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D ; Song, J.J. ; Song, J.J. ; Song, W.M. ; Song, Y.X. ; Sosio, Stefano ; Spataro, Stefano ; Su, K.X. ; Su, P.P. ; Sui, F.F. ; Sun, G.X. ; Sun, H.K. ; Sun, J.F. ; Sun, L. ; Sun, S.S. ; Sun, T. ; Sun, W.Y. ; Sun, X ; Sun, Y.J. ; Sun, Y.Z. ; Sun, Z.T. ; Tan, Y.H. ; Tan, Y.X. ; Tang, C.J. ; Tang, G.Y. ; Tang, J. ; Teng, J.X. ; Thoren, Viktor ; Tian, W.H. ; Tian, Y.T. ; Uman, I. ; Wang, B. ; Wang, C.W. ; Wang, D.Y. ; Wang, H.J. ; Wang, H.P. ; Wang, K. ; Wang, L.L. ; Wang, M. ; Wang, M.Z. ; Wang, Meng ; Wang, S. ; Wang, W. ; Wang, W.H. ; Wang, W.P. ; Wang, X. ; Wang, X.F. ; Wang, X.L. ; Wang, Y. ; Wang, Y.D. ; Wang, Y.F. ; Wang, Y.Q. ; Wang, Y.Y. ; Wang, Z. ; Wang, Z.Y. ; Wang, Ziyi ; Wang, Zongyuan ; Wei, D.H. ; Weidner, Frederik ; Wen, S.P. ; White, D.J. ; Wiedner, Ulrich ; Wilkinson, Guy ; Wolke, M. ; Wollenberg, Leonard ; Wu, J.F. ; Wu, L.H. ; Wu, L.J. ; Wu, X. ; Wu, X.H. ; Wu, Z. ; Xia, L. ; Xiao, H. ; Xiao, S.Y. ; Xiao, Z.J. ; Xie, X.H. ; Xie, Y.G. ; Xie, Y.H. ; Xing, T.Y. ; Xu, C.J. ; Xu, G.F. ; Xu, Q.J. ; Xu, W. ; Xu, X.P. ; Xu, Y.C. ; Yan, F. ; Yan, L. ; Yan, W.B. ; Yan, W.C. ; Yang, H.J. ; Yang, H.X. ; Yang, L. ; Yang, S.L. ; Yang, Y.X. ; Yang, Yifan ; Yang, Zhi ; Ye, M. ; Ye, M.H. ; Yin, J.H. ; You, Z.Y. ; Yu, B.X. ; Yu, C.X. ; Yu, G. ; Yu, J.S. ; Yu, T. ; Yuan, C.Z. ; Yuan, L. ; Yuan, X.Q. ; Yuan, Y. ; Yuan, Z.Y. ; Yue, C.X. ; Zafar, A.A. ; Zeng, X. ; Zeng, Y. ; Zhang, A.Q. ; Zhang, B.X. ; Zhang, Guangyi ; Zhang, H. ; Zhang, H.H. ; Zhang, H.H. ; Zhang, H.Y. ; Zhang, J.J. ; Zhang, J.L. ; Zhang, J.Q. ; Zhang, J.W. ; Zhang, J.Y. ; Zhang, J.Z. ; Zhang, Jianyu ; Zhang, Jiawei ; Zhang, L.M. ; Zhang, L.Q. ; Zhang, Lei ; Zhang, S. ; Zhang, S.F. ; Zhang, Shulei ; Zhang, X.D. ; Zhang, X.Y. ; Zhang, Y. ; Zhang, Y.T. ; Zhang, Y.H. ; Zhang, Yan ; Zhang, Yao ; Zhang, Z.Y. ; Zhao, G. ; Zhao, J. ; Zhao, J.Y. ; Zhao, J.Z. ; Zhao, Lei ; Zhao, Ling ; Zhao, M.G. ; Zhao, Q. ; Zhao, S.J. ; Zhao, Y.B. ; Zhao, Y.X. ; Zhao, Z.G. ; Zhemchugov, Alexey ; Zheng, B. ; Zheng, J.P. ; Zheng, Y.H. ; Zhong, B. ; Zhong, C. ; Zhou, L.P. ; Zhou, Q. ; Zhou, X. ; Zhou, X.K. ; Zhou, X.R. ; Zhou, X.Y. ; Zhu, A.N. ; Zhu, J. ; Zhu, K. ; Zhu, K.J. ; Zhu, S.H. ; Zhu, T.J. ; Zhu, W.J. ; Zhu, W.J. ; Zhu, Y.C. ; Zhu, Z.A. ; Zou, B.S. ; Zou, J.H.
