47 research outputs found

    Knot undulator to generate linearly polarized photons with low on-axis power density

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    Heat load on beamline optics is a serious problem to generate pure linearly polarized photons in the third generation synchrotron radiation facilities. For permanent magnet undulators, this problem can be overcome by a figure-8 operating mode. But there is still no good method to tackle this problem for electromagnetic elliptical undulators. Here, a novel operating mode is suggested, which can generate pure linearly polarized photons with very low on-axis heat load. Also the available minimum photon energy of linearly polarized photons can be extended much by this method

    Self-amplified spontaneous emission for a single pass free-electron laser

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    SPARC (acronym of "Sorgente Pulsata ed Amplificata di Radiazione Coerente", i.e. Pulsed and Amplified Source of Coherent Radiation) is a single pass free-electron laser designed to obtain high gain amplification at a radiation wavelength of 500 nm. Self-amplified spontaneous emission has been observed driving the amplifier with the high-brightness beam of the SPARC linac. We report measurements of energy, spectra, and exponential gain. Experimental results are compared with simulations from several numerical codes

    High-order-harmonic generation and superradiance in a seeded free-electron laser

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    Higher order harmonic generation in a free-electron laser amplifier operating in the superradiant regime [R.\u2009H. Dicke, Phys. Rev. 93, 99 (1954).] has been observed. Superradiance has been induced by seeding a single-pass amplifier with the second harmonic of a Ti:sapphire laser, generated in a \u3b2-Barium borate crystal, at seed intensities comparable to the free-electron laser saturation intensity. Pulse energy and spectral distributions of the harmonics up to the 11th order have been measured and compared with simulations

    Zinc uptake promotes myoblast differentiation via Zip7 transporter and activation of Akt signalling transduction pathway

