection of this kidney during 15 min perfusion time. A strong anti-pig antibody response 3 weeks after the perfusion experiment was found in patient 1 as shown by 27,600/245,300 IgM/IgG molecules bound to pig lymphocytes corresponding to an increase of lymphocytotoxic titer from 8 to 512. The second patient showed a much weaker immune response with 1,400/19,800 IgM/IgG antibodies corresponding to a lymphocytotoxic titer increase from 8 to 32. The use of this quantitation technique enables more accurate investigation of antibody binding to xenogenic target cells than conventional titration techniques.
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3.
  • Rydberg, Lennart, 1944, et al. (författare)
  • Characterisation of the anti-A antibody response following an ABO incompatible (A2 to O) kidney transplantation.
  • 1992
  • Ingår i: Molecular immunology. - 0161-5890. ; 29:4, s. 547-60
  • Tidskriftsartikel (refereegranskat)abstract
    • Anti-A,B antibodies produced in a blood group OLe(a-b-) recipient receiving a kidney graft from a blood group A2Le(a-b+) donor have been analysed for their ability to bind to different glycosphingolipid antigens. Solid-phase RIA using pure glycosphingolipid antigens and a chromatogram binding assay using total nonacid glycosphingolipid fractions from erythrocytes of different human blood group phenotypes together with pure glycolipid antigens were used as assay systems. Serum antibodies were shown to bind equally well to A (types 1, 2, 3 and 4) and B (types 1 and 2) antigenic structures but no binding to H antigens (types 1, 2 and 4) was detected. After adsorption of serum antibodies on A1 Le(a-b+) erythrocytes there was a residual anti-A antibody activity which could not be adsorbed by synthetic A-trisaccharides coupled to crystalline silica (Synsorb-A). These residual antibodies, which are not present in a pretransplant serum sample, had a specificity for the A antigen with type 1 core saccharide chain and the binding epitope obviously included both the N-acetylgalactosamine and the N-acetylglucosamine. The fucose residue was apparently not obligate for binding. The conformation of the sugar units involved in the binding epitope was determined.
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4.
  • Curtis, J M, et al. (författare)
  • Electron ionization-tandem mass spectrometry of glycosphingolipids. I: The identiftcation of compound-specific sequence ions in the collision-induced dissociation spectra of the immonium ions of two isomeric hexaglycosylceramides.
  • 1992
  • Ingår i: Journal of the American Society for Mass Spectrometry. - : American Chemical Society (ACS). - 1044-0305. ; 3:4, s. 353-9
  • Tidskriftsartikel (refereegranskat)abstract
    • A permethylated-reduced hexaglycosylceramide in a complex glycolipid mixture isolated from a unique human tissue has been identified by using tandem mass spectrometry (MS/MS). The mass spectrum of this glycolipid mixture, obtained by using in-beam electron ionization, is very complex, and fragment ions derived from the hexaglycosylceramide cannot be distinguished from other ions. Tandem mass spectrometry using a four-sector mass spectrometer gave the mass spectrum of the immonium ion of the permethylated-reduced hexaglycosykeramide (m / z 1645.8), which is characteristic of its structure. Comparison of this MS/MS spectrum with those of two similarly derivatized blood group hexaglycosylceramide isomers permitted identification of the unknown glycolipid structure.
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5.
  • Holgersson, J, et al. (författare)
  • Basic biochemistry of cell surface carbohydrates and aspects of the tissue distribution of histo-blood group ABH and related glycosphingolipids.
  • 1992
  • Ingår i: APMIS. Supplementum. - 0903-465X. ; 27, s. 18-27
  • Tidskriftsartikel (refereegranskat)abstract
    • Cell surface carbohydrates may be protein- or lipid-linked. The structural polymorphism of the oligosaccharide chains is extensive due to variations in monosaccharide composition, carbohydrate sequence, branching, linkage position and linkage anomericity. Blood group ABH and related glycosphingolipids show a remarkable tissue-specific expression with possible implications in areas such as transfusion medicine, transplantation surgery and oncology. This communication gives a condensed description of the present knowledge of the tissue-specific distribution of histo-blood glycolipids in humans.
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6.
  • Holgersson, J, et al. (författare)
  • Blood group A glycolipid antigen biosynthesis: discrimination between biosynthesized and enzyme preparation derived blood group A antigen by mass spectrometry.
  • 1990
  • Ingår i: Analytical biochemistry. - 0003-2697. ; 184:1, s. 145-50
  • Tidskriftsartikel (refereegranskat)abstract
    • A monofucosyl type 1 chain blood group A hexaglycosylceramide was biosynthesized in solution using the type 1 chain blood group H pentaglycosylceramide as precursor, a crude microsomal fraction prepared from the mucosa scraping of a blood group A pig small intestine as enzyme source, and uridine diphosphate-N-acetyl-(1-14C)galactosamine as sugar donor. The radioactive product was enriched using reversed-phase column chromatography and silica gel HPLC. The peak, as detected by a beta-flow scintillation counter, was collected, permethylated, and analyzed by mass spectrometry. Carbohydrate sequence ions were found, indicating the presence of both the biosynthesized and a native, non-14C-containing blood group A hexaglycosylceramide. The blood group A pig small intestinal mucosa used as the enzyme source contain blood group A hexaglycosylceramide as the predominant glycolipid. Therefore, it is concluded that the nonradioactive blood group A hexaglycosylceramide found after the biosynthesis is derived from the enzyme preparation.
