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Liu X.,Tianjin Medical University | Liu X.,Tianjin Key Laboratory of Cellular and Molecular Immunology | Liu X.,Key Laboratory of Educational Ministry of China | Dong L.,Tianjin Medical University | And 27 more authors.
Cellular and Molecular Immunology | Year: 2011

The multifunctional protein p100 is a vital transcriptional regulator that increases gene transcription by forming a physical bridge between promoter-specific transcription factors and the basal transcription machinery. To identify potential signal transduction pathways in which human p100 acts as a coregulator and to find target promoter regions that may interact with p100, we performed a promoter microarray assay called chromatin immunoprecipitation- guided ligation and selection (ChIP-GLAS). From this assay, we determined that a set of promoter fragments, including several factors in the transforming growth factor beta (TGF-β) signaling pathway, exhibited interaction with p100. The ChIP-GLAS data were validated by RT-PCR assessing the mRNA expression of various factors in the TGF-β signaling pathway in cell lines. © 2011 CSI and USTC. All rights reserved.

Wang X.,Tianjin Medical University | Wang X.,Key Laboratory of Educational Ministry of China | Liu X.,Tianjin Medical University | Liu X.,Key Laboratory of Educational Ministry of China | And 12 more authors.
Anatomical Record | Year: 2010

The family of STAT proteins consists of seven members that mediate highly specific functions in cytokine signaling. STAT6 is a critical regulator of transcription for interleukin-4 (IL-4)-induced genes. Activation of gene expression involves recruitment of coactivator proteins that function as bridging factors connecting sequence-specific transcription factors to the basal transcription machinery, and as chromatin-modifying enzymes. In this report, we show that the coacitivator p100 protein can interact with STAT6 through its SN domain both in vivo and in vitro, resulting in enhancement of STAT6-mediated gene transcriptional acitivation. Consistent with our previous reports, we identified intracellular localization of p100 and STAT-6 by confocal microscopy examined in response to IL-4. Moreover, in consideration of STAT molecules sharing significant homology in structure and function, we detected whether p100 can associate with STAT-1. In conclusion, this study found no evidence that p100 functions as a transcriptional coactivator for STAT1-dependent gene regulation. © 2010 Wiley-Liss, Inc.

Wang F.,Tianjin Medical University | Chang G.,Tianjin Medical University | Geng X.,Tianjin Medical University | Geng X.,Tianjin Key Laboratory of Cellular and Molecular Immunology | Geng X.,Key Laboratory of Educational Ministry of China
PLoS ONE | Year: 2014

Vascular dementia (VaD) is a mental disorder caused by brain damage due to cerebrovascular disease, and incidence of VaD is rising. To date, there is no known effective cure for VaD, so effort in developing an effective treatment for VaD is of great importance. The differentiation plasticity of BMSCs, in conjunction with its weak immunogenicity, makes manipulated BMSCs an attractive strategy for disease treatment. However, BMSCs often display disabled differentiation, premature aging, and unstable proliferation, reducing their neuroprotective function. These problems may be caused by the lack of telomerase activity in BMSCs. Our results show that NGF-TERT co-transfected BMSCs have a better therapeutic effect than BMSCs lacking NGF and TERT expression, demonstrated by significant improvements in learning and memory in VaD rats. The underlying mechanism might be increased expression of NGF, TrkA and SYN in the hippocampal CA1 area, which has potential implication in advancing therapeutics for VaD. © 2014 Wang et al.

Liu X.Y.,Ministry of Health Key Laboratory of Hormone and Development | Liu X.Y.,Tianjin Medical University | Ge L.,Tianjin Medical University | Ge L.,Tianjin Key Laboratory of Cellular and Molecular Immunology | And 3 more authors.
International Journal of Clinical and Experimental Medicine | Year: 2014

Purpose: In the present study, we constructed an efficient expression system for visfatin and identified the peptide sequences which binding to visfatin. Methods and results: The fusion protein was identified by SDS-PAGE and Western blot. The yield of visfatin was 300 mg/L culture medium with optimal conditions. The recombinant visfatin binds with insulin receptor with a dose-dependent effect. All of the 24 sequence identified by ELISA were able to bind to visfatin specifically. Among the 24 DNA sequences, there were 8 clones of AAKTPTE, 4 clones of ATTVPAS and 4 clones of MSLQQEH. Conclusion: The sequence of AA(X)TPT(X) was the most frequently existed sequence in all of sequences analyzed, which suggests that AA(X)TPT(X) is likely to be the essential motif in peptides which visfatin could bind with. © 2014, Int J Clin Exp Med.All right reserved.