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    [EN] Myogenic regeneration occurs through a chain of events beginning with the output of satellite cells from quiescent state, formation of competent myoblasts and later fusion and differentiation into myofibres. Traditionally, growth factors are used to stimulate muscle regeneration but this involves serious off-target effects, including alterations in cell homeostasis and cancer. In this work, we have studied the use of zinc to trigger myogenic differentiation. We show that zinc promotes myoblast proliferation, differentiation and maturation of myofibres. We demonstrate that this process occurs through the PI3K/Akt pathway, via zinc stimulation of transporter Zip7. Depletion of zinc transporter Zip7 by RNA interference shows reduction of both PI3K/Akt signalling and a significant reduction of multinucleated myofibres and myotubes development. Moreover, we show that mature myofibres, obtained through stimulation with high concentrations of zinc, accumulate zinc and so we hypothesise their function as zinc reservoirs into the cell.P.R. and R.S. acknowledges support from the Spanish Ministry of Economy and Competitiveness (MINECO) (MAT2015-69315-C3-1-R). P.R. acknowledges the Fondo Europeo de Desarrollo Regional (FEDER). CIBER-BBN is an initiative funded by the VI National R&D&I Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. R.S. acknowledges the support from the Spanish MECD through the PRX16/00208 grant. MSS acknowledges support from the European Research Council (ERC - HealInSynergy 306990) and the UK Engineering and Physical Sciences Research Council (EPSRC - EP/P001114/1)Mnatsakanyan, H.; Sabater I Serra, R.; Rico Tortosa, PM.; Salmerón Sánchez, M. (2018). Zinc uptake promotes myoblast differentiation via Zip7 transporter and activation of Akt signalling transduction pathway. Scientific Reports. 8:1-14. https://doi.org/10.1038/s41598-018-32067-0S1148Frontera, W. R. & Ochala, J. Skeletal muscle: a brief review of structure and function. Calcif. Tissue Int. 96, 183–195 (2015).Wolfe, R. R., Frontera, W. R. & Ochala, J. The underappreciated role of muscle in health and disease. Am. J. Clin. Nutr. 84, 475–82 (2006).Sciorati, C., Rigamonti, E., Manfredi, A. A. & Rovere-Querini, P. Cell death, clearance and immunity in the skeletal muscle. Cell Death Differ. 23, 927–937 (2016).Wang, Y. X. & Rudnicki, M. A. Satellite cells, the engines of muscle repair. Nat. Rev. Mol. Cell Biol. 13, 127–133 (2011).Yin, H., Price, F. & Rudnicki, M. A. Satellite cells and the muscle stem cell niche. Physiol. Rev. 93, 23–67 (2013).Dhawan, J. & Rando, T. A. Stem cells in postnatal myogenesis: Molecular mechanisms of satellite cell quiescence, activation and replenishment. Trends Cell Biol. 15, 666–673 (2005).Yun, K. & Wold, B. Skeletal muscle determination and differentiation: Story of a core regulatory network and its context. Curr. Opin. Cell Biol. 8, 877–889 (1996).Gharaibeh, B. et al. Biological approaches to improve skeletal muscle healing after injury and disease. Birth Defects Res. Part C Embryo Today Rev. 96, 82–94 (2012).Schiaffino, S. & Mammucari, C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet. Muscle 1, 4 (2011).Sandri, M. Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda). 23, 160–70 (2008).Karalaki, M., Fili, S., Philippou, A. & Koutsilieris, M. Muscle regeneration: cellular and molecular events. In Vivo 23, 779–96 (2009).Fujio, Y. et al. Cell cycle withdrawal promotes myogenic induction of Akt, a positive modulator of myocyte survival. Mol. Cell. Biol. 19, 5073–82 (1999).Wilson, E. M. & Rotwein, P. Control of MyoD function during initiation of muscle differentiation by an autocrine signaling pathway activated by insulin-like growth factor-II. J. Biol. Chem. 281, 29962–29971 (2006).Sun, L., Liu, L., Yang, X. & Wu, Z. Akt binds prohibitin 2 and relieves its repression of MyoD and muscle differentiation. J. Cell Sci. 117, 3021–3029 (2004).Milner, D. & Cameron, J. Muscle repair and regeneration: stem cells, scaffolds, and the contributions of skeletal muscle to amphibian limb regeneration. Curr. Top. Microbiol. Immunol. 367, 133–159 (2013).Liu, C. et al. PI3K/Akt signaling transduction pathway is involved in rat vascular smooth muscle cell proliferation induced by apelin-13. Acta Biochim Biophys Sin 42, 396–402 (2010).Eriksson, M., Taskinen, M. & Leppä, S. Mitogen Activated Protein Kinase-Dependent Activation of c-Jun and c-Fos is required for Neuronal differentiation but not for Growth and Stress Reposne in PC12 cells. J. Cell. Physiol. 207, 12–22 (2006).Arsic, N. et al. Vascular endothelial growth factor stimulates skeletal muscle regeneration in Vivo. Mol. Ther. 10, 844–854 (2004).Borselli, C. et al. Functional muscle regeneration with combined delivery of angiogenesis and myogenesis factors. Proc. Natl. Acad. Sci. USA 107, 3287–3292 (2010).Hanft, J. R. et al. Phase I trial on the safety of topical rhVEGF on chronic neuropathic diabetic foot ulcers. J. Wound Care 17(30–2), 34–7 (2008).Simón-Yarza, T. et al. Vascular endothelial growth factor-delivery systems for cardiac repair: An overview. Theranostics 2, 541–552 (2012).Briquez, P. S., Hubbell, J. A. & Martino, M. M. Extracellular Matrix-Inspired Growth Factor Delivery Systems for Skin Wound Healing. Adv. Wound Care 4, 479–489 (2015).Barthel, A., Ostrakhovitch, E. A., Walter, P. L., Kampkötter, A. & Klotz, L. O. Stimulation of phosphoinositide 3-kinase/Akt signaling by copper and zinc ions: Mechanisms and consequences. Arch. Biochem. Biophys. 463, 175–182 (2007).Ostrakhovitch, E. A., Lordnejad, M. R., Schliess, F., Sies, H. & Klotz, L.-O. Copper ions strongly activate the phosphoinositide-3-kinase/Akt pathway independent of the generation of reactive oxygen species. Arch. Biochem. Biophys. 