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Articles by X. Zhu
Total Records ( 3 ) for X. Zhu
  J Du , Y Li and X. Zhu
 

CENP-F (also named mitosin) is a multifunctional protein of 350 kDa. In interphase, it is a nuclear protein, whereas in M phase it localizes to the kinetochore, the major microtubule-binding structure on chromosomes essential for chromosome segregation. CENP-F is also critical for myocyte differentiation through the interaction with Rb. It binds to ATF4 and negatively regulates the transcriptional activity of ATF4. It is also important for mitotic progression. Here we show that depletion of CENP-F by RNAi markedly downregulated the methylation of histone H3 at K4 and K9. Consistently, association of HP1 with mitotic chromosomes was largely decreased. These results uncover a novel role of CENP-F in regulation of epigenetic modification on histone H3.

  J Du , Y Zhang , Y Liu , Y Li and X. Zhu
 

Cenp-F (also named mitosin) is a 350-kDa human kinetochore protein important for the mitotic progression. It is also a nuclear matrix protein in interphase cells. Here, we showed that overexpression of N-terminal deletion mutants of Cenp-F containing the C-terminal 112 residues induced chromatin condensation into numerous aggregates of varying sizes in interphase nucleus, colocalizing with the exogenous proteins. In situ hybridization using whole chromosome painting probes indicated that the chromatin aggregates were not prematurely condensed individual chromosomes. Neither were they due to apoptosis. We provided evidence showing association of Cenp-F with certain regions of interphase chromatin fibers. Cenp-F associated with the DNA-dependent protein kinase (DNA-PK), a trimeric protein complex critical for genome homeostasis. Moreover, the DNA-PK association activity of Cenp-F mutants correlated with their ability to induce chromatin aggregation. These results imply a role of Cenp-F in organization of interphase chromatin through association and possibly regulation of DNA-PK.

  K. Xiao , X. Zhu , K.M. Peng , N. Wang and H. Song
  The purpose of this study was to elucidate the function of visfatin in the mucosal immune barrier of weaned piglets by observing histological changes in the small intestine and visfatin expression in LPS-induced piglets. The mucosal structure of the small intestine was damaged. The duodenum, jejunum, ileum and the intestinal villous were atrophied and shorter. Epithelial lymphocytes and lamina propria lymphoid tissue was reduced and aggregates of lymphoid nodules were increased. Visfatin-positive products were expressed in the small intestinal mucosa and mainly distributed in lamina propria lymphoid tissue. After LPS administration, visfatin-positive cells were reduced in the epithelial lymphocytes, lamina propria and intestinal gland but increased in aggregates lymphoids. This study suggested that an LPS-induced immune stress model could induce structural changes of piglet small intestine and cause changes of intestinal mucosal immune barrier function. In addition, the distribution and quantity of visfatin-positive cells were altered, suggesting visfatin is involved in the humoral immune responses of piglets.
 
 
 
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