Using 448.1 × 106 ψ(3686) decays collected with the BESIII detector at the BEPCII e+e− storage rings, the branching fractions and angular distributions of the decays χcJ → Ξ−Ξ¯¯¯¯+ and Ξ0Ξ¯¯¯¯0 (J = 0, 1, 2) are measured based on a partial-reconstruction technique. The decays χc1 → Ξ0Ξ¯¯¯¯0 and χc2 → Ξ0Ξ¯¯¯¯0 are observed for the first time with statistical significances of 7σ and 15σ, respectively. The results of this analysis are in good agreement with previous measurements and have significantly improved precision.
Yao, Chenguang ; Xi, Caili ; Hu, Kanghong ; Gao, Wa ; Cai, Xiaofeng ; Qin, Jinlan ; Lv, Shiyun ; Du, Canghao ; Wei, Yanhong
Background: Enterovirus 71 (EV71) is one of the major causative agents of hand, foot, and mouth disease (HFMD), which is sometimes associated with severe central nervous system disease in children. There is currently no specific medication for EV71 infection. Quercetin, one of the most widely distributed flavonoids in plants, has been demonstrated to inhibit various viral infections. However, investigation of the anti-EV71 mechanism has not been reported to date.
Methods: The anti-EV71 activity of quercetin was evaluated by phenotype screening, determining the cytopathic effect (CPE) and EV71-induced cells apoptosis. The effects on EV71 replication were evaluated further by determining virus yield, viral RNA synthesis and protein expression, respectively. The mechanism of action against EV71 was determined from the effective stage and time-of-addition assays. The possible inhibitory functions of quercetin via viral 2Apro, 3Cpro or 3Dpol were tested. The interaction between EV71 3Cpro and quercetin was predicted and calculated by molecular docking.
Results: Quercetin inhibited EV71-mediated cytopathogenic effects, reduced EV71 progeny yields, and prevented EV71-induced apoptosis with low cytotoxicity. Investigation of the underlying mechanism of action revealed that quercetin exhibited a preventive effect against EV71 infection and inhibited viral adsorption. Moreover, quercetin mediated its powerful therapeutic effects primarily by blocking the early post-attachment stage of viral infection. Further experiments demonstrated that quercetin potently inhibited the activity of the EV71 protease, 3Cpro, blocking viral replication, but not the activity of the protease, 2Apro, or the RNA polymerase, 3Dpol. Modeling of the molecular binding of the 3Cpro-quercetin complex revealed that quercetin was predicted to insert into the substrate-binding pocket of EV71 3Cpro, blocking substrate recognition and thereby inhibiting EV71 3Cpro activity.
Conclusions: Quercetin can effectively prevent EV71-induced cell injury with low toxicity to host cells. Quercetin may act in more than one way to deter viral infection, exhibiting some preventive and a powerful therapeutic effect against EV71. Further, quercetin potently inhibits EV71 3Cpro activity, thereby blocking EV71 replication.