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7.
  • Holgersson, J, et al. (författare)
  • Blood group A glycolipid antigen expression in kidney, ureter, kidney artery, and kidney vein from a blood group A1Le(a-b+) human individual. Evidence for a novel blood group A heptaglycosylceramide based on a type 3 carbohydrate chain.
  • 1990
  • Ingår i: The Journal of biological chemistry. - 0021-9258. ; 265:34, s. 20790-8
  • Tidskriftsartikel (refereegranskat)abstract
    • Kidney, ureter, kidney artery, and kidney vein tissue were obtained from a single human transplant specimen. The donors erythrocyte blood group phenotype was A1Le(a-b+). Total non-acid glycolipid fractions were isolated and individual glycolipid components were identified by immunostaining thin layer plates with a panel of monoclonal antibodies and by mass spectrometry of the permethylated and permethylated-reduced total glycolipid fractions. The dominating glycolipids in all tissues were mono- to tetraglycosylceramides. In the kidney, ureter, and artery tissue less than 1% of the glycolipids were of blood group type, having more than 4 sugar residues. In contrast, 14% of the vein glycolipids were of blood group type, and the dominating components were type 1 chain blood group H pentaglycosylceramides and A hexaglycosylceramides. Trace amounts of structurally different blood group A glycolipids (type 1 to 4 core saccharide chains) with up to 10 sugar residues were found in the kidney, ureter, and vein tissues, including evidence for a novel blood group A heptaglycosylceramide based on the type 3 chain in the vein. The only detected A glycolipid antigen in the artery tissue was the blood group A difucosyl type 1 chain heptaglycosylceramide (ALeb) structure. Blood group Lewis and related antigens (Lea, Leb, and ALeb) were expressed in the kidney, ureter, and artery, but were completely lacking in the vein, indicating that the Le gene-coded alpha 1-4-fucosyltransferase was not expressed in this tissue. The X and Y antigens (type 2 chain isomers of the Lea and Leb antigens) were detected only in the kidney tissue.
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8.
  • Holgersson, Jan, et al. (författare)
  • Blood group type glycosphingolipids of human kidneys. Structural characterization of extended globo-series compounds.
  • 1991
  • Ingår i: Glycoconjugate journal. - 0282-0080. ; 8:5, s. 424-33
  • Tidskriftsartikel (refereegranskat)abstract
    • Blood group type glycosphingolipids present in kidneys of blood group A and B human individuals have been isolated and structurally characterized by mass spectrometry, proton NMR spectroscopy, degradation studies and by their reactivity with various monoclonal antibodies and Escherichia coli bacteria. The two major complex glycolipids present in the blood group A and B kidneys were globopentaosylceramide (IV3Gal beta-Gb4Cer) and the X pentaglycosylceramide (III3Fuc alpha-nLc4Cer). The major blood group A glycolipid in the blood group A kidneys was based on the type 4 chain (globo-series). There were also small amounts of the type 2 chain and trace amounts of the type 1 and type 3 chain based A glycolipids. In addition, the blood group H type 4 chain structure was present together with Le(a) and Le(b) compounds. In the blood group B kidneys, the major B glycolipids were monofucosylated hexa- and octaglycosylceramides, where the former were based on the type 2 carbohydrate chain. The blood group B type 4 chain heptaglycosylceramide was found to be a minor component making up only about 1% of the total blood group B structures.
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9.
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10.
  • Holgersson, J, et al. (författare)
  • Glycolipid- and glycoprotein-based blood group A antigen expression in human thrombocytes. A1/A2 difference.
  • 1990
  • Ingår i: Glycoconjugate journal. - 0282-0080. ; 7:6, s. 601-8
  • Tidskriftsartikel (refereegranskat)abstract
    • Total non-acid glycolipid fractions and total sodium dodecylsulphate (SDS) solubilized protein fractions were isolated from human thrombocytes obtained from single human donors having different blood group A1/A2 phenotypes. The blood group A glycolipid antigens were characterized by immunostaining of thin layer plates with different monoclonal anti-A antibodies. The glycoproteins carrying blood group A epitopes were identified by SDS-PAGE and Western blot analysis using a monoclonal anti-A antibody. Blood group A glycolipid antigens were found in both A1 and A2 thrombocytes but the A2 individuals expressed at least ten times less A glycolipids compared to the A1 individuals. Expression of A type 3/4 chain and small amounts of A type 1 chain glycolipids were seen in thrombocytes of both A1 and A2 individuals, while the type 2 chain A glycolipids appeared to be missing from the A2 thrombocytes. Blood group A reactive glycoproteins were only found in thrombocytes of A1 individuals and could not be detected in A2 individuals or a blood group O individual. The major blood group A glycoprotein were found as a double band migrating in the 130 kDa region.
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