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首页> 外文期刊>Cell Research >Blocking of N-acetylglucosaminyltransferase V induces cellular endoplasmic reticulum stress in human hepatocarcinoma 7721 cells.
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Blocking of N-acetylglucosaminyltransferase V induces cellular endoplasmic reticulum stress in human hepatocarcinoma 7721 cells.

机译：N-乙酰氨基葡萄糖氨基转移酶V的阻断在人肝癌7721细胞中诱导细胞内质网应激。

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摘要

N-acetylglucosaminyltransferase V (GnT-V) is an important tumorigenesis and metastasis-associated enzyme. To study its biofunction, the GnT-V stably suppressed cell line (GnT-V-AS/7721) was constructed from 7721 hepatocarcinoma cells in previous study. In this study, cDNA array gene expression profiles were compared between GnT-V-AS/7721 and parental 7721 cells. The data indicated that GnT-V-AS/7721 showed a characteristic expression pattern consistent with the ER stress. The molecular mechanism of the ER stress was explored in GnT-V-AS/7721 by the analysis on key molecules in both two unfolded protein response (UPR) pathways. For ATF6 and Ire1/XBP-1 pathway, it was evidenced by the up-regulation of BIP at mRNA and protein level, and the appearance of the spliced form of XBP-1. As for PERK/eIF2alpha pathway, the activation of ER eIF2alpha kinase PERK was observed. To confirm the results from GnT-V-AS/7721 cells, the key molecules in the UPR were examined again in 7721 cells interfered with the GnT-V bythe specific RNAi treatment. The results were similar with those from GnT-V-AS/7721, indicating that blocking of GnT-V can specifically activate ER stress in 7721 cells. Rate of (3)H-Man incorporation corrected with rate of (3)H-Leu incorporation in GnT-V-AS/7721 was down-regulated greatly compared with the control, which demonstrated the deficient function of the enzyme synthesizing N-glycans after GnT-V blocking. Moreover, the faster migrating form of chaperone GRP94 associated with the underglycosylation, and the extensively changed N-glycans structures of intracellular glycoproteins were also detected in GnT-V-AS/7721. These results supported the mechanism that blocking of GnT-V expression impaired functions of chaperones and N-glycan-synthesizing enzymes, which caused UPR in vivo.Cell Research (2006) 16: 82-92 doi:10.1038/sj.cr.7310011; published online 16 January 2006.
机译：N-乙酰氨基葡萄糖氨基转移酶V（GnT-V）是重要的肿瘤发生和转移相关酶。为了研究其生物学功能，在先前的研究中，从7721个肝癌细胞构建了GnT-V稳定抑制的细胞系（GnT-V-AS / 7721）。在这项研究中，比较了GnT-V-AS / 7721和亲代7721细胞的cDNA阵列基因表达谱。数据表明GnT-V-AS / 7721显示出与ER应力一致的特征表达模式。通过分析两种未折叠蛋白反应（UPR）途径中的关键分子，探索了GnT-V-AS / 7721中ER应激的分子机制。对于ATF6和Ire1 / XBP-1途径，这可以通过在mRNA和蛋白质水平上BIP的上调以及XBP-1剪接形式的出现来证明。至于PERK / eIF2alpha途径，观察到ER eIF2alpha激酶PERK的激活。为了确认来自GnT-V-AS / 7721细胞的结果，再次对UPR中的关键分子在通过特异性RNAi处理干扰GnT-V的7721细胞中进行了检查。结果与来自GnT-V-AS / 7721的结果相似，表明阻断GnT-V可以特异性激活7721细胞中的ER应激。与对照组相比，用GnT-V-AS / 7721中的（3）H-Leu掺入率校正的（3）H-Man掺入率大大降低，这表明酶合成N-聚糖的功能不足。在GnT-V封锁之后。此外，在GnT-V-AS / 7721中也检测到了与糖基化不足相关的伴侣蛋白GRP94的较快迁移形式，以及胞内糖蛋白的N-聚糖结构发生了广泛变化。这些结果支持了阻断GnT-V表达破坏伴侣蛋白和N-聚糖合成酶的功能的机制，其在体内引起UPR。CellResearch（2006）16：82-92 doi：10.1038 / sj.cr.7310011； Science，2006。在线发布于2006年1月16日。

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