Modification of Sialylation Mediates the Invasive Properties and Chemosensitivity of Human Hepatocellular Carcinoma

Zhao, Yongfu; Li, Yanping; Ma, Haiying; Dong, Wei; Zhou, Huimin; Song, Xianmin; Zhang, Jianing; Li, Jia

doi:10.1074/mcp.m113.034025

Cited by 61 publications

(54 citation statements)

References 35 publications

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“…Accordingly, it can be concluded that the effects of ST6GAL1 on EMT induction and cell migration were also mediated through the PI3K/Akt signaling pathway. In agreement with this, several groups, including us, recently reported that ST6GAL1 promotes cell migration and invasion by activating PI3K/Akt signaling (21,24), and this enhanced migratory response has been shown to be due, at least in part, to ST6GAL1-mediated sialylation of the ␤1 integrin receptor (19, 39, 40). Nonetheless, the GE11 cell utilized here is a ␤1 integrin-null cell line.…”

Section: Discussionmentioning

confidence: 55%

“…3F, no significant difference in the expression of phospho-Smad was observed between the St6gal1 knockdown cells and control cells, indicating that St6gal1 may contribute to EMT through non-Smad pathways. Given the recent reports showing that St6gal1 promotes cell migration and invasion by activating PI3K/Akt signaling (21,24), the activity of this signaling pathway was examined. The phosphorylation level of Akt was clearly decreased after knockdown of St6gal1 in GE11 cells with or without TGF-␤ treatment, suggesting that silencing St6gal1 was able to inhibit the PI3K/Akt signaling in TGF-␤-induced EMT.…”

Section: The Sp1 Binding Site Within St6gal1 Promoter-344 Was Requirementioning

confidence: 99%

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β-Galactoside α2,6-Sialyltranferase 1 Promotes Transforming Growth Factor-β-mediated Epithelial-Mesenchymal Transition

Isaji

et al. 2014

Journal of Biological Chemistry

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Background: Molecular mechanisms underlying the effect of sialylation on tumor progression remain unclear. Results: ST6GAL1 promoted the TGF-␤-induced EMT through down-regulation of E-cadherin-mediated cell adhesion and up-regulation of integrin-mediated cell migration. Conclusion: Expression of ST6GAL1 is critical for sufficient induction of EMT. Significance: ␣2,6-Sialylation of N-glycans may play a role in EMT.

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Section: Discussionmentioning

confidence: 55%

Section: The Sp1 Binding Site Within St6gal1 Promoter-344 Was Requirementioning

confidence: 99%

β-Galactoside α2,6-Sialyltranferase 1 Promotes Transforming Growth Factor-β-mediated Epithelial-Mesenchymal Transition

Isaji

et al. 2014

Journal of Biological Chemistry

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“…We investigated the molecular mechanism by which ST6GalNAcII-mediated PI3K/Akt signaling pathway regulates follicular thyroid cancer cells invasiveness. Our study explored a novel mechanism that the invasion and chemosensitivity of human hepatocarcinoma cells can be regulated by the activation of ST6GAL1 or ST8SIA2-mediated PI3K/Akt (28). In this study, we indicated that ST6GalNAcII exerts the role of tumor metastasis of human follicular thyroid carcinoma through activation of the PI3K/Akt/NF-κB signal pathway.…”

Section: Discussionmentioning

confidence: 77%

ST6GalNAcII mediates tumor invasion through PI3K/Akt/NF-κB signaling pathway in follicular thyroid carcinoma

Miao

Zhao

2016

Oncology Reports

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Abstract. Altered sialylation, closely associated with tumor progression and metastasis, has been implicated in human thyroid carcinoma. The present study investigated the alteration in expression of ST6GalNAcII involved in invasion and to clarify the possible mechanism of ST6GalNAcII in the metastasis process in human follicular thyroid carcinoma cell lines. Using real-time PCR, western blot and IHC analysis, ST6GalNAcII differed in three follicular thyroid cancer cell lines (FTC133, primary and FTC238, lung metastasis). It also showed differential expression in follicular thyroid carcinoma and tissue specimens. In addition, we analyzed the PI3K/Akt signaling pathway. The altered expression of ST6GalNAcII corresponded to changed invasive phenotype of FTC-238 and FTC-133 cells in vitro and in vivo. Further studies showed that regulating ST6GalNAcII expression markedly modulated the activity of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. Targeting the PI3K/Akt pathway by its specific inhibitor LY294002, or by Akt small interfering RNA (siRNA) resulted in reduced capacity in invasion of FTC-238. In conclusion, taken together, our results imply that ST6GalNAcII activated the invasion in follicular thyroid cancer cells through regulating the activity of PI3K/Akt pathway.

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“…TACA expression can be a result of changes in several different steps in the glycoprocessing machinery, including increased/decreased sialylation 14–24 or fucosylation 25–29 , increased N-linked glycan branching, altered O-linked glycolipid (ganglioside) compositions 30–34 and truncated mucin-type O-glycans. 16,35–50 These structures, in part, may modify the physical and chemical properties of the tumor cell, leading to altered cell adhesion and signal transduction, often resulting in enhanced aggressiveness and metastatic potential.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and cell-selective antitumor properties of amino acid conjugated tumor-associated carbohydrate antigen-coated gold nanoparticles

Biswas

Medina

Barchi

2015

Carbohydrate Research

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The Thomsen Friedenreich antigen (TFag) disaccharide is a tumor-associated carbohydrate antigen (TACA) found primarily on carcinoma cells and rarely expressed in normal tissue. The TFag has been shown to interact with Galectin-3 (Gal-3), one in a family of β-galactoside binding proteins. Galectins have a variety of cellular functions, and Gal-3 has been shown to be the solegalectin with anti-apoptotic activity. We have previously prepared gold nanoparticles (AuNP) coated with the TFag in various presentations as potential anti-adhesive therapeutic tools or antitumor vaccine platforms. Here we describe the synthesis of TFag-glycoamino acid conjugates attached to gold nanoparticles through a combined alkane/PEG linker, where the TFag was attached to either a serine or threonine amino acid. Particles were fully characterized by a host of biophysical techniques, and along with a control particle carrying hydroxyl-terminated linker units, were evaluated in both Gal-3 positive and negative cell lines. We show that the particles bearing the saccharides selectively inhibited tumor cell growth of the Gal-3 positive cells significantly more than the Gal-3 negative cells. In addition, the threonine-attached TF particles were more potent than the serine-attached constructs. These results support the use of AuNP as antitumor therapeutic platforms, targeted against cell lines that express specific lectins that interact with TFag.

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Modification of Sialylation Mediates the Invasive Properties and Chemosensitivity of Human Hepatocellular Carcinoma

Cited by 61 publications

References 35 publications

β-Galactoside α2,6-Sialyltranferase 1 Promotes Transforming Growth Factor-β-mediated Epithelial-Mesenchymal Transition

β-Galactoside α2,6-Sialyltranferase 1 Promotes Transforming Growth Factor-β-mediated Epithelial-Mesenchymal Transition

ST6GalNAcII mediates tumor invasion through PI3K/Akt/NF-κB signaling pathway in follicular thyroid carcinoma

Synthesis and cell-selective antitumor properties of amino acid conjugated tumor-associated carbohydrate antigen-coated gold nanoparticles

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