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New insights into the epidemiology of gout. Rheumatology (Oxford). 2009;48(2):ii2–8.\nSchiltz C, Lioté F, Prudhommeaux F, Meunier A, Champy R, Callebert J, et al. Monosodium urate monohydrate crystal-induced inflammation in vivo: quantitative histomorphometric analysis of cellular events. Arthritis Rheum. 2002;46(6):1643–50.\nKingsbury SR, Conaghan PG, McDermott MF. The role of the NLRP3 inflammasome in gout. J Inflamm Res. 2011;4:39–49.\nRock KL, Kataoka H, Lai JJ. Uric acid as a danger signal in gout and its comorbidities. Nat Rev Rheumatol. 2013;9(1):13–23.\nDalbeth N, Haskard DO. Mechanisms of inflammation in gout. Rheumatology (Oxford). 2005;44(9):1090–6.\nPunzi L, Scanu A, Ramonda R, Oliviero F. Gout as autoinflammatory disease: new mechanisms for more appropriated treatment targets. Autoimmun Rev. 2012;12(1):66–71.\nGonzalez EB. An update on the pathology and clinical management of gouty arthritis. Clin Rheumatol. 2012;31(1):13–21.\nMitroulis I, Skendros P, Ritis K. Targeting IL-1beta in disease; the expanding role of NLRP3 inflammasome. Eur J Intern Med. 2010;21(3):157–63.\nDinarello CA. How interleukin-1β induces gouty arthritis. Arthritis Rheum. 2010;62(11):3140–4.\nFerraccioli G, Bracci-Laudiero L, Alivernini S, Gremese E, Tolusso B, De Benedetti F. Interleukin-1β and interleukin-6 in arthritis animal models: roles in the early phase of transition from acute to chronic inflammation and relevance for human rheumatoid arthritis. Mol Med. 2010;16(11–12):552–7.\nGhiringhelli F, Apetoh L, Tesniere A, Aymeric L, Ma Y, Ortiz C, et al. Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors. Nat Med. 2009;15(10):1170–8.\nMartinon F, Mayor A, Tschopp J. The inflammasomes: guardians of the body. Annu Rev Immunol. 2009;27:229–65.\nSheedy FJ, Grebe A, Rayner KJ, Kalantari P, Ramkhelawon B, Carpenter SB, et al. CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation. Nat Immunol. 2013;14(8):812–20.\nFreudweiler M. Study of the nature of gouty tophi. Dtsch Arch Klin Med. 1899;63:36–41.\nMcGettrick AF, O’Neill LA. NLRP3 and IL-1β in macrophages as critical regulators of metabolic diseases. Diabetes Obes Metab. 2013;15(3):19–25.\nMurakami Y, Akahoshi T, Hayashi I, Endo H, Kawai S, Inoue M, et al. Induction of triggering receptor expressed on myeloid cells 1 in murine resident peritoneal macrophages by monosodium urate monohydrate crystals. Arthritis Rheum. 2006;54(2):455–62.\nMartinon F, Pétrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature. 2006;440(7081):237–41.\nMartin WJ, Walton M, Harper J. Resident macrophages initiating and driving inflammation in a monosodium urate monohydrate crystal-induced murine peritoneal model of acute gout. Arthritis Rheum. 2009;60(1):281–9.\nAmaral FA, Costa VV, Tavares LD, Sachs D, Coelho FM, Fagundes CT, et al. NLRP3 inflammasome-mediated neutrophil recruitment and hypernociception depend on leukotriene B(4) in a murine model of gout. Arthritis Rheum. 2012;64(2):474–84.\nScanu A, Oliviero F, Gruaz L, Sfriso P, Pozzuoli A, Frezzato F, et al. High-density lipoproteins downregulate CCL2 production in human fibroblast-like synoviocytes stimulated by urate crystals. Arthritis Res Ther. 2010;12(1):R23.\nWijbrandts CA, Van Leuven SI, Boom HD, Gerlag DM, Stroes EG, Kastelein JJ, et al. Sustained changes in lipid profile and macrophage migration inhibitory factor levels after anti-tumour necrosis factor therapy in rheumatoid arthritis. Ann Rheum Dis. 2009;68(8):1316–21.\nLandis RC, Haskard DO. Pathogenesis of crystal-induced inflammation. Curr Rheumatol Rep. 2001;3(1):36–41.\nMitroulis I, Kambas K, Ritis K. Neutrophils, IL-1β, and gout: is there a link? Semin Immunopathol. 2013;35(4):501–12.\nMankan AK, Dau T, Jenne D, Hornung V. The NLRP3\u002FASC\u002FCaspase-1 axis regulates IL-1β processing in neutrophils. Eur J Immunol. 2012;42(3):710–5.\nGuarda G, Dostert C, Staehli F, Cabalzar K, Castillo R, Tardivel A, et al. T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes. Nature 9. 2009;460(7252):269–73.\nDalbeth N, Fransen J, Jansen TL, Neogi T, Schumacher HR, Taylor WJ. New classification criteria for gout: a framework for progress. Rheumatology (Oxford). 2013;52(10):1748–53.\nNeogi T. Clinical practice. Gout N Engl J Med 3. 2011;364(5):443–52.\nPerper SJ, Browning B, Burkly LC, Weng S, Gao C, Giza K, et al. TWEAK is a novel arthritogenic mediator. J Immunol 15. 2006;177(4):2610–20.\nChang SK, Noss EH, Chen M, Gu Z, Townsend K, Grenha R, et al. Cadherin-11 regulates fibroblast inflammation. Proc Natl Acad Sci U S A. 2011;108(20):8402–7.\nThwin MM, Douni E, Arjunan P, Kollias G, Kumar PV, Gopalakrishnakone P. Suppressive effect of secretory phospholipase A2 inhibitory peptide on interleukin-1beta-induced matrix metalloproteinase production in rheumatoid synovial fibroblasts, and its antiarthritic activity in hTNFtg mice. Arthritis Res Ther. 2009;11(5):R138.\nGravallese EM. Bone destruction in arthritis. Ann Rheum Dis. 2002;61(2):ii84–6.\nPeng YJ, Lee CH, Wang CC, Salter DM, Lee HS. Pycnogenol attenuates the inflammatory and nitrosative stress on joint inflammation induced by urate crystals. Free Radic Biol Med. 2012;52(4):765–74.\nStanczyk J, Ospelt C, Karouzakis E, Filer A, Raza K, Kolling C, et al. Altered expression of microRNA-203 in rheumatoid arthritis synovial fibroblasts and its role in fibroblast activation. Arthritis Rheum. 2011;63(2):373–81.\nOussirot E, Streit G, Wendling D. Infectious complications with anti-TNFalpha therapy in rheumatic diseases: a review. Recent Pat Inflamm Allergy Drug Discov. 2007;1(1):39–47.\nDa Chen P, Wong CK, Tam LS, Li EK, Lam CW. Activation of human fibroblast-like synoviocytes by uric acid crystals in rheumatoid arthritis. Cell Mol Immunol. 2011;8(6):469–78.\nScott P, Ma H, Viriyakosol S, Terkeltaub R, Liu-Bryan R. Engagement of CD14 mediates the inflammatory potential of monosodium urate crystals. J Immunol. 2006;177(9):6370–8.\nYao X, Ding Z, Xia Y, Wei Z, Luo Y, Feleder C, et al. Inhibition of monosodium urate crystal-induced inflammation by scopoletin and underlying mechanisms. Int Immunopharmacol. 2012;14(4):454–62.\nMylona EE, Mouktaroudi M, Crisan TO, Makri S, Pistiki A, Georgitsi M, et al. Enhanced interleukin-1β production of PBMCs from patients with gout after stimulation with Toll-like receptor-2 ligands and urate crystals. Arthritis Res Ther. 2012;4(4):R158.\nMargalit A, Duffin KL, Shaffer AF, Gregory SA, Isakson PC. Altered arachidonic acid metabolism in urate crystal induced inflammation. Inflammation. 1997;21(2):205–22.\nPascual E, Batlle-Gualda E, Martínez A, Rosas J, Vela P. Synovial fluid analysis for diagnosis of intercritical gout. Ann Intern Med. 1999;131(10):756–9.\nAntommattei O, Schumacher HR, Reginato AJ, Clayburne G. Prospective study of morphology and phagocytosis of synovial fluid monosodium urate crystals in gouty arthritis. J Rheumatol. 1984;11(6):741–4.\nPerez-Ruiz F. Treating to target: a strategy to cure gout. Rheumatology (Oxford). 2009;48(2):ii9–14.\nVirtue A, Wang H, Yang XF. MicroRNAs and toll-like receptor\u002Finterleukin-1 receptor signaling. J Hematol Oncol. 2012;5:66.\nDuff GW, Atkins E, Malawista SE. The fever of gout: urate crystals activate endogenous pyrogen production from human and rabbit mononuclear phagocytes. Trans Assoc Am Physicians. 1983;96:234–45.\nDi Giovine FS, Malawista SE, Thornton E, Duff GW. Urate crystals stimulate production of tumor necrosis factor alpha from human blood monocytes and synovial cells. Cytokine mRNA and protein kinetics, and cellular distribution. J Clin Invest. 1991;7(4):1375–81.\nMasters SL, Simon A, Aksentijevich I, Kastner DL. Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*). Annu Rev Immunol. 2009;27:621–68.\nDinarello CA. Immunological and inflammatory functions of the interleukin-1 family. Annu Rev Immunol. 2009;27:519–50.\nAgostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J. NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity. 2004;20(3):319–25.