Abstract
Aim:
We aimed to investigate the potential modification of previously unrecognized surface glycoprotein(s) by α2,6-sialylation other than by integrins.
Methods:
The expression of β-galactoside α2,6-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. α2,6-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 α2,6-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.
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Acknowledgements
This work was supported by the National Basic Research Program Grant (No 2003CB716400) of China, the Natural Science Foundation of China for Distinguished Young Scholars (No 30725046) and the Natural Science Foundation of China for Innovation Research Group (No 30721005).
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Qian, J., Zhu, Ch., Tang, S. et al. α2,6-hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells. Acta Pharmacol Sin 30, 1039–1045 (2009). https://doi.org/10.1038/aps.2009.84
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DOI: https://doi.org/10.1038/aps.2009.84
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