Aim: We aimed to investigate the potential modification of previously unrecognized surface glycoprotein(s) by alpha2,6-sialylation other than by integrins.
Methods: The expression of beta-galactoside alpha2,6-sialyltransferase (ST6Gal-I) in the colon cancer cell line HCT116 was reduced by siRNA. The adhesion and Boyden chamber assay were used to detect the variation in cell motility. alpha2,6-Sialylation proteins were detected with lectin affinity assay. The mRNA expression, protein expression and downstream signaling modulation with siRNA were detected using reverse transcription-polymerase chain reaction, flow cytometry analysis, and Western blot.
Results: In HCT116 cells, the knockdown of ST6Gal-I inhibited cell motility, but did not affect cell adhesion. This selectively altered cell migration was caused by the loss of alpha2,6-sialic acid structures on c-Met. Moreover, STAT3 was dephosphorylated at tyrosine 705 in ST6Gal-I-knockdown (ST6Gal-I-KD) HCT116 cells.
Conclusion: c-Met is the substrate of ST6Gal-I. The hyposialylation of c-Met can abolish cell motility in ST6Gal-I-KD HCT116 cells.Acta Pharmacologica Sinica (2009) 30: 1039-1045; doi: 10.1038/aps.2009.84; published online 1 June 2009.
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| http://dx.doi.org/10.1038/aps.2009.84 | DOI Listing |
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