\nMartinon F, Agostini L, Meylan E, Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3\u002Fcryopyrin inflammasome. Curr Biol. 2004;14(21):1929–34.\nGiamarellos-Bourboulis EJ, Mouktaroudi M, Bodar E, Van der Ven J, Kullberg BJ, Netea MG, et al. Crystals of monosodium urate monohydrate enhance lipopolysaccharide-induced release of interleukin 1 beta by mononuclear cells through a caspase 1-mediated process. Ann Rheum Dis. 2009;68(2):273–8.\nHoffman HM, Scott P, Mueller JL, Misaghi A, Stevens S, Yancopoulos GD, et al. Role of the leucine-rich repeat domain of cryopyrin\u002FNALP3 in monosodium urate crystal-induced inflammation in mice. Arthritis Rheum. 2010;62(7):2170–9.\nSchroder K, Tschopp J. The inflammasomes. Cell. 2010;140(6):821–32.\nVan de Veerdonk FL, Netea MG, Dinarello CA, Joosten LA. Inflammasome activation and IL-1β and IL-18 processing during infection. Trends Immunol. 2011;32(3):110–6.\nChen GY, Nuñez G. Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol. 2010;10(12):826–37.\nMigita K, Koga T, Satomura K, Izumi M, Torigoshi T, Maeda Y, et al. Serum amyloid A triggers the mosodium urate -mediated mature interleukin-1β production from human synovial fibroblasts. Arthritis Res Ther. 2012;14(3):R119.\nChoi AJ, Ryter SW. Inflammasomes: molecular regulation and implications for metabolic and cognitive diseases. Mol Cells. 2014;37(6):441–8.",{"EN":185},"To investigate whether monosodium urate (MSU) crystals induce interleukin (IL)-1β in human fibroblast-like synoviocytes (FLS), and whether the NLRP3 inflammasome is involved in the inflammatory mechanism. Human FLS isolated from explants of synovial tissue were stimulated with MSU crystals (0.001 to 0.5 mg\u002Fml) for different time course (6 hours to 48 hours). The expressions of IL-1β, IL-6, TNF-α and NLRP3 were evaluated with ELISA, Western blot and quantitative real-time PCR. Exposure of FLS to MSU crystals transiently induced a significant increase in IL-1β expression in culture medium with a peak at 6 h. The mRNA level of IL-1β in the FLS cells had a similar pattern at this time point. Changes in IL-6 and TNF-α expression were not observed. Simultaneously, intercellular pro-IL-1β was detected at 6 h. Furthermore, MSU crystals also induced NLRP3 mRNA and protein expression at 6 h to 48 h after MSU treatment. MSU crystals directly increased IL-1β and intercellular NLRP3 expression in FLS cells. It is suggested that the NLRP3 inflammasome may be associated with IL-1β in FLS treated with MSU. Altogether, MSU could induce production and release of IL-1β through the NLRP3 inflammasome in human synoviocytes.",{"EN":187},"Role of the NLRP3 inflammasome in the transient release of IL-1β induced by monosodium urate crystals in human fibroblast-like synoviocytes",{"VOID":189},"10.1186\u002Fs12950-015-0070-7","PUBLICATION","VERIFIED","Auto 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Trends in Biochemical Sciences. 2001, 26: 112-117. 10.1016\u002FS0968-0004(00)01745-X.\nWiley JS, Dao-Ung LP, Gu BJ, Sluyter R, Shemon AN, Li C, Taper J, Gallo J, Manoharan A: A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: a molecular study. Lancet. 2002, 359 (9312): 1114-1119. 10.1016\u002FS0140-6736(02)08156-4.\nSellick GS, Rudd M, Eve P, Allinson R, Matutes E, Catovsky D, Houlston RS: The P2X7 Receptor Gene A1513C Polymorphism Does Not Contribute to Risk of Familial or Sporadic Chronic Lymphocytic Leukemia. Cancer Epidemiol Biomarkers Prev. 2004, 13: 1065-1067.\nThunberg U, Tobin G, Johnson A, Soderberg O, Padyukov L, Hultdin M, Klareskog L, Enblad G, Sundstrom C, Roos G, Rosenquist R: Polymorphism in the P2X7 receptor gene and survival in chronic lymphocytic leukaemia. Lancet. 2002, 360 (9349): 1935-1939. 10.1016\u002FS0140-6736(02)11917-9.\nCarta S, Tassi S, Semino C, Fossati G, Mascagni P, Dinarello CA, Rubartelli A: Histone deacetylase inhibitors prevent exocytosis of interleukin-1{beta}-containing secretory lysosomes: role of microtubules. Blood. 2006",{"EN":396},"The inflammatory process, orchestrated against a variety of injurious stimuli, is composed of three inter-related phases; initiation, propagation and resolution. Understanding the interplay between these three phases and harnessing the beneficial properties of inflammation whilst preventing its damaging effects, will undoubtedly lead to the advent of much needed therapies, particularly in chronic disease states. The P2X7 receptor (P2X7R) is increasingly recognised as an important cell surface regulator of several key inflammatory molecules including IL-1β, IL-18, TNF-α and IL-6. Moreover, as P2X7R-dependent cytokine production is driven by activating the inflammasome, antagonists of this receptor are likely to have therapeutic potential as novel anti-inflammatory therapies. The function of the P2X7R in inflammation, immunity and its potential role in disease will be reviewed and discussed.",{"EN":398},"The role of the purinergic P2X7 receptor in inflammation",{"VOID":400},"10.1186\u002F1476-9255-4-5","https:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002F1476-9255-4-5",[403,418,433,445,457,469,481],{"id":404,"sortIndex":202,"researcher":18,"roles":405,"affiliations":406,"properties":415},"318ebfc2-ad17-454b-ad6f-00b3ea9b5b9b",[198],[407],{"id":18,"sortIndex":19,"affiliation":408,"properties":18},{"id":409,"createTime":410,"updateTime":410,"relativeEntities":411,"slug":18,"properties":412,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"761ffd73-bfe4-47a1-959f-b7f0302fe852","2024-01-13T15:34:09.978+00:00",[],{"title":413},{"VI":414},"Astellas CNS Research in Edinburgh, The Chancellor's Building, The University of Edinburgh, 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               \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>Abnormal and deregulated skin wound healing associated with prolonged inflammation may result in dermal fibrosis. Since the current therapeutic strategies revealed unsatisfactory, the investigation of alternative approaches such as those based on the use of specific probiotic strains could provide promising therapeutic options. In this study, we aimed to evaluate whether the lysate from \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> could antagonize the fibrogenic effects of TGF-β1 in normal human dermal fibroblasts (NHDF).\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Methods\u003C\u002Fjats:title>\n                \u003Cjats:p>NHDF were exposed to TGF-β1 to establish a fibrotic phenotype. Proliferation rate and cell number were measured using the IncuCyte® Live Cell Imager system and the trypan blue dye exclusion test. Phenoconversion markers (α-SMA and fibronectin) and collagen I levels were assessed by western blot and immunofluorescence. The mRNA levels of TGF-β1 were evaluated by RT-PCR. The Smad2\u002F3 phosphorylation level as well as β-catenin and PPARγ expression, were assessed by western blot. The cell contractility function and migration of NHDF were studied using collagen gel retraction assay, and scratch wound healing assay, respectively. The effects of \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> lysate, alone or combined with TGF-β1, were evaluated on all of the above-listed parameters and markers associated with TGF-β1-induced fibrotic phenotype.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>Exposure to the \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> lysate significantly reduced the key mediators and events involved in the abnormal activation of myofibroblasts by TGF-β1 within the fibrotic profile. The \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> treatment significantly reduced cell proliferation, migration, and myo-differentiation. In addition, the treatment with probiotic lysate reduced the α-SMA, fibronectin, collagen-I expression levels, and affected the collagen contraction ability of activated dermal fibroblasts. Moreover, the probiotic targeted the TGF-β1 signaling, reducing Smad2\u002F3 activation, TGF-β1 mRNA level, and β-catenin expression through the upregulation of PPARγ.