@article{APS5116,
author = {Jin Qian and Cai-hua Zhu and Shuai Tang and Ai-jun Shen and Jing Ai and Jing Li and Mei-yu Geng and Jian Ding},
title = {α2,6-hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells},
journal = {Acta Pharmacologica Sinica},
volume = {30},
number = {7},
year = {2016},
keywords = {},
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.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/5116}
}