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Related Experiment Videos

Human small-intestinal apolipoprotein B-48 oligosaccharide chains.

W V Sasak1, J S Lown, K A Colburn

  • 1Department of Pediatrics, New England Medical Center, Tufts University School of Medicine, Boston, MA 02111.

The Biochemical Journal
|February 15, 1991
PubMed
Summary

This study characterizes the carbohydrate structures of apolipoprotein B-48 (apo B-48) from human small intestine. Researchers found apo B-48 contains a mix of high-mannose and complex N-linked oligosaccharides, with potential O-linked sugars.

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Area of Science:

  • Glycobiology
  • Biochemistry
  • Molecular Biology

Background:

  • Hepatic apolipoprotein B-100 (apo B-100) contains N-linked oligosaccharides.
  • Apolipoprotein B-48 (apo B-48), derived from the small intestine, shares N-terminal sequences with apo B-100.
  • Apo B-48 has five potential N-linked glycosylation sites.

Purpose of the Study:

  • To characterize the carbohydrate moiety of human small-intestinal apo B-48.
  • To identify the types and structures of N-linked oligosaccharides present on apo B-48.
  • To investigate potential O-linked glycosylation in apo B-48.

Main Methods:

  • Organ culture of human small-intestinal explants with L-[35S]methionine and D-[3H]glucosamine labeling.
  • N-Glycanase treatment to release N-linked glycans.

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  • Monosaccharide analysis, lectin binding assays (concanavalin A, wheat germ, peanut, Limulus, soy, Ulex), and chromatography (HPLC, ion-exchange).

    • Main Results:

    • N-Glycanase treatment released D-[3H]glucosamine, indicating N-linked glycosylation.
    • Monosaccharide analysis revealed N-acetylglucosamine, mannose, galactose, fucose, xylose, and N-acetylgalactosamine.
    • Lectin binding confirmed the presence of mannose residues and specific lectin interactions.
    • Oligosaccharide analysis showed 78% biantennary complex-type, 16% high-mannose type, and 6% higher-branched structures.
    • Specific structures identified include Man8GlcNAc2 and various complex-type oligosaccharides (monosialylated, desialylated, fucosylated).

    Conclusions:

    • Human small-intestinal apo B-48 is N-glycosylated with a predominance of biantennary complex-type oligosaccharides.
    • High-mannose type and potentially O-linked sugars are also present on apo B-48.
    • The glycosylation pattern of apo B-48 differs from that of hepatic apo B-100.