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Articles by Wei Xie
Total Records ( 3 ) for Wei Xie
  Guang-Hua Xie , Wei Xie , Heyun Piao and Dan Li
  Background and Objective: Cyanidin-3-glucoside (C3G) is one of the major bioactive compounds in anthocyanins, which have been shown to prevent a large spectrum of diseases. It has been reported that hypoxia is a common characteristic of many types of solid tumor and that the hypoxia-inducible factor 1α (HIF-1α) plays an important role in the process of angiogenesis and metastasis in cancer cells. The objective of this study was to explore the effects of C3G on HIF-1α activation in cholangiocarcinoma (CCA) cells. Materials and Methods: The human cholangiocarcinoma cell line QBC939 was used in this study. Hypoxic conditions were achieved by using the chemical hypoxia agent cobalt chloride or incubation at 1% O2. and MTT assay, Luciferase reporter assay, flow cytometric apoptosis assay, western blot, RT-PCR and immuno fluorescence methods were used to determine the C3G efficacy. Results: C3G markedly decreased the hypoxia-induced accumulation of HIF-1α reporter activity and protein expression in a dose-dependent manner and exerted a large apoptotic effect in CCA cells. Furthermore, C3G reduced expression of several genes downstream of HIF-1α, such as vascular endothelial growth factor and erythropoietin, without affecting the expression level of HIF-1α mRNA, thus indicating that C3G acts as an inhibitor of HIF-1α mRNA translation. Conclusion: This study provides a novel strategy to develop a low toxicity, high efficiency and multi-target natural active substance for the treatment of cancers.
  Mei Zhu , Fengsong Wang , Feng Yan , Phil Y. Yao , Jian Du , Xinjiao Gao , Xiwei Wang , Quan Wu , Tarsha Ward , Jingjing Li , Steve Kioko , Renming Hu , Wei Xie , Xia Ding and Xuebiao Yao
  Chromosome segregation in mitosis is orchestrated by dynamic interaction between spindle microtubules and the kinetochore. Septin (SEPT) belongs to a conserved family of polymerizing GTPases localized to the metaphase spindle during mitosis. Previous study showed that SEPT2 depletion results in chromosome mis-segregation correlated with a loss of centromere-associated protein E (CENP-E) from the kinetochores of congressing chromosomes (1). However, it has remained elusive as to whether CENP-E physically interacts with SEPT and how this interaction orchestrates chromosome segregation in mitosis. Here we show that SEPT7 is required for a stable kinetochore localization of CENP-E in HeLa and MDCK cells. SEPT7 stabilizes the kinetochore association of CENP-E by directly interacting with its C-terminal domain. The region of SEPT7 binding to CENP-E was mapped to its C-terminal domain by glutathione S-transferase pull-down and yeast two-hybrid assays. Immunofluorescence study shows that SEPT7 filaments distribute along the mitotic spindle and terminate at the kinetochore marked by CENP-E. Remarkably, suppression of synthesis of SEPT7 by small interfering RNA abrogated the localization of CENP-E to the kinetochore and caused aberrant chromosome segregation. These mitotic defects and kinetochore localization of CENP-E can be successfully rescued by introducing exogenous GFP-SEPT7 into the SEPT7-depleted cells. These SEPT7-suppressed cells display reduced tension at kinetochores of bi-orientated chromosomes and activated mitotic spindle checkpoint marked by Mad2 and BubR1 labelings on these misaligned chromosomes. These findings reveal a key role for the SEPT7-CENP-E interaction in the distribution of CENP-E to the kinetochore and achieving chromosome alignment. We propose that SEPT7 forms a link between kinetochore distribution of CENP-E and the mitotic spindle checkpoint.
  Yong Yang , Fang Wu , Tarsha Ward , Feng Yan , Quan Wu , Zhaoyang Wang , Tanisha McGlothen , Wei Peng , Tianpa You , Mingkuan Sun , Taixing Cui , Renming Hu , Zhen Dou , Jingde Zhu , Wei Xie , Zihe Rao , Xia Ding and Xuebiao Yao
  Chromosome movements in mitosis are orchestrated by dynamic interactions between spindle microtubules and the kinetochore, a multiprotein complex assembled onto centromeric DNA of the chromosome. Here we show that phosphorylation of human HsMis13 by Aurora B kinase is required for functional kinetochore assembly in HeLa cells. Aurora B interacts with HsMis13 in vitro and in vivo. HsMis13 is a cognate substrate of Aurora B, and the phosphorylation sites were mapped to Ser-100 and Ser-109. Suppression of Aurora B kinase by either small interfering RNA or chemical inhibitors abrogates the localization of HsMis13 but not HsMis12 to the kinetochore. In addition, non-phosphorylatable but not wild type and phospho-mimicking HsMis13 failed to localize to the kinetochore, demonstrating the requirement of phosphorylation by Aurora B for the assembly of HsMis13 to kinetochore. In fact, localization of HsMis13 to the kinetochore is spatiotemporally regulated by Aurora B kinase, which is essential for recruiting outer kinetochore components such as Ndc80 components and CENP-E for functional kinetochore assembly. Importantly, phospho-mimicking mutant HsMis13 restores the assembly of CENP-E to the kinetochore, and tension developed across the sister kinetochores in Aurora B-inhibited cells. Thus, we reason that HsMis13 phosphorylation by Aurora B is required for organizing a stable bi-oriented microtubule kinetochore attachment that is essential for faithful chromosome segregation in mitosis.
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