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

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 urealytictan （ 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.

Distinct effects of nuclear membrane localization on gene transcription silencing in Drosophila S2 cells and germ cells

Nuclear envelope proteins have important roles in chromatin organization and signal-dependent transcriptional regulation. A previous study reported that the inner nuclear membrane protein, Otefin （Ote）, was essential for germline stem cell （GSC） maintenance via interaction with Smad complex. The interaction of Ore with the Smad complex recruits the barn locus to the nuclear periphery and subsequently results in bam transcriptional silencing, revealing that nuclear peripheral localization is essential for barn gene regulation. However, it remains unknown whether the nuclear peripheral localization is sufficient for barn silencing. To address this issue, we have established a tethering system, in which the Gal4 DNA binding domain （DBD） of the Flag：Gal4 DBD：Ote△LEM fusion protein physically interacts with the Gal4 binding sites upstream of bamP-gfp to artificially recruit the reporter gene gfp to the nuclear membrane. Our data demonstrated that the nuclear peripheral localization seemed to affect the expression of the target naked gene in S2 ceils. By contrast, in Drosophila germ cells, the nuclear membrane localization was not sufficient for gene silencing.