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1. IL-37b inhibits the activation of T cells by inhibiting the activation of dendritic cells | |||
WU Wantong,SUN Zhina,FENG Xiaoming | |||
Biology 19 May 2016 | |||
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Abstract:In this paper Interleukin 37b (IL-37b) plays a key role in suppressing immune responses, partially by modulating the function of dendritic cells (DCs). However, the precise mechanisms are still largely unknown. Here, we investigated the effects of IL-37b on DC maturation and T cell responses induced by DCs, and explored the involved signaling pathways. It was found that IL-37b down-regulated the expressions of co-stimulatory molecules CD80 and CD86 on DCs in vitro. At the same time, the expressions of pro-inflammatory cytokines, such as TNF-α and IL-6, were suppressed, while the expression of the T cell inhibitory cytokine TGF-β was increased in IL-37b-treated DCs. In addition, the activation effect of DCs on T cells was impaired by IL-37b. We further revealed that extracellular single-regulated kinase (ERK), nuclear factor-κB (NF-κB), and mTOR-S6K signaling pathways were involved in the inhibition of DCs induced by IL-37b. This was confirmed by the similarly suppressive effect of chemical inhibitors against NF-κB, ERK, and S6K on the expressions of IL-6 and TNF-α in DCs. In conclusion, these results demonstrated that IL-37b suppressed DC maturation and immunostimulatory capacityin T cell priming by involving in ERK, NF-κB, and S6K-based inhibitory signaling pathways. | |||
TO cite this article:WU Wantong,SUN Zhina,FENG Xiaoming. IL-37b inhibits the activation of T cells by inhibiting the activation of dendritic cells[OL].[19 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4690228 |
2. Caldesmon Phosphorylation Plays a Key Role in Tumor Metastasis | |||
JIANG Qifeng,XIONG Xingliang | |||
Biology 18 May 2016 | |||
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Abstract:In this paper, we have performed transwell migration assays and contractility measurements by traction microscopy using human breast cancer cell lines MDA MB-231 and MCF-7, transfected with wild-type or mutated CaD. We found that cells expressing the A1234 mutant of CaD exhibited most robust contractile activity, the effect being more profound in MDA-MB231 cells than in MCF-7 cells, whereas the same mutant resulted in most severely hampered migration in both types of cells. These mutant cells also exhibited enhanced stress fibers and delayed trypsin-induced detachment from substratum. Taken together, phosphorylation of CaD appears to have an opposite effect on cell migration and contractility. Cells with extensive and dynamic CaD phosphorylation favor motile activities. Unphosphorylated CaD facilitates stable actin filaments, which is needed to support cell contractility, but could stifle cell movement if irreversible. The observed difference between the two tumor cell lines may thus reflect their different intrinsic kinase activities. The metastatic MDA-MB231 cells have higher levels of CaD and more active kinases than the non-metastatic MCF-7 cells. An elevated amount of phosphorylated CaD contributes to cell migration and invasion. Our findings not only shed light on the mechanism by which CaD regulates cell motility, but also provide new insights into the nature of metastasis of cancer cells. | |||
TO cite this article:JIANG Qifeng,XIONG Xingliang. Caldesmon Phosphorylation Plays a Key Role in Tumor Metastasis[OL].[18 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4689102 |
3. The Biochemical Characterization of the Interaction between Ca2+-CaM and NINAC | |||
YOU Xia,LIU Haiyang,LIU Wei | |||
Biology 18 May 2016 | |||
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Abstract:The Drosophila visual cascade is the fastest G-protein-coupled signaling pathways, involving the opening of TRP/TRPL channels and the influx of Ca2+ ion. NINAC (neither inactivation nor afterpotential C) is a member of class III myosins, specially localizing in photoreceptor cell and playing a significant role in termination of Drosophila visual signal transduction. There are two isoforms of NINAC: p132 and p174, which share a protein kinase catalytic domain (kinase domian), a motor domain, but differ in their C-terminal region which contains calmodulin-binding domains (IQ motif). These two isoforms have remarkable difference in localization and calmodulin (CaM) binding capability. The interaction between IQ motif and CaM is very important: the mutations in NINAC impairing of CaM binding will lead to defects in visual signal transduction. By using the analytical gel-filtration, isothermal titration calorimetry (ITC), size exclusion chromatography and multi-angle laser light scattering (SEC-MALS), we systematically characterized the interaction between CaM and NINAC IQ motifs. We found that p174 could bind two Ca2+-CaMs whereas p132 could only bind one Ca2+-CaM. By mutagenesis experiments, we also showed that the minor sequence differences in IQ2 between p174 and p132 cause this CaM binding difference. Our finding will contribute to the further functional studies of NINAC's regulation by CaM. | |||
