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A more recent version of this article appeared on September 1, 2004
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Submitted on May 14, 2004
Revised on June 2, 2004
Accepted on June 7, 2004
Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115
Monitoring Editor: Reid Gilmore
Cell surface CD147 shows remarkable variation in size (31-65 kDa) due to heterogeneous N-glycosylation, with the most highly glycosylated forms functioning to induce of MMP (matrix metalloproteinase) production. Here we show that all three CD147 N-glycosylation sites make similar contributions to both high and low glycoforms (HG- and LG-CD147). L-PHA lectin binding and swainsonine inhibition experiments indicate that HG-CD147 contains GnT-V (N-acetylglucosaminyl transferase-V) catalyzed, 
1,6 branched, polylactosamine-type sugars, which account for its excess size. Hence CD147, which is itself elevated on invasive tumor cells, may make a major contribution to the abundance of 1,6 branched polylactosamine sugars that appear on invasive tumor cells. Previously it was shown that caveolin-1 associates with CD147, thereby inhibiting CD147 self-aggregation and MMP induction; now we show that caveolin-1 associates with LG-CD147 and restricts the biosynthetic conversion of LG-CD147 to HG-CD147. In addition, HG-CD147 (but not LG-CD147), was a) preferentially captured as a multimer upon treatment of cells with homobifunctional cross-linking agent, and b) exclusively recognized by mAb AAA6, a reagent that selectively recognizes self-associated CD147 and inhibits CD147-mediated MMP induction. In conclusion, we have 1) uncovered the biochemical basis for the unusual size variation in CD147, 2) established that CD147 is a major carrier of 1,6 branched polylactosamine sugars on tumor cells, 3) determined that caveolin-1 can inhibit conversion of LG-CD147 to HG-CD147, and 4) since it is HG-CD147 that self-aggregates and stimulates MMP induction, we how have a mechanism to explain how caveolin-1 inhibits these processes. These results help to explain previously established tumor suppressor functions of caveolin-1.
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