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusion\u003C\u002Fjats:title>\n                \u003Cjats:p>This is the first report showing that \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> lysate had a remarkable anti-fibrotic effect in TGF-β1-activated NHDF by inhibiting Smad signaling. Notably, the probiotic was able to reduce β-catenin and increase PPARγ levels. The findings support our point that \u003Cjats:italic>S. thermophilus\u003C\u002Fjats:italic> may help prevent or treat hypertrophic scarring and keloids.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":604},"Efficacy of probiotic Streptococcus thermophilus in counteracting TGF-β1-induced fibrotic response in normal human dermal 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Sci Rep. 2020;10:17300.",{"doi":804},"10.1038\u002Fs41598-020-74179-6",{"id":18,"text":806,"url":18,"identifiers":807},"Liu J, Deng T, Wang Y, Zhang M, Zhu G, Fang H, Wang J. Calycosin inhibits intestinal fibrosis on CCD-18Co cells via modulating transforming growth Factor-beta\u002FSmad signaling pathway. Pharmacology. 2019;104:81–9.",{"doi":808},"10.1159\u002F000500186",{"id":18,"text":810,"url":18,"identifiers":811},"Griffin MF, Huber J, Evan FJ, Quarto N, Longaker MT. The role of wnt signaling in skin fibrosis. Med Res Rev. 2022;42:615–28.",{"doi":812},"10.1002\u002Fmed.21853",{"id":18,"text":814,"url":18,"identifiers":815},"MacDonald BT, Tamai K, He X. Wnt\u002Fbeta-catenin signaling: components, mechanisms, and diseases. Dev Cell. 2009;17:9–26.",{"doi":816},"10.1016\u002Fj.devcel.2009.06.016",{"id":18,"text":818,"url":18,"identifiers":819},"Mullin NK, Mallipeddi NV, Hamburg-Shields E, Ibarra B, Khalil AM, Atit RP. Wnt\u002Fbeta-catenin signaling pathway regulates specific lncRNAs that impact dermal fibroblasts and skin fibrosis. Front Genet. 2017;8:183.",{"doi":820},"10.3389\u002Ffgene.2017.00183",{"id":18,"text":822,"url":18,"identifiers":823},"Akhmetshina A, Palumbo K, Dees C, Bergmann C, Venalis P, Zerr P, et al. Activation of canonical wnt signalling is required for TGF-beta-mediated fibrosis. Nat Commun. 2012;3:735.",{"doi":824},"10.1038\u002Fncomms1734",{"id":18,"text":826,"url":18,"identifiers":827},"Cheon SS, Wei QX, Gurung A, Youn A, Bright T, Poon R, Whetstone H, Guha A, Alman BA. Beta-catenin regulates wound size and mediates the effect of TGF-beta in cutaneous healing. Faseb J. 2006;20:692–701.",{"doi":828},"10.1096\u002Ffj.05-4759com",{"id":18,"text":830,"url":18,"identifiers":831},"Vallee A, Lecarpentier Y. TGF-beta in fibrosis by acting as a conductor for contractile properties of myofibroblasts. 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Arch Dermatol Res. 2013;305:341–52.",{"doi":940},"10.1007\u002Fs00403-013-1314-0",{"id":18,"text":942,"url":18,"identifiers":943},"Shi JH, Li J, Guan H, Cai WX, Bai XZ, Fang XB, et al. Anti-fibrotic actions of Interleukin-10 against hypertrophic scarring by activation of PI3K\u002FAKT and STAT3 signaling pathways in scar-forming fibroblasts. Plos One. 2014;9:e98228.",{"doi":944},"10.1371\u002Fjournal.pone.0098228",{"id":18,"text":946,"url":18,"identifiers":947},"La Torre C, Cinque B, Lombardi F, Miconi G, Palumbo P, Evtoski Z, Placidi G, Fanini D, Cimini AM, Benedetti E, et al. Nitric oxide chemical donor affects the early phases of in vitro wound healing process. J Cell Physiol. 2016;231:2185–95.",{"doi":948},"10.1002\u002Fjcp.25331",{"id":18,"text":950,"url":18,"identifiers":951},"Ngo P, Ramalingam P, Phillips JA, Furuta GT. Collagen gel contraction assay. Methods Mol Biol. 2006;341:103–9.",{},{"id":953,"createTime":954,"updateTime":955,"relativeEntities":956,"slug":957,"properties":958,"entityType":190,"verifyStatus":191,"verifyTime":955,"verifyNote":192,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":967,"fullTextUrl":18,"authors":968,"publicationType":349,"publisherRelationship":1013,"citationCount":18,"citationInfo":18,"publishDate":1046,"publishYear":1047,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":385},"7f1f40ef-3294-4b99-945a-3e06ecb6c9f7","2023-12-15T07:11:40.770+00:00","2025-01-02T23:50:04.092+00:00",[],"TGF-%CE%B2-gene-polimorphisms-as-risk-factors-for-asthma-control-among-clinic-patients",{"references":959,"abstract":961,"title":963,"doi":965},{"VOID":960},"GINA Main Report dostępny na 2019https:\u002F\u002Fginasthma.org\u002F\nDroszcz W, Grzanka A. Asthma in adolescents and adults. 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Biometrics. 1988;44(3):837–45. https:\u002F\u002Fdoi.org\u002F10.2307\u002F2531595.",{"EN":962},"TGF-β and its receptors play a crucial role in asthma pathogenesis, bronchial hyperreactivity, and bronchial remodeling. Expression of isoforms 1–3 of TGFβ cytokine is influenced by tagging polymorphisms in the TGFβ1, TGFβ2 and TGFβ3 gene, and these SNPs may be associated with the risk of asthma development and severity as well as with other diseases. Polymorphic forms of TGF-β1, TGF-β2 and TGF-β3 genes regulate the degree of bronchial inflammation, deterioration of lung functional parameters in spirometry and elevated level of total IgE. All this results in intensification of disease symptoms. According to current GINA 2020 guidelines, the Asthma Control Test (ACT™) should be applied to assess asthma symptoms. An analysis of polymorphisms localized in TGF-β1, TGF-β2 and TGF-β3 genes was conducted on 652 DNA samples with an application of the MassARRAY® system using the mass spectrometry technique MALDI TOF MS. The degree of asthma control was evaluated with ACT™. The occurrence of the T \u002F C genotype in rs8109627 (p = 0.0171) in the TGF-β1 gene is significantly associated with a higher ACT result (controlled asthma) in a multivariate linear regression analysis model after using backward stepwise selection of variables. In addition, in the linear model for prediction of ACT score we showed SNP rs8109627 (p = 0.0497) in the TGF-β1 gene (improvement of the disease control - controlled asthma) and rs2796822 (p = 0.0454) in the TGF-β2 gene (deterioration of the diseases control - uncontrolled asthma) significantly modify the degree of asthma control. We described clinical significance of two SNPs in two genes TGF-β1 and TGF-β2, as yet unknown. We proved that the use of both genotypes and MAC allows to create a moderately correct prognostic model which is about 70% efficient on the entire set of analyzed SNPs in TGF-β1, TGF-β2, and TGF-β3 genes.",{"EN":964},"TGF-β gene polimorphisms as risk factors for asthma control among clinic patients",{"VOID":966},"10.1186\u002Fs12950-021-00294-4","https:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12950-021-00294-4",[969,984,996],{"id":970,"sortIndex":19,"researcher":18,"roles":971,"affiliations":972,"properties":981},"5403d310-5d0b-44c6-9e8c-f7aa8894681c",[198],[973],{"id":18,"sortIndex":19,"affiliation":974,"properties":18},{"id":975,"createTime":976,"updateTime":976,"relativeEntities":977,"slug":18,"properties":978,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"73288770-16a4-4628-b15f-807162b7c9ff","2023-12-15T07:11:23.633+00:00",[],{"title":979},{"VI":980},"Department of Internal Medicine, Asthma and Allergy, Medical University of Lodz, Łódź, Poland",{"title":982},{"VI":983},"Panek Michał",{"id":985,"sortIndex":116,"researcher":18,"roles":986,"affiliations":987,"properties":993},"cfcd4064-e437-44e2-b1b5-b2a39324c880",[198],[988],{"id":18,"sortIndex":19,"affiliation":989,"properties":18},{"id":975,"createTime":976,"updateTime":976,"relativeEntities":990,"slug":18,"properties":991,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":992},{"VI":980},{"title":994},{"VI":995},"Kuna 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Curr Med Chem. 2007, 14: 243-248. 10.2174\u002F092986707779313381.\nBustos C, Hernandez-Presa MA, Ortego M, Tunon J, Ortega L, Perez F, Diaz C, Hernandez G, Egido J: HMG-CoA reductase inhibition by atorvastatin reduces neointimal inflammation in a rabbit model of atherosclerosis. J Am Coll Cardiol. 