TO cite this article:YOU Xia,LIU Haiyang,LIU Wei. The Biochemical Characterization of the Interaction between Ca2+-CaM and NINAC[OL].[18 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4689798 |
4. Cloning and expression analysis of LeMYC gene in Lithospermum Erythrorhizon | |||
Hu Zhao,Jinliang Qi,Yonghua Yang | |||
Biology 17 May 2016 | |||
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Abstract:LeMYC is a novel member of the basic helix-loop-helix (bHLH) family that was cloned from Lithospermum erythrorhizon by using rapid amplification of cDNA ends method. Bioinformatics analyses showed that the predicted LeMYC protein contained a potential bHLH domain and was highly homologous to AtMYC2 from Arabidopsis thaliana. The promoter of LeMYC was further cloned to analyze its expression pattern, and sequence analysis revealed a number of potential regulatory motifs related to tissue-specific gene expression and abiotic and biotic stress responses. Real-time PCR results suggested that LeMYC was significantly induced transiently during the early stage when L. erythrorhizon cells were transferred from a B5 to an M9 medium to form shikonin. Exogenous methyl jasmonate (MeJA), an effective inducer of shikonin accumulation, also remarkably induced the rapid LeMYC expression. By contrast, ibuprofen (IBU), an inhibitor of jasmonate biosynthesis, significantly inhibited LeMYC expression. Tissue-specific expression analysis showed that LeMYC mRNA predominantly accumulated in the roots where shikonin was biosynthesized. These results indicated that LeMYC gene could be a novel member of the bHLH gene family and may have an important function in shikonin formation. | |||
TO cite this article:Hu Zhao,Jinliang Qi,Yonghua Yang. Cloning and expression analysis of LeMYC gene in Lithospermum Erythrorhizon[OL].[17 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4690111 |
5. Bioactive silicate materials for bone regeneration | |||
LI Haiyan | |||
Biology 16 May 2016 | |||
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Abstract:The demanding for bioactive materials to repair or regenerate bone has being growing fast. Silicate-based bioactive materials have attracted much attention in the last ten years due to their excellent biological response in vitro and in vivo. This chapter introduces the design methods for silicate-based bioglass and silicate-based ceramics materials. Strategies about structure design and composition design for these two types of materials and the subsequent enhanced properties of the designed materials have been introduced in detail. | |||
TO cite this article:LI Haiyan. Bioactive silicate materials for bone regeneration[OL].[16 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4689726 |
6. Identification of two dazl splicing variants in Japanese flounder (Paralichthys olivaceus) | |||
WANG Xubo,JIANG Jiajun,ZHANG Quanqi | |||
Biology 16 May 2016 | |||
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Abstract:DAZL is an RNA-binding protein of DAZ family, playing key roles in reproduction of organisms. Here in this study, we clone and identify the dazl gene in a kind of flatfish, Japanese flounder (Paralichthys olivaceus). Two different splicing variants of dazl mRNAs are found, and they differ from each other by a 51-bp insertion/deletion. We characterize the two mRNA variants by qPCR and in situ hybridization and prove their germ cell specific expression patterns. Results of western blot and immunohistochemistry show that the two isoforms of their translational production also express specifically in germ cells of both sexes. The similar expression patterns of the two variants may imply their complementary functions in germ cell development. But there are also differences in their functions. By RNA-binding protein immunoprecipitation, we find Podazl-I and Podazl-II may be the target of both PODAZL isoforms. More sequencing results will offer more detailed and accurate information on their functions. Studies on the two dazl variants in Japanese flounder are rare in teleosts. Our results may facilitate further studies on reproduction related genes and germ cell development. | |||
TO cite this article:WANG Xubo,JIANG Jiajun,ZHANG Quanqi. Identification of two dazl splicing variants in Japanese flounder (Paralichthys olivaceus)[OL].[16 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4689150 |
7. Ghrelin reduces A-type potassium channels in nigral dopaminergic neurons via PKCδ pathway | |||
SHI Limin,LI Chen,JIANG Hong | |||
Biology 14 May 2016 | |||
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Abstract:Ghrelin is an endogenous ligand of the growth hormone secretagogue receptor (GHS-R). Through affecting the electrical properties of neurons in central nervous system, ghrelin exerts multiple effects, including appetite stimulation, energy balance modulation and neuroprotection. Our previous study showed that ghrelin increased the firing frequency of nigral dopaminergic neurons via inhibition of Kv7/KCNQ/M channels through activation of GHS-R/PLC/PKC pathway. However, whether the other potassium channels are also involved in the ghrelin-induced excitability of dopaminergic neurons still remain unclear. In this study, we focus on two voltage-gated potassium channels, the delayed rectifier potassium channels (IK) and A-type potassium channels (IA), which have a wide expression on dopaminergic neurons. Using whole-cell patch clamp recordings in vitro, our results indicated that ghrelin could reversibly inhibit IK and IA. The inhibition of IA showed an dose-dependent tendency, as the amplitude of IA decreased by 33.43% ± 3.78% and 52.92%±6.56% after 10 nM and 100 nM ghrelin treatment, respectively. These inhibitory effects of ghrelin were mediated by PKCδ system. The broad spectrum voltage-gated potassium channels blocker TEA, IA specific blocker 4-AP, and PKCδ specific blocker Rottlerin, occluded the excitatory effects of ghrelin. These results demonstrated that inhibition of IK and IA may contribute to the ghrelin-induced excitation of dopaminergic neurons. | |||