397, 232–239 (2002).Kaur, K., Gupta, R., Saraf, S. A. & Saraf, S. K. Zinc: The metal of life. Compr. Rev. Food Sci. Food Saf. 13, 358–376 (2014).Coleman, J. E. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61, 897–946 (1992).Fukada, T. & Kambe, T. Molecular and genetic features of zinc transporters in physiology and pathogenesis. Metallomics 3, 662–674 (2011).Murakami, M. & Hirano, T. Intracellular zinc homeostasis and zinc signaling. Cancer Sci. 99, 1515–1522 (2008).Hogstrand, C., Kille, P., Nicholson, R. I. & Taylor, K. M. Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation. Trends Mol. Med. 15, 101–111 (2009).Kolenko, V., Teper, E., Kutikov, A. & Uzzo, R. Zinc and zinc transporters in prostate carcinogenesis. Nat. Rev. Urol. 10, 219–26 (2013).Myers, S. A., Nield, A., Chew, G. S. & Myers, M. A. The zinc transporter, Slc39a7 (Zip7) is implicated in glycaemic control in skeletal muscle cells. Plos One 8 (2013).Kambe, T., Tsuji, T., Hashimoto, A. & Itsumura, N. The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism. Physiol. Rev. 95, 749–784 (2015).Jinno, N., Nagata, M. & Takahashi, T. Marginal zinc deficiency negatively affects recovery from muscle injury in mice. Biol. Trace Elem. Res. 158, 65–72 (2014).Taylor, K. M., Hiscox, S., Nicholson, R. I., Hogstrand, C. & Kille, P. Protein Kinase CK2 Triggers Cytosolic Zinc Signaling Pathways by Phosphorylation of Zinc Channel ZIP7. Sci. Signal. 5, ra11–ra11 (2012).Yamasaki, S. et al. Zinc is a novel intracellular second messenger. J. Cell Biol. 177, 637–45 (2007).Sumitani, S., Goya, K., Testa, J. R., Kouhara, H. & Kasayama, S. Akt1 and Akt2 differently regulate muscle creatine kinase and myogenin gene transcription in insulin-induced differentiation of C2C12 myoblasts. Endocrinology 143, 820–828 (2002).Ohashi, K. et al. Zinc promotes proliferation and activation of myogenic cells via the PI3K/Akt and ERK signaling cascade. Exp. Cell Res. 333, 228–237 (2015).Chesters, J. K. In Zinc in human biology 53, 109–118 (1989).Burattini, S. et al. C2C12 murine myoblasts as a model of skeletal muscle development: Morpho-functional characterization. Eur. J. Histochem. 48, 223–233 (2004).Mnatsakanyan, H. et al. Controlled Assembly of Fibronectin Nanofibrils Triggered by Random Copolymer Chemistry. ACS Appl. Mater. Interfaces 7, 18125–18135 (2015).Jeong, J. & Eide, D. J. The SLC39 family of zinc transporters. Molecular Aspects of Medicine 34, 612–619 (2013).Huang, L., Kirschke, C. P., Zhang, Y. & Yan, Y. Y. The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus. J. Biol. Chem. 280, 15456–15463 (2005).Vallee, B. L. & Falchuk, K. H. The biochemical basis of zinc physiology. Physiological reviews 73 (1993).Ganju, N. & Eastman, A. Zinc inhibits Bax and Bak activation and cytochrome c release induced by chemical inducers of apoptosis but not by death-receptor-initiated pathways. Cell Death Differ. 10, 652–61 (2003).Chai, F., Truong-Tran, A. Q., Ho, L. H. & Zalewski, P. D. Regulation of caspase activation and apoptosis by cellular zinc fluxes and zinc deprivation: A review. Immunol. Cell Biol. 77, 272–278 (1999).Smith, P. J., Wiltshire, M., Furon, E., Beattie, J. H. & Errington, R. J. Impact of overexpression of metallothionein-1 on cell cycle progression and zinc toxicity. Am. J. Physiol. Cell Physiol. 295, C1399–C1408 (2008).Bozym, R. A. et al. Free zinc ions outside a narrow concentration range are toxic to a variety of cells in vitro. Exp. Biol. Med. (Maywood). 235, 741–50 (2010).Plum, L. M., Rink, L. & Hajo, H. The essential toxin: Impact of zinc on human health. Int. J. Environ. Res. Public Health 7, 1342–1365 (2010).Chen, C.-J. & Liao, S.-L. Zinc toxicity on neonatal cortical neurons: involvement of glutathione chelation. J. Neurochem. 85, 443–453 (2003).Chassot, A. A. et al. Confluence-induced cell cycle exit involves pre-mitotic CDK inhibition by p27Kip1 and cyclin D1 downregulation. Cell Cycle 7, 2038–2046 (2008).Spencer, S. L. et al. XThe proliferation-quiescence decision is controlled by a bifurcation in CDK2 activity at mitotic exit. Cell 155, 369–383 (2013).Walsh, K. & Perlman, H. Cell cycle exit upon myogenic differentiation. Curr. Opin. Genet. Dev. 7, 597–602 (1997).Puri, P. L. & Sartorelli, V. Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications. Journal of Cellular Physiology 185, 155–173 (2000).Zammit, P. S., Partridge, T. A. & Yablonka-Reuveni, Z. The skeletal muscle satellite cell: the stem cell that came in from the cold. J Histochem Cytochem 54, 1177–1191 (2006).McCord, M. C. & Aizenman, E. The role of intracellular zinc release in aging, oxidative stress, and Alzheimer’s disease. Front. Aging Neurosci. 6, 1–16 (2014).Dirksen, R. T. Sarcoplasmic reticulum–mitochondrial through-space coupling in skeletal muscle. This paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic. Appl. Physiol. Nutr. Metab. 34, 389–395 (2009).Groth, C., Sasamura, T., Khanna, M. R., Whitley, M. & Fortini, M. E. Protein trafficking abnormalities in Drosophila tissues with impaired activity of the ZIP7 zinc transporter Catsup. Development 140, 3018–3027 (2013).Ellis, C. D. et al. Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function. J. Cell Biol. 166, 325–335 (2004).Koch, U., Lehal, R. & Radtke, F. Stem cells living with a Notch. Development 140, 689–704 (2013).Gardner, S., Anguiano, M. & Rotwein, P. Defining Akt actions in muscle differentiation. Am. J. Physiol. Physiol. 303, C1292–C1300 (2012).Knight, J. D. & Kothary, R. The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis. Skelet. Muscle 1, 29 (2011).Roth, S. M. Genetic aspects of skeletal muscle strength and mass with relevance to sarcopenia. Bonekey Rep. 1, 1–7 (2012).Mebratu, Y. & Tesfaigzi, Y. How ERK1/2 Activation Controls Cell Proliferation and Cell Death Is Subcellular Localization the Answer? Cell Cycle 8, 1168–1175 (2009)