1998, 32: 2057-2064. 10.1016\u002FS0735-1097(98)00487-2.\nChung HK, Lee IK, Kang H, Suh JM, Kim H, Park KC, Kim DW, Kim YK, Ro HK, Shong M: Statin inhibits interferon-gamma-induced expression of intercellular adhesion molecule-1 (ICAM-1) in vascular endothelial and smooth muscle cells. Exp Mol Med. 2002, 34: 451-461.\nStefanick ML, Mackey S, Sheehan M, Ellsworth N, Haskell WL, Wood PD: Effects of diet and exercise in men and postmenopausal women with low levels of HDL cholesterol and high levels of LDL cholesterol. N Engl J Med. 1998, 339: 12-20. 10.1056\u002FNEJM199807023390103.\nHaskell WL, Lee IM, Pate RR, Powell KE, Blair SN, Franklin BA, Macera CA, Heath GW, Thompson PD, Bauman A: Physical activity and public health: updated recommendation for adults from the American College of Sports Medicine and the American Heart Association. Med Sci Sports Exerc. 2007, 39: 1423-1434. 10.1249\u002Fmss.0b013e3180616b27.\nKingwell BA: Nitric oxide-mediated metabolic regulation during exercise: effects of training in health and cardiovascular disease. FASEB J. 2000, 14: 1685-1696. 10.1096\u002Ffj.99-0896rev.\nMaxwell AJ, Schauble E, Bernstein D, Cooke JP: Limb blood flow during exercise is dependent on nitric oxide. Circulation. 1998, 98: 369-374.\nDurstine JL, Grandjean PW, Davis PG, Ferguson MA, Alderson NL, DuBose KD: Blood lipid and lipoprotein adaptations to exercise: a quantitative analysis. Sports Med. 2001, 31: 1033-1062. 10.2165\u002F00007256-200131150-00002.\nGoto C, Nishioka K, Umemura T, Jitsuiki D, Sakagutchi A, Kawamura M, Chayama K, Yoshizumi M, Higashi Y: Acute moderate-intensity exercise induces vasodilation through an increase in nitric oxide bioavailiability in humans. Am J Hypertens. 2007, 20: 825-830. 10.1016\u002Fj.amjhyper.2007.02.014.\nde Moraes C, Davel AP, Rossoni LV, Antunes E, Zanesco A: Exercise training improves relaxation response and SOD-1 expression in aortic and mesenteric rings from high caloric diet-fed rats. BMC Physiol. 2008, 8: 12-10.1186\u002F1472-6793-8-12.\nBai Y, Sigala W, Adams GR, Vaziri ND: Effect of exercise on cardiac tissue oxidative and inflammatory mediators in chronic kidney disease. Am J Nephrol. 2009, 29: 213-221. 10.1159\u002F000156715.\nPeake J, Nosaka K, Suzuki K: Characterization of inflammatory responses to eccentric exercise in humans. Exerc Immunol Rev. 2005, 11: 64-85.\nPedersen BK, Febbraio MA: Muscle as an endocrine organ: focus on muscle-derived interleukin-6. Physiol Rev. 2008, 88: 1379-1406. 10.1152\u002Fphysrev.90100.2007.\nPedersen BK: The diseasome of physical inactivity--and the role of myokines in muscle--fat cross talk. J Physiol. 2009, 587: 5559-5568. 10.1113\u002Fjphysiol.2009.179515.\nPedersen BK, Akerstrom TC, Nielsen AR, Fischer CP: Role of myokines in exercise and metabolism. J Appl Physiol. 2007, 103: 1093-1098. 10.1152\u002Fjapplphysiol.00080.2007.\nPedersen BK, Fischer CP: Physiological roles of muscle-derived interleukin-6 in response to exercise. Curr Opin Clin Nutr Metab Care. 2007, 10: 265-271. 10.1097\u002FMCO.0b013e3280ebb5b3.\nPedersen BK, Hoffman-Goetz L: Exercise and the immune system: regulation, integration, and adaptation. Physiol Rev. 2000, 80: 1055-1081.\nReese EP: Arthritis; the use of physical therapy as an aspect of management. Calif Med. 1958, 89: 204-209.\nOberbach A, Lehmann S, Kirsch K, Krist J, Sonnabend M, Linke A, Tonjes A, Stumvoll M, Bluher M, Kovacs P: Long-term exercise training decreases interleukin-6 (IL-6) serum levels in subjects with impaired glucose tolerance: effect of the -174G\u002FC variant in IL-6 gene. Eur J Endocrinol. 2008, 159: 129-136. 10.1530\u002FEJE-08-0220.\nLemos ET, Reis F, Baptista S, Pinto R, Sepodes B, Vala H, Rocha-Pereira P, Silva GC, Teixeira N, Silva AS: Exercise training decreases proinflammatory profile in Zucker diabetic (type 2) fatty rats. Nutrition. 2008, 25: 330-9. 10.1016\u002Fj.nut.2008.08.014.\nWilund KR: Is the anti-inflammatory effect of regular exercise responsible for reduced cardiovascular disease?. Clin Sci (Lond). 2007, 112: 543-555. 10.1042\u002FCS20060368.\nRich PR: The molecular machinery of Keilin's respiratory chain. Biochem Soc Trans. 2003, 31: 1095-1105. 10.1042\u002FBST0311095.\nBloomer RJ: Effect of exercise on oxidative stress biomarkers. Adv Clin Chem. 2008, 46: 1-50. full_text.\nJi LL: Antioxidants and oxidative stress in exercise. Proc Soc Exp Biol Med. 1999, 222: 283-292. 10.1046\u002Fj.1525-1373.1999.d01-145.x.\nBrennan ML, Penn MS, Van LF, Nambi V, Shishehbor MH, Aviles RJ, Goormastic M, Pepoy ML, McErlean ES, Topol EJ: Prognostic value of myeloperoxidase in patients with chest pain. N Engl J Med. 2003, 349: 1595-1604. 10.1056\u002FNEJMoa035003.\nMeilhac O, Ramachandran S, Chiang K, Santanam N, Parthasarathy S: Role of arterial wall antioxidant defense in beneficial effects of exercise on atherosclerosis in mice. Arterioscler Thromb Vasc Biol. 2001, 21: 1681-1688. 10.1161\u002Fhq1001.097106.\nMignini F, Tomassoni D, Traini E, Streccioni V: Antioxidant endogenous defense in a human model of physical stress. Clin Exp Hypertens. 2008, 30: 776-784. 10.1080\u002F07420520802572341.\nSeals DR, Desouza CA, Donato AJ, Tanaka H: Habitual exercise and arterial aging. J Appl Physiol. 2008, 105: 1323-1332. 10.1152\u002Fjapplphysiol.90553.2008.\nFukai T, Siegfried MR, Ushio-Fukai M, Cheng Y, Kojda G, Harrison DG: Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training. J Clin Invest. 2000, 105: 1631-1639. 10.1172\u002FJCI9551.\nSun MW, Zhong MF, Gu J, Qian FL, Gu JZ, Chen H: Effects of different levels of exercise volume on endothelium-dependent vasodilation: roles of nitric oxide synthase and heme oxygenase. Hypertens Res. 2008, 31: 805-816. 10.1291\u002Fhypres.31.805.\nde Winther MP, Kanters E, Kraal G, Hofker MH: Nuclear factor kappaB signaling in atherogenesis. Arterioscler Thromb Vasc Biol. 2005, 25: 904-914. 10.1161\u002F01.ATV.0000160340.72641.87.",{"EN":1058},"Hypercholesterolemia is defined as excessively high plasma cholesterol levels, and is a strong risk factor for many negative cardiovascular events. Total cholesterol levels above 200 mg\u002Fdl have repeatedly been correlated as an independent risk factor for development of peripheral vascular (PVD) and coronary artery disease (CAD), and considerable attention has been directed toward evaluating mechanisms by which hypercholesterolemia may impact vascular outcomes; these include both results of direct cholesterol lowering therapies and alternative interventions for improving vascular function. With specific relevance to the microcirculation, it has been clearly demonstrated that evolution of hypercholesterolemia is associated with endothelial cell dysfunction, a near-complete abrogation in vascular nitric oxide bioavailability, elevated oxidant stress, and the creation of a strongly pro-inflammatory condition; symptoms which can culminate in profound impairments\u002Falterations to vascular reactivity. Effective interventional treatments can be challenging as certain genetic risk factors simply cannot be ignored. However, some hypercholesterolemia treatment options that have become widely used, including pharmaceutical therapies which can decrease circulating cholesterol by preventing either its formation in the liver or its absorption in the intestine, also have pleiotropic effects with can directly improve peripheral vascular outcomes. While physical activity is known to decrease PVD\u002FCAD risk factors, including obesity, psychological stress, impaired glycemic control, and hypertension, this will also increase circulating levels of high density lipoprotein and improving both cardiac and vascular function. This review will provide an overview of the mechanistic consequences of the predominant pharmaceutical interventions and chronic exercise to treat hypercholesterolemia through their impacts on chronic sub-acute inflammation, oxidative stress, and microvascular structure\u002Ffunction relationships.",{"EN":1060},"Hypercholesterolemia and microvascular dysfunction: interventional 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Brock",{"id":1091,"sortIndex":116,"researcher":18,"roles":1092,"affiliations":1093,"properties":1106},"5f59a4b2-dab7-47cc-9c2c-eb363b83633a",[198],[1094,1101],{"id":1095,"sortIndex":202,"affiliation":1096,"properties":1100},"c1ebb7eb-600f-4cf3-a985-f3ee1a88a0d9",{"id":1072,"createTime":1073,"updateTime":1073,"relativeEntities":1097,"slug":18,"properties":1098,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1099},{"VI":1077},{},{"id":18,"sortIndex":19,"affiliation":1102,"properties":18},{"id":1081,"createTime":1082,"updateTime":1082,"relativeEntities":1103,"slug":18,"properties":1104,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1105},{"VI":1086},{"title":1107},{"VI":1108},"Milinda E 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USA",{},{"id":18,"sortIndex":19,"affiliation":1124,"properties":18},{"id":1081,"createTime":1082,"updateTime":1082,"relativeEntities":1125,"slug":18,"properties":1126,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1127},{"VI":1086},{"title":1129},{"VI":1130},"Phoebe A 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Am J Pathol. 