Increase in β1‐6 GlcNAc branching caused by <i>N</i>‐acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC‐7721

Wang, Liying; Liang, Yulong; Li, Zengxia; Cai, Xiumei; Zhang, Wen; Wu, Guoqiang; Jin, Jun; Fang, Zhengyu; Yang, Yong; Zha, Xiliang

doi:10.1002/jcb.21071

Cited by 27 publications

(21 citation statements)

References 43 publications

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“…Furthermore, depletion of the Mgat5-modified glycans by swainsonine can enhance Ag-dependent T cell proliferation in vitro (16), and similar results were observed in Mgat5 gene knockout mice (13). Recently it was reported that Mgat5 directed integrin stability (17) and regulated expression of cytokine receptors, which balances their surface retention against loss via endocytosis (18). These reports suggest that stimulated IFN-␥ production and enhanced T cell activation and differentiation might be achieved by down-regulation of Mgat5.…”

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confidence: 70%

Knockdown of Mgat5 Inhibits Breast Cancer Cell Growth with Activation of CD4+ T Cells and Macrophages

et al. 2008

The Journal of Immunology

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N-acetylglucosaminyltransferase V (Mgat5 or GnT-V) is an enzyme that catalyzes β1–6 branching of N-acetylglucosamine on asparagine (N)-linked oligosaccharides (N-glycan) of cell proteins. The levels of Mgat5 glycan products commonly are increased in malignancies. Although Mgat5 is known to be important in tumor metastases, the effects of Mgat5 on host immune responses are not fully defined. In this study, a Mgat5 specific-short hairpin RNA (shRNA) vector was transfected into murine mammary adenocarcinoma MA782 cells to assess the effects of Mgat5 on tumor cell growth, T cells, and macrophages following inoculation of mice with shRNA-transfected cancer cells. The results showed that blocking expression of Mgat5-modified glycans in MA782 cells significantly suppressed tumor progression both in vivo and in vitro, strongly stimulated Th1 cytokine production, and enhanced opsonophagocytic capability of macrophages in vivo. Importantly, reduction of complex N-glycans on MA782 tumor cells by Mgat5-shRNA resulted in significantly increased proliferation and CD45 surface expression of CD4+ T cells. Our data suggest Mgat5-shRNA could serve as a useful tool to treat breast cancer as well as a powerful tool for the functional investigation of N-glycans and glycoprotein synthesis. Our data suggest that knockdown of Mgat5 inhibits breast cancer cells’ growth with activation of CD4+ T cells and macrophages.

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confidence: 70%

Knockdown of Mgat5 Inhibits Breast Cancer Cell Growth with Activation of CD4+ T Cells and Macrophages

et al. 2008

The Journal of Immunology

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“…S6B). The mature form of ITGB1 showed the same reduction, but persisted longer that the newly synthesized form, apparently because of the fact that it is glycosylated and, thus, more stable than the nascent ITGB1 polypeptide (25). After 9 h of incubation with 10 g/ml cycloheximide (a lower concentration of the drug was necessary to avoid cell death), the mature ITGB1 (upper band) started diminishing as well.…”

Section: Expression Of Mrad9 Restores Migration and Invasion Potentiamentioning

confidence: 91%

Rad9 Protein Contributes to Prostate Tumor Progression by Promoting Cell Migration and Anoikis Resistance

Broustas

Zhu

Lieberman

2012

Journal of Biological Chemistry

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Background: Rad9, a cell cycle checkpoint and DNA repair protein, is functionally related to human prostate tumorigenesis. Results: Rad9 deletion in prostate cancer cells impairs migration and invasion, sensitizes to anoikis, and down-regulates integrin ␤1. Conclusion: Rad9 controls ITGB1 expression, migration, invasion, and anoikis resistance of prostate cancer cells. Significance: This study reveals the significance of Rad9 in prostate tumor migration and invasion.

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“…The protein A/G plus-agarose was purchased from Santa Cruz (Santa Cruz, CA, USA). The production of horseradish peroxidaselinked lectins Galanthus nivalis agglutinin (GNA) and wheat germ agglutinin (WGA) were performed as described previously [39].…”

Section: Cell Lines Antibodies and Reagentsmentioning

confidence: 99%

Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD

Zhou

et al. 2008

Glycoconj J

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The human E-cadherin is a single transmembrane domain protein involved in Ca(2+)-dependent cell-cell adhesion. In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded. In this study we investigated the molecular mechanism of E-cadherin, which lacks N-glycosylation at Asn-633 (M4), degradation and the role of the N-glycan at Asn-633 in E-cadherin folding. We treated cells stably expressed M4 E-cadherin with MG123, DMM, respectively. Either MG132 or DMM could efficiently block degradation of M4 E-cadherin. M4 E-cadherin was recognized as the substrate of ERAD and was retro-translocated from ER lumen to cytoplasm by p97. It was observed that the ration of M4 E-cadherin binding to calnexin was significantly increased compared with that of other variants, suggesting that it was a misfolded protein, though cytoplasmic domain of M4 E-cadherin could associate with beta-catenin. Furthermore, we found that N-glycans of M4 E-cadherin were modified in immature high mannose type, suggesting that it could not depart to Golgi apparatus. In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking.

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Increase in β1‐6 GlcNAc branching caused by N‐acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC‐7721

Cited by 27 publications

References 43 publications

Knockdown of Mgat5 Inhibits Breast Cancer Cell Growth with Activation of CD4+ T Cells and Macrophages

Knockdown of Mgat5 Inhibits Breast Cancer Cell Growth with Activation of CD4+ T Cells and Macrophages

Rad9 Protein Contributes to Prostate Tumor Progression by Promoting Cell Migration and Anoikis Resistance

Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD

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