Zhi L.,Peking Union Medical College | Zhi L.,Tianjin Medical University | Zhi L.,Tianjin Key Laboratory of Cellular and Molecular Immunology | Zhi L.,Key Laboratory of Educational Ministry of China | And 12 more authors.
Oligonucleotides | Year: 2011

G-rich oligonucleotides (GROs) can inhibit cell proliferation by inducing cell cycle arrest at S phase in tumor cell lines. GROs bind specific cellular proteins, such as nucleolin, a crucial protein interacting with P53; however, little is known about the relationship between GROs and P53. In this study, we have shown that GROs inhibited the proliferation of U937 cells (a human monocytic leukemia cell line without P53 expression) by inducing S-phase arrest. We also showed that GRO colocalized with nucleolin in U937 cells. GRO treatment induced alteration of a series of cell cycle regulatory proteins in U937 cells. Increased Cdk2 expression might promote the cells to enter S phase and subsequent decrease of Cdk2 might induce cell cycle arrest in S phase. Transfection of U937 cells with a wild-type p53 gene caused the formation of nucleolin-P53 complex, which alleviated the effect of GRO on leukemia cells. This alleviated effect is probably due to the decreased uptake of GRO. © 2011, Mary Ann Liebert, Inc. 2011.

Wang F.,Tianjin Medical University | Chang G.-M.,Tianjin Medical University | Geng X.,Tianjin Medical University | Geng X.,Tianjin Key Laboratory of Cellular and Molecular Immunology | Geng X.,Key Laboratory of Educational Ministry of China
European Review for Medical and Pharmacological Sciences | Year: 2014

OBJECTIVES: Alternative splicing of human telomerase reverse transcriptase (hTERT) has an important effect on regulating telomerase activity. Exonic splicing enhancers (ESEs) are a family of conserved splicing factors that participate in multiple steps of the splicing pathway. Our aim is to analyze the ESEs for predicting the potential regulatory elements of hTERT mRNA splicing. MATERIALS AND METHODS: Enter the FASTA format of hTERT total sequences or individual exon as the input data in the main interface of ESEfinder3.0 and ESEfinder2.0 program. Analyze the data of output results and compare the differences between ESEfinder3.0 and ESEfinder2.0 program. RESULTS: Five ESEs were predicted in exon 5 to exon 9 of hTERT. They were at position 108 located in hTERT exon 5, at position 92 located in exon 6, at position 22 located in exon 7, at position 73 located in exon 8 and at position 5 located in exon 9. There were no differences between ESEfinder 3.0 and ESEfinder 2.0 in our case. CONCLUSIONS: The identification of these potential ESEs of hTERT might be helpful for the design of antisense oligonucleotides, which could modulate hTERT alternative splicing and inhibit telomerase activity.

Gao X.,Tianjin Medical University | Gao X.,Tianjin Key Laboratory of Cellular and Molecular Immunology | Gao X.,Key Laboratory of Educational Ministry of China | Ge L.,Tianjin Medical University | And 23 more authors.
FEBS Letters | Year: 2010

SGs are mRNA containing cytoplasmic structures that are assembled in response to stress. Tudor-SN protein is a ubiquitously expressed protein. Here, Tudor-SN protein was found to physiologically interact with G3BP, which is the marker and effector of SG. The kinetics of the assembly of SGs in the living cells demonstrated that Tudor-SN co-localizes with G3BP and is recruited to the same SGs in response to different stress stimuli. Knockdown of endogenous Tudor-SN did not inhibit the formation of SGs, but retarded the aggregation of small SGs into large SGs. Thus Tudor-SN may not be an initiator as essential as G3BP for the formation of SGs, but affects the aggregation of SGs. These findings identify Tudor-SN as a novel component of SGs. © 2010 Federation of European Biochemical Societies.

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