2003, 163 (6): 2555-2563.\nOtterbein LE, Bach FH, Alam J, Soares M, Tao Lu H, Wysk M, Davis RJ, Flavell RA, Choi AM: Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway. Nat Med. 2000, 6 (4): 422-428. 10.1038\u002F74680.\nZuckerbraun BS, McCloskey CA, Gallo D, Liu F, Ifedigbo E, Otterbein LE, Billiar TR: Carbon monoxide prevents multiple organ injury in a model of hemorrhagic shock and resuscitation. Shock. 2005, 23 (6): 527-532.\nHoetzel A, Dolinay T, Schmidt R, Choi AM, Ryter SW: Carbon monoxide in sepsis. Antioxid Redox Signal. 2007, 9 (11): 2013-2026. 10.1089\u002Fars.2007.1762.\nMayr FB, Spiel A, Leitner J, Marsik C, Germann P, Ullrich R, Wagner O, Jilma B: Effects of carbon monoxide inhalation during experimental endotoxemia in humans. Am J Respir Crit Care Med. 2005, 171 (4): 354-360. 10.1164\u002Frccm.200404-446OC.\nAberg AM, Hultin M, Abrahamsson P, Larsson JE: Circulatory effects and kinetics following acute administration of carbon monoxide in a porcine model. Life Sci. 2004, 75 (9): 1029-1039. 10.1016\u002Fj.lfs.2003.12.030.\nSundin AM, Larsson JE: Rapid and sensitive method for the analysis of carbon monoxide in blood using gas chromatography with flame ionisation detection. Journal of chromatography. 2002, 766 (1): 115-121. 10.1016\u002FS0378-4347(01)00460-1.\nMazzola S, Forni M, Albertini M, Bacci ML, Zannoni A, Gentilini F, Lavitrano M, Bach FH, Otterbein LE, Clement MG: Carbon monoxide pretreatment prevents respiratory derangement and ameliorates hyperacute endotoxic shock in pigs. Faseb J. 2005, 19 (14): 2045-2047.\nTuchscherer M, Kanitz E, Puppe B, Tuchscherer A, Stabenow B: Effects of postnatal social isolation on hormonal and immune responses of pigs to an acute endotoxin challenge. Physiol Behav. 2004, 82 (2-3): 503-511. 10.1016\u002Fj.physbeh.2004.04.056.\nBrix-Christensen V, Gjedsted J, Andersen SK, Vestergaard C, Nielsen J, Rix T, Nyboe R, Andersen NT, Larsson A, Schmitz O, Tonnesen E: Inflammatory response during hyperglycemia and hyperinsulinemia in a porcine endotoxemic model: the contribution of essential organs. Acta Anaesthesiol Scand. 2005, 49 (7): 991-998. 10.1111\u002Fj.1399-6576.2005.00749.x.\nMyers MJ, Farrell DE, Palmer DC, Post LO: Inflammatory mediator production in swine following endotoxin challenge with or without co-administration of dexamethasone. Int Immunopharmacol. 2003, 3 (4): 571-579. 10.1016\u002FS1567-5769(03)00048-1.\nGoldfarb RD, Dellinger RP, Parrillo JE: Porcine models of severe sepsis: emphasis on porcine peritonitis. Shock. 2005, 24 Suppl 1: 75-81. 10.1097\u002F01.shk.0000191337.01036.b7.\nSwindle MM, Smith AC, Hepburn BJ: Swine as models in experimental surgery. J Invest Surg. 1988, 1 (1): 65-79. 10.3109\u002F08941938809141077.\nKonrad D, Haney M, Johansson G, Wanecek M, Weitzberg E, Oldner A: Cardiac effects of endothelin receptor antagonism in endotoxemic pigs. American journal of physiology. 2007, 293 (2): H988-96.\nFrank JW, Carroll JA, Allee GL, Zannelli ME: The effects of thermal environment and spray-dried plasma on the acute-phase response of pigs challenged with lipopolysaccharide. J Anim Sci. 2003, 81 (5): 1166-1176.\nBergmann M, Gornikiewicz A, Tamandl D, Exner R, Roth E, Fugger R, Gotzinger P, Sautner T: Continuous therapeutic epinephrine but not norepinephrine prolongs splanchnic IL-6 production in porcine endotoxic shock. Shock. 2003, 20 (6): 575-581. 10.1097\u002F01.shk.0000095934.86703.83.\nJaveshghani D, Magder S: Regional changes in constitutive nitric oxide synthase and the hemodynamic consequences of its inhibition in lipopolysaccharide-treated pigs. Shock. 2001, 16 (3): 232-238.\nNalos M, Vassilev D, Pittner A, Asfar P, Bruckner UB, Schneider EM, Georgieff M, Radermacher P, Froeba G: Tin-mesoporphyrin for inhibition of heme oxygenase during long-term hyperdynamic porcine endotoxemia. Shock. 2003, 19 (6): 526-532. 10.1097\u002F01.shk.0000070732.34700.07.\nKondo A, Saito Y, Seki A, Sugiura C, Maegaki Y, Nakayama Y, Yagi K, Ohno K: Delayed neuropsychiatric syndrome in a child following carbon monoxide poisoning. Brain Dev. 2007, 29 (3): 174-177. 10.1016\u002Fj.braindev.2006.08.002.\nMannaioni PF, Vannacci A, Masini E: Carbon monoxide: the bad and the good side of the coin, from neuronal death to anti-inflammatory activity. Inflamm Res. 2006, 55 (7): 261-273. 10.1007\u002Fs00011-006-0084-y.\nEkblom B, Huot R: Response to submaximal and maximal exercise at different levels of carboxyhemoglobin. Acta Physiol Scand. 1972, 86 (4): 474-482.\nAnderson EW, Andelman RJ, Strauch JM, Fortuin NJ, Knelson JH: Effect of low-level carbon monoxide exposure on onset and duration of angina pectoris. A study in ten patients with ischemic heart disease. Ann Intern Med. 1973, 79 (1): 46-50.\nAronow WS, Isbell MW: Carbon monoxide effect on exercise-induced angina pectoris. Ann Intern Med. 1973, 79 (3): 392-395.\nAronow WS, Stemmer EA, Isbell MW: Effect of carbon monoxide exposure on intermittent claudication. Circulation. 1974, 49 (3): 415-417.\nAronow WS: Aggravation of angina pectoris by two percent carboxyhemoglobin. Am Heart J. 1981, 101 (2): 154-157. 10.1016\u002F0002-8703(81)90658-X.\nKlimisch HJ, Chevalier HJ, Harke HP, Dontenwill W: Uptake of carbon monoxide in blood of miniture pigs and other mammals. Toxicology. 1975, 3 (3): 301-310. 10.1016\u002F0300-483X(75)90031-1.\nWestphal M, Weber TP, Meyer J, von Kegler S, Van Aken H, Booke M: Affinity of carbon monoxide to hemoglobin increases at low oxygen fractions. Biochem Biophys Res Commun. 2002, 295 (4): 975-977. 10.1016\u002FS0006-291X(02)00781-7.",{"EN":1214},"Carbon monoxide (CO) has recently been suggested to have anti-inflammatory properties, but data seem to be contradictory and species-specific. Thus, in studies on macrophages and mice, pretreatment with CO attenuated the inflammatory response after endotoxin exposure. On the other hand, human studies showed no effect of CO on the inflammatory response. Anti-inflammatory efficacy of CO has been shown at concentrations above 10% carboxyhaemoglobin. This study was undertaken to elucidate the possible anti-inflammatory effects of CO at lower CO concentrations. Effects of CO administration on cytokine (TNF-alpha, IL-6, IL-1beta and IL-10) release were investigated in a porcine model in which a systemic inflammatory response syndrome was induced by endotoxin infusion. Endotoxin was infused in 20 anaesthetized and normoventilated pigs. Ten animals were targeted with inhaled CO to maintain 5% COHb, and 10 animals were controls. In the control group, mean pulmonary artery pressure increased from a baseline value of 17 mmHg (mean, n = 10) to 42 mmHg (mean, n = 10) following 1 hour of endotoxin infusion. Similar mean pulmonary artery pressure values were found in animals exposed to carbon monoxide. Plasma levels of all of the measured cytokines