TO cite this article:SHI Limin,LI Chen,JIANG Hong. Ghrelin reduces A-type potassium channels in nigral dopaminergic neurons via PKCδ pathway[OL].[14 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4690524 |
8. Caldesmon is a key factor in contraction and stiffness of vascular smooth muscle cells | |||
JIANG Qifeng | |||
Biology 12 May 2016 | |||
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Abstract:In this paper, the potential role of CaD in mediating mechanical properties of VSMCs was probed and the regulatory effect of CaD on cell motilities was also discussed. First, structural effect of CaD on cytoskeleton integrity was analyzed with CaD knock-down; Second, Fourier transform traction cytometry was used to measure cell traction force dynamics; Third, the Optical Magnetic Twisting Cytometry was employed to determine cell stiffness dynamics. We found that CaD is an integral component to maintain cytoskeleton integrity of VSMCs. CaD not only sustains the basic value of contraction and stiffness of VSMCs in stationary condition, but also restores these mechanical parameters after cytoskeleton disruption. | |||
TO cite this article:JIANG Qifeng. Caldesmon is a key factor in contraction and stiffness of vascular smooth muscle cells[OL].[12 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4687312 |
9. E3 Activity of MDM2 is not required for MDM2 to Inhibits Axin-induced p53 Activation | |||
He Ying,Lian Guili,Ma Huanhuan,Lin Shuyong,Li Qinxi | |||
Biology 11 May 2016 | |||
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Abstract:MDM2 plays a crucial role in negatively regulating the functions of tumor suppressor p53. Here we show that MDM2 can inhibit Axin-stimulated p53-dependent apoptosis by suppressing p53 phosphorylation at Ser 46 and apoptosis-related p53 transactivational activity. Interestingly, the ubiquitin E3 ligase activity of MDM2 is not required for this inhibitory effect. Mechanically, either wildtype Mdm2 or its E3-dead mutant, disrupts the Axin-based HIPK2/p53 complex formation by blocking the binding of p53 and HIPK2 to Axin. Mdm2Δp53, a deletion mutant that lacks p53 binding domain fails to exert the inhibitory effect, demonstrating that the interaction of Mdm2 and p53, but not its E3 ligase activity toward p53 plays key role in suppressing Axin-stimulated p53 activation. Our results thus have revealed a novel aspect of the mechanism by which MDM2 regulates p53 activities. | |||
TO cite this article:He Ying,Lian Guili,Ma Huanhuan, et al. E3 Activity of MDM2 is not required for MDM2 to Inhibits Axin-induced p53 Activation[OL].[11 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4688749 |
10. Identification and Characterization of a New Calmodulin Binding Site at the C Terminus of Drosophila TRP Channel | |||
ZHENG Yunhua,LIU Wei | |||
Biology 11 May 2016 | |||
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Abstract:TRP channels are widely expressed in animal cells ranging from Drosophila to human beings and closely related to our vision, gestation, olfaction, temperature feeling, cell development, cell death, and oncogenesis, etc. Previous studies indicated that calcium can positively and negatively regulate the opening of the Drosophila TRP channel. Nevertheless, the concrete regulation mechanism of how the calcium regulates Drosophila TRP channel is not clear yet. It is also generally believed that calcium may regulate the Drosophila TRP channel through binding to calmodulin (CaM), but the mechanistic detail of the binding remains unresolved. In this study, we identified an unreported strong Ca2+-CaM binding site located at the C-terminus of Drosophila TRP channel. We confirmed the interaction using both bacterial expressed recombinant protein and synthetic peptide. FPLC (fast protein liquid chromatography) and SEC-MALS (size exclusion chromatography and multi-angle laser light scattering) showed that the recombinant protein formed a stable complex with Ca2+-CaM. And ITC (isothermal titration calorimetry) showed that the binding affinity (Kd) was at a range of submicromolar. We also determined the critical residues involved in Ca2+-CaM binding by mutagenesis studies. Our data would help to understand the mechanism of how calcium regulates Drosophila TRP channel through CaM. | |||
TO cite this article:ZHENG Yunhua,LIU Wei. Identification and Characterization of a New Calmodulin Binding Site at the C Terminus of Drosophila TRP Channel[OL].[11 May 2016] http://en.paper.edu.cn/en_releasepaper/content/4689311 |
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