Escherichia coli maltose-binding protein (MBP) activates mouse Th1 through TLR2-mediated MyD88-dependent pathway and TLR4-mediated TRIF-dependent pathway.

MBP (maltose-binding protein) is a component of Escherichia coli. Our previous study found that MBP directly induces the activation of Th1 (T helper type 1), but the molecular mechanism remains unclear. In the present study, CD4T cells were purified from the spleens of normal mice using antibody-coated immunomagnetic beads by negative selection.

The Combination of MBP and BCG-Induced Dendritic Cell Maturation through TLR2/TLR4 Promotes Th1 Activation In Vitro and Vivo.

To explore whether TLR2/TLR4 could be involved in the maturation of dendritic cells and polarization of CD4 T cells induced by dendritic cells stimulated with MBP and BCG, in vitro and in vivo experiments using TLR2 or TLR4 mice were employed. MBP and BCG elevated CD80, CD86 and MHC class II expressed on dendritic cells and increased IL-12 protein, induced DC maturation, and indirectly promoted Th1 activation. Moreover, MBP and BCG upregulated costimulatory molecules on DCs in a TLR2- and TLR4-dependent manner.

Targeting MUC1 and JNK by RNA interference and inhibitor inhibit the development of hepatocellular carcinoma.

Mucin 1 (MUC1), as an oncogene, is overexpressed in hepatocellular carcinoma (HCC) cells and promotes the progression and tumorigenesis of HCC through JNK/TGF-β signaling pathway. In the present study, RNA interference (RNAi) and JNK inhibitor SP600125, which target MUC1 and/or JNK, were used to treat HCC cells in vitro, and the results showed that both silencing the expression of MUC1 and blocking the activity of JNK inhibited the proliferation of HCC cells. In addition, MUC1-stable-knockdown and SP600125 significantly inhibited the growth of tumors in the subcutaneous transplant tumor models that established in BALB/c nude mice rather than MUC1 or JNK siRNAs transiently transfection.

Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner.

Maltose-binding protein (MBP) is a critical player of the maltose/maltodextrin transport system in Escherichia coli. Our previous studies have revealed that MBP nonspecifically induces T helper type 1 (Th1) cell activation and activates peritoneal macrophages obtained from mouse. In the present study, we reported a direct stimulatory effect of MBP on RAW264.

Inhibitory effect of activin A on activation of lipopolysaccharide-stimulated mouse macrophage RAW264.7 cells.

Activin A is a member of transforming growth factor beta (TGF-beta) superfamily, which is also named restrictin-P, and can inhibit the secretion of nitric oxide (NO) and interleukin-1beta (IL-1beta) from LPS-activated mouse macrophages. In this study, the regulation effect and possible mechanism of activin A as an anti-inflammatory factor on lipopolysaccharide (LPS)-activated macrophages were investigated in vitro. It was observed that activin A could not only decrease the secretion of IL-1beta and NO, as well as the mRNA expressions of IL-1beta and iNOS, but also suppress the pinocytosis of mouse macrophage cell line RAW264.

Regulation of activin receptor-interacting protein 2 expression in mouse hepatoma Hepa1-6 cells and its relationship with collagen type IV.

Aim: To investigate the regulation of activin receptor-interacting protein 2 (ARIP2) expression and its possible relationships with collagen type IV (collagen IV) in mouse hepatoma cell line Hepal-6 cells.

Methods: The ARIP2 mRNA expression kinetics in Hepal-6 cells was detected by RT-PCR, and its regulation factors were analyzed by treatment with signal transduction activators such as phorbol 12-myristate 13-acetate (PMA), forskolin and A23187. After pcDNA3-ARIP2 was transfected into Hepal-6 cells, the effects of ARIP2 overexpression on activin type II receptor (ActRII) and collagen IV expression were evaluated.

Effects of activin A on the activities of the mouse peritoneal macrophages.

Activin A is a kind of pre-inflammatory factor that belongs to the transforming growth factor-beta (TGF-beta) superfamily. To investigate the effect and mechanism of activin A on the activities of mouse macrophages, the secretion of NO in the supernatant of cultured mouse peritoneal macrophages was examined by NO assay kit, and the expression of iNOS, ActRIIA and ARIP2 mRNA in mouse peritoneal macrophages was analyzed by RT-PCR. The results showed that activin A stimulated the secretion of NO and the expression of iNOS mRNA in non-activated mouse macrophages in a time- and dose-dependent manner.