increased in response to the endotoxin infusion. The largest increase was observed in TNF-alpha, which peaked after 1.5 hours at 9398 pg\u002Fml in the control group and at 13395 pg\u002Fml in the carbon monoxide-exposed group. A similar peak was found for IL-10 while the IL-6 concentration was maximal after 2.5 hours. IL-1beta concentrations increased continuously during the experiment. There were no significant differences between carbon monoxide-exposed animals and controls in any of the measured cytokines. Our conclusion is that 5% COHb does not modify the cytokine response following endotoxin infusion in pigs.",{"EN":1216},"Does carbon monoxide treatment alter cytokine levels after endotoxin infusion in pigs? A randomized controlled study",{"VOID":1218},"10.1186\u002F1476-9255-5-13","http:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002F1476-9255-5-13",[1221,1236,1248,1260,1272,1284],{"id":1222,"sortIndex":132,"researcher":18,"roles":1223,"affiliations":1224,"properties":1233},"ca39ab60-8bbf-40cd-ad96-aae01dd4f240",[198],[1225],{"id":18,"sortIndex":19,"affiliation":1226,"properties":18},{"id":1227,"createTime":1228,"updateTime":1228,"relativeEntities":1229,"slug":18,"properties":1230,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"e3672958-2643-412b-83f5-cdbcea18442d","2023-12-17T23:34:30.615+00:00",[],{"title":1231},{"VI":1232},"Division of Anaesthesiology and Intensive Care Medicine, Department of Surgical and Perioperative Sciences, Umeå University Hospital, Umeå, Sweden",{"title":1234},{"VI":1235},"Jan Erik Larsson",{"id":1237,"sortIndex":236,"researcher":18,"roles":1238,"affiliations":1239,"properties":1245},"495c600d-0a36-4592-8b6b-81cacacd72c5",[198],[1240],{"id":18,"sortIndex":19,"affiliation":1241,"properties":18},{"id":1227,"createTime":1228,"updateTime":1228,"relativeEntities":1242,"slug":18,"properties":1243,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1244},{"VI":1232},{"title":1246},{"VI":1247},"Michael 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Åberg",{"id":1261,"sortIndex":312,"researcher":18,"roles":1262,"affiliations":1263,"properties":1269},"9a7d0857-e3ed-43e6-9f05-9452b19076e0",[198],[1264],{"id":18,"sortIndex":19,"affiliation":1265,"properties":18},{"id":1227,"createTime":1228,"updateTime":1228,"relativeEntities":1266,"slug":18,"properties":1267,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1268},{"VI":1232},{"title":1270},{"VI":1271},"Ola 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M, et al. 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Brain Res. 2016;1649(Pt B):143–50.\nMaday S, Holzbaur EL. Compartment-specific regulation of autophagy in primary neurons. J Neurosci. 2016;36(22):5933–45.\nSon JH, et al. Neuronal autophagy and neurodegenerative diseases. Exp Mol Med. 2012;44(2):89.\nZiv NE, Spira ME. Axotomy induces a transient and localized elevation of the free intracellular calcium concentration to the millimolar range. J Neurophysiol. 1995;74(6):2625–37.\nKnöferle J, et al. Mechanisms of acute axonal degeneration in the optic nerve in vivo. Proc Natl Acad Sci. 2010;107(13):6064–9.\nWong E, Cuervo AM. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci. 2010;13(7):805.\nFrake RA, et al. Autophagy and neurodegeneration. J Clin Invest. 2015;125(1):65–74.\nWong YC, Holzbaur EL. Autophagosome dynamics in neurodegeneration at a glance. J Cell Sci. 2015;128(7):1259–67.\nKiriyama Y, Nochi H. The function of autophagy in neurodegenerative diseases. Int J Mol Sci. 2015;16(11):26797–812.\nDello Russo C, et al. mTOR kinase, a key player in the regulation of glial functions: relevance for the therapy of multiple sclerosis. Glia. 2013;61(3):301–11.\nRusso CD, et al. Involvement of mTOR kinase in cytokine-dependent microglial activation and cell proliferation. Biochem Pharmacol. 2009;78(9):1242–51.\nRodolfo C, Campello S, Cecconi F. Mitophagy in neurodegenerative diseases. Neurochem Int. 2018;117:156–66.\nBanerjee R, Beal MF, Thomas B. Autophagy in neurodegenerative disorders: pathogenic roles and therapeutic implications. Trends Neurosci. 2010;33(12):541–9.\nNixon RA. The role of autophagy in neurodegenerative disease. Nat Med. 2013;19(8):983.\nMartinez-Vicente M. Neuronal mitophagy in neurodegenerative diseases. Front Mol Neurosci. 2017;10:64.\nXu J, et al. Regional protein expression in human Alzheimer’s brain correlates with disease severity. Commun Biol. 2019;2(1):43.\nSato S, et al. Loss of autophagy in dopaminergic neurons causes Lewy pathology and motor dysfunction in aged mice. Sci Rep. 2018;8(1):2813.\nLópez-Pérez Ó, et al. Dysregulation of autophagy in the central nervous system of sheep naturally infected with classical scrapie. Sci Rep. 2019;9:1.\nLiu X, et al. Autophagy dysfunction in neuropathic pain. Neuropeptides. 2019;75(June):41–48\nShen S, et al. The end of autophagic cell death?. Autophagy. 2012;8(1):1–3.\nWu JJ, et al. Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy. Aging. 2009;1(4):425.\nAlirezaei M, et al. Elevated ATG5 expression in autoimmune demyelination and multiple sclerosis. Autophagy. 2009;5(2):152–8.\nChoileain SN, Astier AL. CD46 plasticity and its inflammatory bias in multiple sclerosis. Arch Immunol Ther Exp. 2011;59(1):49–59.\nYang Z, Goronzy JJ, Weyand CM. Autophagy in autoimmune disease. J Mol Med. 2015;93(7):707–17.\nConsortium WTCC. Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls. Nature. 2007;447(7145):661.\nFriese MA, Fugger L. Autoreactive CD8+ T cells in multiple sclerosis: a new target for therapy? Brain. 2005;128(8):1747–63.\nPaludan C, et al. Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science. 2005;307(5709):593–6.\nNedjic J, et al. Autophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance. Nature. 2008;455(7211):396.\nBhattacharya A, et al. Deficiency of autophagy in dendritic cells protects against experimental autoimmune encephalomyelitis. J Biol Chem. 2014;289(38):26525–32.\nCooney R, et al. NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation. Nat Med. 2010;16(1):90.\nShaw SY, et al. Selective modulation of autophagy, innate immunity, and adaptive immunity by small molecules. ACS Chem Biol. 2013;8(12):2724–33.\nLiguori M, et al. Combined microRNA and mRNA expression analysis in pediatric multiple sclerosis: an integrated approach to uncover novel pathogenic mechanisms of the disease. Hum Mol Genet. 2017;27(1):66–79.\nJia W, et al. Autophagy regulates endoplasmic reticulum homeostasis and calcium mobilization in T lymphocytes. J Immunol. 2011;186(3):1564–74.\nPua HH, He Y-W. Maintaining T lymphocyte homeostasis: another duty of autophagy. Autophagy. 2007;3(3):266–7.\nMiller BC, et al. The autophagy gene ATG5 plays an essential role in B lymphocyte development. Autophagy. 2008;4(3):309–14.\nDelgoffe GM, et al. The mTOR kinase differentially regulates effector and regulatory T cell lineage commitment. Immunity. 2009;30(6):832–44.\nYin L, et al. Autophagy-related gene16L2, a potential serum biomarker of multiple sclerosis evaluated by bead-based proteomic technology. Neurosci Lett. 2014;562:34–8.\nMahad DH, Trapp BD, Lassmann H. Pathological mechanisms in progressive multiple sclerosis. Lancet Neurol. 2015;14(2):183–93.\nHara T, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature. 2006;441(7095):885.\nKomatsu M, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature. 2006;441(7095):880.\nVan Horssen J, et al. Radical changes in multiple sclerosis pathogenesis. Biochimica et Biophysica Acta (BBA)-Mol Basis Dis. 2011;1812(2):141–50.\nChen Y, et al. Oxidative stress induces autophagic cell death independent of apoptosis in transformed and cancer cells. Cell Death Differ. 2008;15(1):171.\nRubinsztein DC, et al. Potential therapeutic applications of autophagy. Nat Rev Drug Discov. 2007;6(4):304.\nRavikumar B, et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet. 2004;36(6):585.\nFeng X, et al. Defective autophagy is associated with neuronal injury in a mouse model of multiple sclerosis. Bosnian J Basic Med Sci. 2017;17(2):95.