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| 1 | Lipid-associated membrane proteins of Mycoplasma penetrans induce production of proinflammatory cytokines in human monocytic cells显示文摘The aim of this study is to explore potential pathogenicity of Mycoplasma penetrans, and to investigate whether M.penetrans lipid-associated membrane proteins (LAMPs) could induce human monocytic cell line (THP-1) to produce some proinflammatory cytokines in vitro, including interleukin-1β(IL-1β) , tumor necrosis factor alpha (TNF-α) , and IL-8. THP-1 was stimulated with different concentrations of M .penetrans LAMPs and at different time to analyze the production of human IL-1β, TNF-αand IL-8. The protein levels of human IL-1β, TNF-αand IL-8 were measured by enzyme-linked immunoadsorbent assay (ELISA) and the mRNA levels of these proinflamrnatory cytokines were detected by reverse transcriptase -PCR (RT-PCR). It was demonstrated in the present study that the production of IL-1β, TNF-αand IL-8 increased in dose- and time-dependent manner after stimulation with M. penetrans LAMPs in THP-1 cells. M.penetrans LAMPs also induced the expression of IL-1β, TNF-αand IL-8 mRNA. The production of IL-1β, TNF-αand IL-8 and the expression of mRNA were down-regulated by pyrrolidine dithiocarbamate (PDTC). This study demonstrated that M. penetrans LAMPs can induce the production of proinflammatory cytokines in human monocytic cells in vitro, thus suggesting that it may be an important etiological factor. | YI MOU WU MIN JUN YU LI ZHI TAN XIAO XING YOU | 2006 | Journal of Microbiology and Immunology2006，4，4： | 3 |
| 2 | Eukaryotic expression of outer membrane protein Gpd from Treponema pallidum and preliminary studies on its immune response in rabbits显示文摘The Gpd gene was amplified from the genomic DNA of Treponema pallidum and cloned into the appropriate site of pcDNA3.1(+) vector. The expression of pcDNA3.1(+)-Gpd in HeLa cells was tested with Western blotting and technology of immunocytochemistry. New Zealand rabbits were immunized with the eukaryotic expression recombinant pcDNA3.1(+)-Gpd. A fusion protein of Gpd with 4.1 kDa has been effectively expressed in HeLa cells, which were detected by Western blotting and the immunocytochemistry techniques. The New Zealand rabbits were able to elicit the specific antibody after immunization with the nucleic acid vaccine. The antibody titer could reach as high as 1∶1024 after 2 weeks of the third injection; and the splenocytes proliferated evidently due to the Gpd protein stimulation. Both the antibody titer and the splenocytes proliferation were higher substantially than those of controls (P<0.01). All above data will contribute to an experimental basis of further study of the biological function of Gpd protein as well as DNA vaccine for syphilis. | FEI JUN ZHAO YI Mou WU XIAO HONG ZHANG SnUANG QUAN LIU MIN JUN YU LI SHENG ZHAN | 2005 | Journal of Microbiology and Immunology2005，3，2： | 2 |
| 3 | Study on collision avoidance in busy waterways by using AIS data显示文摘 | Jun Min Mou Cees van der Tak Han Ligteringen | 2010 | Ocean Engineering2010，，5： | 1 |
| 4 | Study on collision avoidance in busy waterways by using AIS data显示文摘 | Jun Min Mou Cees van der Tak Han Ligteringen | 2010 | Ocean Engineering2010，37，5： | 1 |
| 5 | Expression and functional identification of the hypothetical adhesin P32 from Mycoplasma genitalium显示文摘Mycoplasma genitalium is the main causative agent for non-gonococcal and non-chlamydial urethritis. P32 is the putative surface-exposed membrane protein of M. genitalium and it has substaintial identity in amino acid sequence with adhesin protein P30 from M. pnewnoniae. Since M. pneumoniae mutants lacking P30 protein is defective in cytadherence, P32 protein has been proposed to be an essential adhesin implicated in the adherence of M. genitalium to host cells. The prokaryotic expression vector pET-30 ( + )/p32 was constructed in the present study, and the recombinant protein was expressed in E. coli and purified under denaturing condition. As demonstrated by the immunoblotting analysis, the recombinant protein could react with rabbit antisera against M. genitalium, and adherence inhibition assays were petformed with antisera against this recombinant protein. It was demonstrated that P32 protein apperared to be an adhesion protein of M. genitalium, thus providing the experimental basis for better understanding of the pathogenesis of M. genitalium infection and for the development of the related vaccines against the infection. | LIN BO LI YI MOU WU WEN BO ZHANG MIN JUN YU | 2006 | Journal of Microbiology and Immunology2006，4，3： | 0 |
| 6 | Expression of inducible nitric oxide synthase induced by lipid-associated membrane proteins of Ureaplasma urealyticum is regulated by nuclear factor κB-mediated mechanism in murine macrophages显示文摘The aim was to investigate the molecular mechanisms responsible for the inducible nitric oxide synthase (iNOS) gene expression stimulated by lipid associated membrane proteins (LAMPs) of Ureaplasma urealyticum (U.urealyticum). Detection of NO, the expression of iNOS and the activation of nuclear factor κB (NF-κB) in direct response to U.urealyticum LAMPs in a murine macrophages, the effects of pyrrolidine dithiocarbamate (PDTC), an inhibitor of NF-κB and of cycloheximide (CHX), a protein synthase inhibitor were available. The results indicated that U.urealyticum LAMPs stimulated mouse macrophages to express iNOS and thus produce NO in dose- and time-dependent manner by activating NF-κB. The expression of iNOS, NO production and the activation of NF-κB were inhibited by U.urealyticum LAMPs combination with PDTC or CHX. In conclusion, our findings suggest that U.urealyticum may be an etiological factor to certain diseases due to its ability to stimulate the expression of iNOS, which is probably mediated through the activation of NF-κB. | ZHONG LIANG DENG YI MOU WU YAN HUA ZENG LI LI CHEN MIN JUN YU | 2005 | Journal of Microbiology and Immunology2005，3，4： | 0 |
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