Ma, Danhui ; Chen, Sinuo ; Wang, Heming ; Wei, Jiayi ; Wu, Hao ; Gao, Hong ; Cheng, Xinlai ; Liu, Taotao ; Luo, Shi-Hua ; Zhao, Yicheng ; Song, Guangqi
Pancreatic cancer is a common malignant tumor with a high incidence and mortality rate. The prognosis of patients with pancreatic cancer is considerably poor due to the lack of effective treatment in clinically. Despite numerous studies have revealed that baicalein, a natural product, is responsible for suppressing multiple cancer cells proliferation, motility and invasion. The mechanism by which baicalein restraining pancreatic cancer progression remains unclear. In this study, we firstly verified that baicalein plays a critical role in inhibiting pancreatic tumorigenesis in vitro and in vivo. Then we analyzed the alteration of microRNAs (miRNAs) expression levels in Panc-1 cells incubated with DMSO, 50 and 100 μM baicalein by High-Throughput sequencing. Intriguingly, we observed that 20 and 39 miRNAs were accordingly up- and down-regulated through comparing Panc-1 cells exposed to 100 μM baicalein with the control group. Quantitative PCR analysis confirmed that miR-139-3p was the most up-regulated miRNA after baicalein treatment, while miR-196b-5p was the most down-regulated miRNA. Further studies showed that miR-139-3p induced, miR-196b-5p inhibited the apoptosis of Panc-1 cells via targeting NOB1 and ING5 respectively. In conclusion, we demonstrated that baicalein is a potent inhibitor against pancreatic cancer by modulating the expression of miR-139-3p or miR-196b-5p.
Schmidtko, Achim ; Gao, Wei ; König, Peter ; Heine, Sandra ; Sausbier, Matthias ; Ruth, Peter ; Koesling, Doris ; Tegeder, Irmgard ; Friebe, Andreas ; Geisslinger, Gerd
Oral presentation from 4th International Conference of cGMP Generators, Effectors and Therapeutic Implications ; Regensburg, Germany. 19–21 June 2009 Background: An exaggerated pain sensitivity is the dominant feature of inflammatory and neuropathic pain both in the clinical setting and in experimental animal models. It manifests as pain in response to normally innocuous stimuli (allodynia), increased response to noxious stimuli (hyperalgesia) or spontaneous pain, and can persist long after the initial injury is resolved. Research over the last decades has revealed that several signaling pathways in the spinal cord essentially contribute to the pain sensitization. To test the contribution of cGMP produced by NO-sensitive guanylyl cyclase (NO-GC) to pain sensitization, we investigated the localization of NO-GC in the spinal cord and in dorsal root ganglia, and we characterized the nociceptive behavior of mice deficient in NO-GC (GC-KO mice). Results: We show that NO-GC (β1 subunit) is distinctly expressed in neurons of the mouse spinal cord, while its distribution in dorsal root ganglia is restricted to non-neuronal cells. GC-KO mice exhibited a considerably reduced nociceptive behavior in models of inflammatory or neuropathic pain, but their responses to acute pain were not impaired. Moreover, GC-KO mice failed to develop pain sensitization induced by spinal administration of drugs releasing NO. Surprisingly, during spinal nociceptive processing cGMP produced by NO-GC may activate signaling pathways different from cGMP-dependent protein kinase I (cGKI), while cGKI can be activated by natriuretic peptide receptor-B (NPR-B) dependent cGMP production. Conclusion: Taken together, our results provide evidence that NO-GC has a dominant role in the development of exaggerated pain sensitivity during inflammatory and neuropathic pain. Furthermore, beside the NO-mediated cGMP synthesis, cGMP produced by NPR-B contributes to pain sensitization by activation of cGKI.