\nLeidal AM, Levine B, Debnath J. Autophagy and the cell biology of age-related disease. Nat Cell Biol. 2018;20(12):1338.\nGlass CK, et al. Mechanisms underlying inflammation in neurodegeneration. Cell. 2010;140(6):918–34.\nPatergnani S, et al. Autophagy and mitophagy elements are increased in body fluids of multiple sclerosis-affected individuals. J Neurol Neurosurg Psychiatry. 2018;89(4):439–41.\nIgci M, et al. Gene expression profiles of autophagy-related genes in multiple sclerosis. Gene. 2016;588(1):38–46.\nZhao Y, et al. Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity. Nat Cell Biol. 2010;12(7):665.\nDavid MA, Tayebi M. Detection of protein aggregates in brain and cerebrospinal fluid derived from multiple sclerosis patients. Front Neurol. 2014;5:251.\nAlbert M, et al. Synaptic pathology in the cerebellar dentate nucleus in chronic multiple sclerosis. Brain Pathol. 2017;27(6):737–47.\nRangaraju S, et al. Rapamycin activates autophagy and improves myelination in explant cultures from neuropathic mice. J Neurosci. 2010;30(34):11388–97.\nSanjuan MA, et al. Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis. Nature. 2007;450(7173):1253.\nMeikle L, et al. Response of a neuronal model of tuberous sclerosis to mammalian target of rapamycin (mTOR) inhibitors: effects on mTORC1 and Akt signaling lead to improved survival and function. J Neurosci. 2008;28(21):5422–32.\nSmith CM, Mayer JA, Duncan ID. Autophagy promotes oligodendrocyte survival and function following dysmyelination in a long-lived myelin mutant. J Neurosci. 2013;33(18):8088–100.\nAndersson Å, et al. Pivotal advance: HMGB1 expression in active lesions of human and experimental multiple sclerosis. J Leukoc Biol. 2008;84(5):1248–55.\nPark KK, et al. Promoting axon regeneration in the adult CNS by modulation of the PTEN\u002FmTOR pathway. Science. 2008;322(5903):963–6.\nRubinsztein DC, et al. Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy. 2005;1(1):11–22.",{"EN":1341},"The occurrence of neurodegenerative disease is increasingly raised. From physiopathological aspect, the emergence of auto-reactive antibodies against the nervous system antigens contributes to de-myelination in Multiple sclerosis (MS). These features cause the nervous system dysfunction. The follow-up of molecular alterations could give us a real-state vision about intracellular status during pathological circumstances. In this review, we focus on the autophagic response during MS progression and further understand the relationship between autophagy and MS and its modulatory effect on the MS evolution. The authors reviewed studies published on the autophagy status in neurodegenerative disease and on the autophagy modulation in MS prognosis, diagnosis, and possible therapies. The inevitable role of autophagy was shown in the early-stage progression of MS. Due to critical role of autophagy in different stage of cell activity in nervous system, the distinct role of autophagy should not be neglected in the development, pathogenesis, and treatment of MS.",{"EN":1343},"Real-state of autophagy signaling pathway in neurodegenerative disease; focus on multiple sclerosis",{"VOID":1345},"10.1186\u002Fs12950-020-0237-8","https:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12950-020-0237-8",[1348,1363,1378,1395,1412,1427,1454,1480],{"id":1349,"sortIndex":202,"researcher":18,"roles":1350,"affiliations":1351,"properties":1360},"598d93bc-3cd0-4863-9e11-abcc52139325",[198],[1352],{"id":18,"sortIndex":19,"affiliation":1353,"properties":18},{"id":1354,"createTime":1355,"updateTime":1355,"relativeEntities":1356,"slug":18,"properties":1357,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"c6d1f23c-648a-41ea-a082-72a1338347ba","2024-01-11T11:39:14.196+00:00",[],{"title":1358},{"VI":1359},"Department of Health Management, School of Management and Medical informatics, Tabriz University of Medical Sciences, Tabriz, Iran",{"title":1361},{"VI":1362},"Fateme Hajihassani",{"id":1364,"sortIndex":236,"researcher":18,"roles":1365,"affiliations":1366,"properties":1375},"ee6bce60-123f-43e6-aa6c-9154efa9cbff",[198],[1367],{"id":18,"sortIndex":19,"affiliation":1368,"properties":18},{"id":1369,"createTime":1370,"updateTime":1370,"relativeEntities":1371,"slug":18,"properties":1372,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"f9847dc1-61e5-48b5-9325-9fdb7ce56ebe","2024-01-11T11:39:14.216+00:00",[],{"title":1373},{"VI":1374},"Endocrine Research Center, Tabriz University of Medical Science, Tabriz, Iran",{"title":1376},{"VI":1377},"Nasser Aghamohammadzadeh",{"id":1379,"sortIndex":116,"researcher":18,"roles":1380,"affiliations":1381,"properties":1392},"ed61f921-5906-4ea2-a0a5-65719873690a",[198],[1382],{"id":18,"sortIndex":19,"affiliation":1383,"properties":18},{"id":1384,"createTime":1385,"updateTime":1386,"relativeEntities":1387,"slug":1388,"properties":1389,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"16c1cb5f-33f0-42d1-8921-802f21b2397e","2024-01-11T08:12:08.507+00:00","2024-09-05T14:30:51.066+00:00",[],"-Pediatric-Health-Research-Center-Tabriz-University-of-Medical-Sciences-Tabriz-Iran",{"title":1390},{"VI":1391}," Pediatric Health Research Center, Tabriz University of Medical Sciences, Tabriz, Iran",{"title":1393},{"VI":1394},"Amirataollah 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W, Wardlaw J, Dennis M, Lowe G, Rumley A, Sattar N, et al. The use of blood biomarkers to predict poor outcome after acute transient ischemic attack or ischemic stroke. Stroke. 2012;43:86–91.\nShichita T, Ito M, Yoshimura A. Post-ischemic inflammation regulates neural damage and protection. Front Cell Neurosci. 2014;8:319.\nDi Napoli M, Papa F, Bocola V. Prognostic influence of increased C-reactive protein and fibrinogen levels in ischemic stroke. Stroke. 2001;32:133–8.\nWhiteley W, Jackson C, Lewis S, Lowe G, Rumley A, Sandercock P, et al. Inflammatory markers and poor outcome after stroke: a prospective cohort study and systematic review of interleukin-6. PLoS Med. 2009;6:e1000145.\nBitsch A, Klene W, Murtada L, Prange H, Rieckmann P. A longitudinal prospective study of soluble adhesion molecules in acute stroke. Stroke. 1998;29:2129–35.\nWang HC, Lin WC, Lin YJ, Rau CS, Lee TH, Chang WN, et al. The association between serum adhesion molecules and outcome in acute spontaneous intracerebral hemorrhage. Crit Care. 2011;15:R284.\nYilmaz G, Granger DN. Leukocyte recruitment and ischemic brain injury. Neuromolecular Med. 2010;12:193–204.\nBlum A, Khazim K, Merei M, Peleg A, Blum N, Vaispapir V. The stroke trial - can we predict clinical outcome of patients with ischemic stroke by measuring soluble cell adhesion molecules (CAM)? Eur Cytokine Netw. 2006;17:295–8.\nWhiteley W, Chong WL, Sengupta A, Sandercock P. Blood markers for the prognosis of ischemic stroke: a systematic review. Stroke. 2009;40:e380–9.\nTurck N, Robin X, Walter N, Fouda C, Hainard A, Sztajzel R, et al. Blood glutathione S-transferase-π as a time indicator of stroke onset. PLoS One. 2012;7:e43830.\nTobin MK, Bonds JA, Minshall RD, Pelligrino DA, Testai FD, Lazarov O. Neurogenesis and inflammation after ischemic stroke: what is known and where we go from here. J Cereb Blood Flow Metab. 2014;34:1573–84.\nO’Carroll SJ, Kho DT, Wiltshire R, Nelson V, Rotimi O, Johnson R, et al. Pro-inflammatory TNFα and IL-1β differentially regulate the inflammatory phenotype of brain microvascular endothelial cells. J Neuroinflammation. 2015;12:131.\nFrijns CJ, Kappelle LJ. Inflammatory cell adhesion molecules in ischemic cerebrovascular disease. Stroke. 2002;33:2115–22.\nGrønberg NV, Johansen FF, Kristiansen U, Hasseldam H. Leukocyte infiltration in experimental stroke. J Neuroinflammation. 2013;10:115.\nHuang J, Upadhyay UM, Tamargo RJ. Inflammation in stroke and focal cerebral ischemia. Surg Neurol. 2006;66:232–45.\nCampbell DJ, Woodward M, Chalmers JP, Colman SA, Jenkins AJ, Kemp BE, et al. Soluble vascular cell adhesion molecule 1 and N-terminal pro-B-type natriuretic peptide in predicting ischemic stroke in patients with cerebrovascular disease. Arch Neurol. 