2,728 research outputs found

    Lagrangian Floer potential of orbifold spheres

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    For each sphere with three orbifold points, we construct an algorithm to compute the open Gromov–Witten potential, which serves as the quantum-corrected Landau–Ginzburg mirror and is an infinite series in general. This gives the first class of general-type geometries whose full potentials can be computed. As a consequence we obtain an enumerative meaning of mirror maps for elliptic curve quotients. Furthermore, we prove that the open Gromov–Witten potential is convergent, even in the general-type cases, and has an isolated singularity at the origin, which is an important ingredient of proving homological mirror symmetry.National Research Foundation of Korea; 2010-0019516; 2012R1A1A2003117; 2013R1A1A1058646 - National Research Foundation of Kore

    The mechanism of low-concentration sodium nitroprusside-mediated protection of chondrocyte death

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    Sodium nitroprusside (SNP), a widely used nitric oxide donor, has recently been shown to mediate chondrocyte apoptosis by generating reactive oxygen species, whereas more potent nitric oxide donors do not induce chondrocyte apoptosis. The present study was performed to investigate the protective effect of a low concentration of SNP upon the cytotoxicity of chondrocytes to higher concentrations of SNP, and to elucidate the underlying mechanism. Human osteoarthritis chondrocytes were cultured as monolayers, and first-passage cells were used for the experiments. Chondrocyte death induced by 1 mM SNP was completely inhibited by pretreating with 0.1 mM SNP. This protective effect of SNP was replicated by the guanosine-3',5'κ-cyclic monophosphate analog, DBcGMP. Protection from chondrocyte death conferred by 0.1 mM SNP was mediated by heme oxygenase 1 (HO-1), as was revealed by the increased expression of HO-1 in 0.1 mM SNP pretreated chondrocytes and by the reversal of this protective effect by the HO-1 inhibitor, zinc protoporphyrin. SNP-mediated chondrocyte protection correlated with the downregulation of both extracellular signal-regulated protein kinase 1/2 and p38 kinase activation. SNP at 0.1 mM induced significant NF-κB activation as revealed by electrophoretic mobility shift assays, and the inhibition of NF-κB by MG132 or Bay 11-7082 nullified 0.1 mM SNP-mediated chondrocyte protection. The upregulation of p53 and the downregulation of Bcl-(XL )and Mcl-1 by 1 mM SNP were reversed by 0.1 mM SNP pretreatment at the protein level by western blotting. Our study shows that priming with 0.1 mM SNP confers complete protection against cell death induced by 1 mM SNP in human articular chondrocytes. This protective effect was found to be correlated with the upregulation of both HO-1 and NF-κB and with the concomitant downregulation of both extracellular signal-regulated protein kinase 1/2 and p38 activation

    Surface Modification of Magnesium and its Alloys Using Anodization for Orthopedic Implant Application

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    Magnesium (Mg) as a biodegradable implant brings a revolution in medical field application, especially in bone implant and stent application. Biodegradability of Mg has attracted attentions of researchers to avoid secondary surgery to remove the implant materials after healing process. Various advantages of Mg make it suitable for medical application such as density, good mechanical properties and biodegradation. However, Mg biodegradability must be controlled to meet tissue-healing period of time because of the high degradation in a physiological environment. Fast corrosion and high alkalinity due to hydrogen release induce tissue inflammation, which limits its clinical applications. Many techniques are applied to the Mg surface to improve surface biocompatibility and control its biodegradability. This chapter focuses on anodization of Mg and its alloys to improve corrosion resistance and biocompatibility for orthopedic application. Mg coating with thin film apatite could enhance the biocompatibility and increase osseointegration formation in the bone fracture side. Evaluation of the required anodized film discussed in the chapter such as chemical composition, biodegradability and biocompatibility

    Protein Degradation of RNA Polymerase II-Association Factor 1(PAF1) Is Controlled by CNOT4 and 26S Proteasome

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    The PAF complex (PAFc) participates in various steps of the transcriptional process, from initiation to termination, by interacting with and recruiting various proteins to the proper locus for each step. PAFc is an evolutionarily conserved, multi-protein complex comprising PAF1, CDC73, CTR9, LEO1, yRTF1 and, in humans, hSKI8. These components of PAFc work together, and their protein levels are closely interrelated. In the present study, we investigated the mechanism of PAF1 protein degradation. We found that PAF1 protein levels are negatively regulated by the expression of CNOT4, an ortholog of yNOT4 and a member of the CCR4-NOT complex. CNOT4 specifically controls PAF1 but not other components of PAFc at the protein level by regulating the polyubiquitination of PAF1 and its subsequent degradation by the 26S proteasome. The degradation of PAF1 was found to require nuclear localization, as no PAF1 degradation by CNOT4 and the 26S proteasome was observed with NLS (nucleus localization signal)-deficient PAF1 mutants. However, chromatin binding by PAF1 was not necessary for 26S proteasome- or CNOT4-mediated degradation. Our results suggest that CNOT4 controls the degradation of chromatin-unbound PAF1 via the 26S proteasome.open1184Ysciescopu
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