Schmidtko, Achim ; Gao, Wei ; Sausbier, Matthias ; Grundei, Inga ; Niederberger, Ellen ; Scholich, Klaus ; Huber, Andrea ; Allescher, Hans-Dieter ; Hofmann, Franz ; Ruth, Peter ; Geisslinger, Gerd
The experience of pain is mediated by a specialized sensory system, the nociceptive system. There is considerable evidence that the cGMP/cGMP kinase I (cGKI) signaling pathway modulates the nociceptive processing within the spinal cord. However, downstream targets of cGKI in this context have not been identified to date. In this study we investigated whether cysteine-rich protein 2 (CRP2) is a downstream effector of cGKI in the spinal cord and is involved in nociceptive processing. Immunohistochemistry of the mouse spinal cord revealed that CRP2 is expressed in superficial laminae of the dorsal horn. CRP2 is colocalized with cGKI and with markers of primary afferent C fibers. Importantly, the majority of CRP2 mRNA-positive dorsal root ganglion (DRG) neurons express cGKI and CRP2 is phosphorylated in a cGMP-dependent manner. To elucidate the functional role of CRP2 in nociception, we investigated the nociceptive behavior of CRP2-deficient (CRP2-/-) mice. Touch perception and acute thermal nociception were unaltered in CRP2-/- mice. However, CRP2-/- mice showed an increased nociceptive behavior in models of persistent pain as compared to wild type mice. Intrathecal administration of cGKI activating cGMP analogs increased the nociceptive behavior in wild type but not in CRP2-/- mice, indicating that the presence of CRP2 was essential for cGMP/cGKI-mediated nociception. These data indicate that CRP2 is a new downstream effector of cGKI-mediated spinal nociceptive processing and point to an inhibitory role of CRP2 in the generation of inflammatory pain.
Prostaglandin D2 (PGD2) is involved in a variety of physiological and pathophysiological processes, but its role in fever is poorly understood and the data obtained so far are rather controversial. Here we investigated the effects of central PGD2 delivery and of systemic prostaglandin D synthase (PGDS) or cyclooxygenase (COX) inhibition on core body temperature (TC) and on prostaglandin levels in the cerebrospinal fluid (CSF) of rats. Both PGE2 and PGD2 were detectable in CSF samples from control rats (6.2 ± 1.1 and 17.3 ± 3.1 pg/ml, respectively). Lipopolysaccharide (LPS) injection (50 μg i.p.) induced fever during the 5-hour observation period. Five hours after LPS injection, the levels of PGE2 and PGD2 were increased in the CSF about 90-fold (541.0 ± 47.5 pg/ml) and 5-fold (95.4 ± 23.1 pg/ml), respectively. Administration of PGD2 (50 - 500 ng) into the cisterna magna (i.c.m) evoked a delayed fever response in a dose-dependent manner that was accompanied by increased levels of PGE2 in the CSF. RT-PCR analyses revealed that the increased levels of PGE2 after PGD2 administration were not caused by up-regulation of COX-2 or microsomal prostaglandin E synthase 1 (mPGES-1) in the hypothalamus. Interestingly, i.c.m. pretreatment of animals with PGD2 considerably sustained the pyrogenic effects of i.c.m. administered PGE2. Pretreatment with a novel PGDS inhibitor, EDJ300520 (10 – 40 mg/kg p.o.), 1 h prior to the LPS injection impaired the LPS-induced increase of both PGD2 and PGE2 in the CSF and inhibited the fever response. In contrast, administration of EDJ300520 3 h after LPS injection did not ameliorate the LPS-induced fever. Accordingly, the concentration of PGE2 in the CSF was not decreased after EDJ300520 treatment. However, the CSF levels of PGD2 were reduced after administration of a high dose of EDJ300520 (40 mg/kg). We also investigated the effects of antipyretic drugs on the CSF levels of PGE2 and PGD2 during LPS-induced fever. Four antipyretic drugs with different mechanisms of action were used, including ibuprofen (5 - 20 mg/kg), celecoxib (10 - 50 mg/kg), SC560 5 - 20 mg/kg), and paracetamol (50 - 150 mg/kg). Each drug was used in three different doses and was orally administered 3 h after the LPS injection. All drugs were capable to attenuate the LPS-induced fever. The decrease of TC paralleled the reduction of PGE2 levels in the CSF. Of note, there was a tendency to reduced PGD2 levels in the CSF after treatment with the antipyretic drugs. However, only SC560 and the high dose of celecoxib (50 mg/kg) reduced the PGD2 levels significantly. In summary, our experiments underscore the pivotal role of PGE2 as the principal downstream mediator of fever. Moreover, we demonstrate that PGD2 is also involved in the mechanisms underlying fever. Our data suggest that PGD2 exerts an indirect pyrogenic effect by modulating the availability of PGE2 in the CSF. Additional studies are needed to explore the exact mechanism by