    Erratum to: EuPRAXIA Conceptual Design Report – Eur. Phys. J. Special Topics 229, 3675-4284 (2020), https://doi.org/10.1140/epjst/e2020-000127-8

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    International audienceThe online version of the original article can be found at http://https://doi.org/10.1140/epjst/e2020-000127-8</A

    SEEDING SCHEMES ON THE FRENCH FEL PROJECT LUNEX5

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    Abstract LUNEX5 is a single pass FEL project aims at producing coherent synchrotron radiation with, in a first step, an electron bunch accelerated in conventional RF cavities up to 300 Me

    Robustness of a plasma acceleration based Free Electron Laser

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    International audienceLaser plasma accelerators (LPA) can sustain GeV/m accelerating fields offering outstanding new possibilities for compact applications. The LPA beam brightness can now be comparable to radio-frequency accelerators’ (RFA), thanks essentially to the beams short duration (<3  fs) and low emittance (as small as 0.1 micron). Still, the mrad level divergence and few percent level energy spread, remain limiting parameters in the cases of demanding applications such as free electron lasers (FELs). Several concepts of transfer line were proposed to mitigate those intrinsic properties targeting undulator radiation applications. We study here the robustness of the chromatic matching strategy for FEL amplification at 200 nm in a dedicated transport line, and analyze its sensitivity to several parameters. We consider not only the possible LPA source jitters, but also various realistic defaults of the equipment such as magnetic elements misalignments or focussing strength errors, imperfect undulator fields, etc
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