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Wnt/β-连环蛋白信号通路下调 N-乙酰氨基葡萄糖基转移酶 III 的表达:两种相互排斥的调控途径的意义。

Wnt/beta-catenin signaling down-regulates N-acetylglucosaminyltransferase III expression: the implications of two mutually exclusive pathways for regulation.

机构信息

Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai Miyagi 981-8558, Japan.

出版信息

J Biol Chem. 2011 Feb 11;286(6):4310-8. doi: 10.1074/jbc.M110.182576. Epub 2010 Nov 29.

Abstract

In previous studies, we reported that N-acetylglucosaminyltransferase III (GnT-III) activity and the enzyme product, bisected N-glycans, both were induced in cells cultured under dense conditions in an E-cadherin-dependent manner (Iijima, J., Zhao, Y., Isaji, T., Kameyama, A., Nakaya, S., Wang, X., Ihara, H., Cheng, X., Nakagawa, T., Miyoshi, E., Kondo, A., Narimatsu, H., Taniguchi, N., and Gu, J. (2006) J. Biol. Chem. 281, 13038-13046). Furthermore, we found that α-catenin, a component of the E-cadherin-catenin complex, was also required for this induction (Akama, R., Sato, Y., Kariya, Y., Isaji, T., Fukuda, T., Lu, L., Taniguchi, N., Ozawa, M., and Gu, J. (2008) Proteomics 8, 3221-3228). To further explore the molecular mechanism of this regulation, the roles of β-catenin, an essential molecule in both cadherin-mediated cell adhesion and canonical Wnt signaling, were investigated. Unexpectedly, shRNA knockdown of β-catenin resulted in a dramatic increase in GnT-III expression and its product, the bisected N-glycans, which was confirmed by RT-PCR and GnT-III activity and by E4-PHA lectin blot analysis. The induction of GnT-III expression increased bisecting GlcNAc residues on β1 integrin, which led to down-regulation of integrin-mediated cell adhesion and cell migration. Immunostaining showed that nuclear localization of β-catenin was greatly suppressed; intriguingly, the knockdown of β-catenin in the nuclei was more effective than that in cell-cell contacts in the knockdown cells, which was also confirmed by Western blot analysis. Stimulation of the Wnt signaling pathway by the addition of exogenous Wnt3a or BIO, a GSK-3β inhibitor, consistently and significantly inhibited GnT-III expression and its products. Conversely, the inhibition of β-catenin translocation into the nuclei increased GnT-III activation. Taken together, the results of the present study are the first to clearly demonstrate that GnT-III expression may be precisely regulated by the interplay of E-cadherin-catenin complex-mediated cell-cell adhesion and Wnt/β-catenin signaling, which are both crucial in the process of epithelial-mesenchymal transitions in physiological and pathological conditions.

摘要

在之前的研究中,我们报道了 N-乙酰氨基葡萄糖基转移酶 III(GnT-III)活性和酶产物双分支 N-聚糖在细胞在 E-钙粘蛋白依赖性方式下在密集培养条件下被诱导(Iijima,J.,Zhao,Y.,Isaji,T.,Kameyama,A.,Nakaya,S.,Wang,X.,Ihara,H.,Cheng,X.,Nakagawa,T.,Miyoshi,E.,Kondo,A.,Narimatsu,H.,Taniguchi,N.,和 Gu,J.(2006)J. Biol. Chem. 281,13038-13046)。此外,我们发现 E-钙粘蛋白-catenin 复合体能的一个组成部分 α-连环蛋白(α-catenin)对于这种诱导也是必需的(Akama,R.,Sato,Y.,Kariya,Y.,Isaji,T.,Fukuda,T.,Lu,L.,Taniguchi,N.,Ozawa,M.,和 Gu,J.(2008)Proteomics 8,3221-3228)。为了进一步探讨这种调节的分子机制,研究了 β-连环蛋白(β-catenin)的作用,β-连环蛋白是钙粘蛋白介导的细胞黏附和经典 Wnt 信号传导所必需的分子。出乎意料的是,β-连环蛋白的 shRNA 敲低导致 GnT-III 表达及其产物双分支 N-聚糖的显著增加,这通过 RT-PCR 和 GnT-III 活性以及 E4-PHA 凝集素印迹分析得到证实。GnT-III 表达的诱导增加了 β1 整联蛋白上的双分支 GlcNAc 残基,导致整联蛋白介导的细胞黏附和细胞迁移的下调。免疫染色显示β-连环蛋白的核定位大大受到抑制;有趣的是,β-连环蛋白在核内的敲低比在细胞间接触中的敲低更有效,这也通过 Western blot 分析得到证实。外源性 Wnt3a 或 BIO(GSK-3β 抑制剂)的添加刺激 Wnt 信号通路,一致且显著抑制 GnT-III 表达及其产物。相反,β-连环蛋白向核内的转移抑制增加了 GnT-III 的激活。综上所述,本研究的结果首次清楚地表明,GnT-III 的表达可能受到 E-钙粘蛋白-catenin 复合体能介导的细胞-细胞黏附和 Wnt/β-连环蛋白信号传导的相互作用的精确调节,这两者在生理和病理条件下上皮-间充质转化过程中都是至关重要的。

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