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Related Experiment Videos

Links between CD147 function, glycosylation, and caveolin-1.

Wei Tang1, Sharon B Chang, Martin E Hemler

  • 1Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.

Molecular Biology of the Cell
|June 18, 2004
PubMed
Summary
This summary is machine-generated.

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This study reveals how CD147 protein size varies due to N-glycosylation, identifying beta1,6-branched polylactosamine sugars on invasive tumor cells. Caveolin-1 inhibits this conversion, explaining its tumor suppressor role.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Biology

Background:

  • Cell surface CD147 exhibits size heterogeneity (31-65 kDa) due to N-glycosylation.
  • Highly glycosylated CD147 (HG-CD147) induces matrix metalloproteinase (MMP) production.
  • Caveolin-1 associates with CD147, inhibiting MMP induction.

Purpose of the Study:

  • To elucidate the biochemical basis of CD147 size variation.
  • To determine the role of CD147 in carrying beta1,6-branched polylactosamine sugars on tumor cells.
  • To investigate the mechanism by which caveolin-1 regulates CD147 glycosylation and function.

Main Methods:

  • N-glycosylation site analysis.
  • Lectin binding assays (l-Phytohemagglutinin).
  • Enzyme inhibition studies (swainsonine).

Related Experiment Videos

  • Protein cross-linking and immunoprecipitation.
  • Monoclonal antibody characterization (AAA6).

    • Main Results:

    • All three CD147 N-glycosylation sites contribute to both high and low glycoforms (HG- and LG-CD147).
    • HG-CD147 contains N-acetylglucosaminyltransferase V-catalyzed beta1,6-branched polylactosamine sugars.
    • Caveolin-1 associates with LG-CD147 and inhibits its conversion to HG-CD147.
    • HG-CD147, but not LG-CD147, self-aggregates and is recognized by antibody AAA6, which inhibits MMP induction.

    Conclusions:

    • CD147 is a significant carrier of beta1,6-branched polylactosamine sugars on invasive tumor cells.
    • Caveolin-1 restricts the conversion of LG-CD147 to HG-CD147, thereby inhibiting CD147 self-aggregation and MMP induction.
    • These findings provide a mechanism for the tumor suppressor functions of caveolin-1.