alpha 2,6-Hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells

doi:10.1038/aps.2009.84

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	alpha 2,6-Hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells
	Qian, Jin 2; Zhu, Cai-hua 2; Tang, Shuai 1; Shen, Ai-jun2 ; Ai, Jing1 ; Li, Jing1 ; Geng, Mei-yu1,2 ; Ding, Jian2
刊名	ACTA PHARMACOLOGICA SINICA
	2009-07
卷号	30 期号:7 页码:1039-1045
关键词	cell motility c-Met hyposialylation ST6Gal-I
ISSN号	1671-4083
DOI	10.1038/aps.2009.84
文献子类	Article
英文摘要	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.
资助项目	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]
WOS关键词	FIBRONECTIN RECEPTORS ; SIALIC-ACID ; EXPRESSION ; ADHESION ; SIALYLTRANSFERASE ; GLYCOSYLATION ; TUMORIGENESIS ; PROGRESSION ; ACTIVATION ; INTEGRINS
WOS研究方向	Chemistry ; Pharmacology & Pharmacy
语种	英语
CSCD记录号	CSCD:3628681
出版者	ACTA PHARMACOLOGICA SINICA
WOS记录号	WOS:000268066400022
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/279191]
专题	药理学第一研究室
通讯作者	Geng, Mei-yu
作者单位	1.Ocean Univ China, Dept Pharm, Marine Drug & Food Inst, Qingdao 266003, Peoples R China 2.Shanghai Inst Mat Med, Div Antitumor Pharmacol, Shanghai 201203, Peoples R China;
推荐引用方式 GB/T 7714	Qian, Jin,Zhu, Cai-hua,Tang, Shuai,et al. alpha 2,6-Hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells[J]. ACTA PHARMACOLOGICA SINICA,2009,30(7):1039-1045.
APA	Qian, Jin.,Zhu, Cai-hua.,Tang, Shuai.,Shen, Ai-jun.,Ai, Jing.,...&Ding, Jian.(2009).alpha 2,6-Hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells.ACTA PHARMACOLOGICA SINICA,30(7),1039-1045.
MLA	Qian, Jin,et al."alpha 2,6-Hyposialylation of c-Met abolishes cell motility of ST6Gal-I-knockdown HCT116 cells".ACTA PHARMACOLOGICA SINICA 30.7(2009):1039-1045.