期刊
ACTA PHARMACOLOGICA SINICA
卷 30, 期 7, 页码 1039-1045出版社
ACTA PHARMACOLOGICA SINICA
DOI: 10.1038/aps.2009.84
关键词
cell motility; c-Met; hyposialylation; ST6Gal-I
资金
- National Basic Research Program [2003CB716400]
- Natural Science Foundation of China for Distinguished Young Scholars [30725046]
- Natural Science Foundation of China for Innovation Research Group [30721005]
Aim: We aimed to investigate the potential modification of previously unrecognized surface glycoprotein(s) by alpha 2,6-sialylation other than by integrins. Methods: The expression of beta-galactoside alpha 2,6-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. alpha 2,6-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 alpha 2,6-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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