2006;63:60–5.\nFrijns CJ, Kappelle LJ, van Gijn J, Nieuwenhuis HK, Sixma JJ, Fijnheer R. Soluble adhesion molecules reflect endothelial cell activation in ischemic stroke and in carotid atherosclerosis. Stroke. 1997;28:2214–8.\nStanimirovic DB, Wong J, Shapiro A, Durkin JP. Increase in surface expression of ICAM-1, VCAM-1 and E-selectin in human cerebromicrovascular endothelial cells subjected to ischemia-like insults. Acta Neurochir Suppl. 1997;70:12–6.\nCastillo J, Alvarez-Sabín J, Martínez-Vila E, Montaner J, Sobrino T, Vivancos J, et al. Inflammation markers and prediction of post-stroke vascular disease recurrence: the MITICO study. J Neurol. 2009;256:217–24.\nTchalla AE, Wellenius GA, Travison TG, Gagnon M, Iloputaife I, Dantoine T, et al. Circulating vascular cell adhesion molecule-1 is associated with cerebral blood flow dysregulation, mobility impairment, and falls in older adults. Hypertension. 2015;66:340–6.\nLenglet S, Montecucco F, Mach F, Schaller K, Gasche Y, Copin J-C. Analysis of the expression of nine secreted matrix metalloproteinases and their endogenous inhibitors in the brain of mice subjected to ischaemic stroke. Thromb Haemost. 2014;112:363–78.\nSuzuki Y, Nagai N, Umemura K, Collen D, Lijnen HR. Stromelysin-1 (MMP-3) is critical for intracranial bleeding after t-PA treatment of stroke in mice. J Thromb Haemost. 2007;5:1732–9.\nCorbin ZA, Rost NS, Lorenzano S, Kernan WN, Parides MK, Blumberg JB, et al. White matter hyperintensity volume correlates with matrix metalloproteinase-2 in acute ischemic stroke. J Stroke Cerebrovasc Dis. 2014;23:1300–6.\nBrouns R, Wauters A, De Surgeloose D, Mariën P, De Deyn PP. Biochemical markers for blood–brain barrier dysfunction in acute ischemic stroke correlate with evolution and outcome. Eur Neurol. 2011;65:23–31.\nKaplan M, Hamoud S, Tendler Y, Meilin E, Lazarovitch A, Nitecki S, et al. A significant correlation between C- reactive protein levels in blood monocytes derived macrophages versus content in carotid atherosclerotic lesions. J Inflamm (Lond). 2014;11:7.\nRajeshwar K, Kaul S, Al-Hazzani A, Babu MS, Balakrishna N, Sharma V, et al. C-reactive protein and nitric oxide levels in ischemic stroke and its subtypes: correlation with clinical outcome. Inflammation. 2012;35:978–84.\nShenhar-Tsarfaty S, Ben Assayag E, Bova I, Shopin L, Fried M, Berliner S, et al. Interleukin-6 as an early predictor for one-year survival following an ischaemic stroke\u002Ftransient ischaemic attack. Int J Stroke. 2010;5:16–20.\nBustamante A, Sobrino T, Giralt D, García-Berrocoso T, Llombart V, Ugarriza I, et al. Prognostic value of blood interleukin-6 in the prediction of functional outcome after stroke: a systematic review and meta-analysis. J Neuroimmunol. 2014;274:215–24.\nDi Napoli M, Parry-Jones AR, Smith CJ, Hopkins SJ, Slevin M, Masotti L, et al. C-reactive protein predicts hematoma growth in intracerebral hemorrhage. Stroke. 2014;45:59–65.\nMaruyama K, Shiga T, Iijima M, Moriya S, Mizuno S, Toi S, et al. Brain natriuretic peptide in acute ischemic stroke. J Stroke Cerebrovasc Dis. 2014;23:967–72.\nLlombart V, Antolin-Fontes A, Bustamante A, Giralt D, Rost NS, Furie K, et al. B-type natriuretic peptides help in cardioembolic stroke diagnosis: pooled data meta-analysis. Stroke. 2015;46:1187–95.\nFonseca AC, Brito D, Pinho e Melo T, Geraldes R, Canhão P, Caplan LR, et al. N-terminal pro-brain natriuretic peptide shows diagnostic accuracy for detecting atrial fibrillation in cryptogenic stroke patients. Int J Stroke. 2014;9:419–25.\nChen X, Zhan X, Chen M, Lei H, Wang Y, Wei D, et al. The prognostic value of combined NT-pro-BNP levels and NIHSS scores in patients with acute ischemic stroke. Intern Med. 2012;51:2887–92.\nGarcía-Berrocoso T, Giralt D, Bustamante A, Etgen T, Jensen JK, Sharma JC, et al. B-type natriuretic peptides and mortality after stroke: a systematic review and meta-analysis. Neurology. 2013;81:1976–85.\nNigro N, Wildi K, Mueller C, Schuetz P, Mueller B, Fluri F, et al. BNP but Not s-c TnIn is associated with cardioembolic aetiology and predicts short and long term prognosis after cerebrovascular events. PLoS One. 2014;9:e102704.\nDassan P, Keir G, Brown MM. Criteria for a clinically informative serum biomarker in acute ischaemic stroke: a review of S100B. Cerebrovasc Dis. 2009;27:295–302.\nWorthmann H, Tryc AB, Goldbecker A, Ma YT, Tountopoulou A, Hahn A, et al. The temporal profile of inflammatory markers and mediators in blood after acute ischemic stroke differs depending on stroke outcome. Cerebrovasc Dis. 2010;30:85–92.\nLeeflang MM, Moons KG, Reitsma JB, Zwinderman AH. Bias in sensitivity and specificity caused by data-driven selection of optimal cutoff values: mechanisms, magnitude, and solutions. Clin Chem. 2008;54:729–37.",{"EN":1553},"Inflammation is known to worsen cerebral damage at the acute phase of stroke. In this setting, cell adhesion molecules (CAMs) play a crucial role mediating migration of immune cells into the infarcted area. However, their value in long-term outcome prediction for patients with cerebrovascular diseases (CVD) is less described. Levels of four CAMs (E-selectin, P-selectin glycoprotein ligand-1, intercellular adhesion molecule-1, and vascular cell adhesion molecule-1 (VCAM-1)) and six other known biomarkers (C-reactive protein (CRP), interleukin-6 (IL-6), N-terminal pro-brain natriuretic peptide (NT-proBNP), troponin I, vasopressin-neurophysin 2-copeptin, and S100 calcium-binding protein B) were measured in a population of patients presenting CVD. Blood collections for analysis were performed within different time windows after stroke onset: 0–6 h, 6–36 h, 2–3 days, 5–7 days, and 2–3 weeks. Independent associations with poor outcome at 3 months (modified Rankin Scale score > 2) were sought using univariate and multivariate analysis after adjustments for age and National Institute of Health Stroke Scale score. Predictive ability of each biomarker has also been assessed with ROC analysis. One hundred patients were prospectively included whom 75 presented with ischemic strokes, nine with hemorrhagic strokes and 16 with transient ischemic attacks. During the first 6 h after stroke onset, E-selectin was found to be an independent predictor of 3-month outcome (odds ratio (OR) =24; 95 % confidence interval (95 % CI), 2–354; p = 0.022) (area under the curve (AUC) =78 %), as was VCAM-1 during the third week after onset (OR = 8; 95 % CI, 2–37; p = 0.01) (AUC = 73 %). Associations remained after the exclusion of patients with hemorrhagic strokes and transient ischemic attacks. Independent associations with outcome were also found for CRP (OR = 5; 95 % CI, 1–22; p = 0.023) and IL-6 (OR = 5; 95 % CI, 1–17; p = 0.021) at 2–3 days and for NT-proBNP at 6–36 h (OR = 20; 95 % CI, 1–337; p = 0.04). E-selectin and VCAM-1 were independent predictors of outcome in a population of patients with CVD. The predictive capability of other biomarkers known to be indicators for prognosis also emerged, confirming the study’s robustness. CAMs levels could be considered as objective biological criteria for prognosis in CVD.",{"EN":1555},"E-selectin and vascular cell adhesion molecule-1 as biomarkers of 3-month outcome in cerebrovascular diseases",{"VOID":1557},"10.1186\u002Fs12950-015-0106-z","http:\u002F\u002Fwww.journal-inflammation.com\u002Fcontent\u002F12\u002F1\u002F61",[1560,1575,1590,1602,1614,1633],{"id":1561,"sortIndex":312,"researcher":18,"roles":1562,"affiliations":1563,"properties":1572},"412d54df-0745-44b4-a92e-f13d2988bab3",[198],[1564],{"id":18,"sortIndex":19,"affiliation":1565,"properties":18},{"id":1566,"createTime":1567,"updateTime":1567,"relativeEntities":1568,"slug":18,"properties":1569,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"8a02c3a2-54fa-477b-9370-218e541fdcf3","2023-12-18T05:22:43.804+00:00",[],{"title":1570},{"VI":1571},"Department of Human Protein Sciences, University Medical Center, Geneva, Switzerland",{"title":1573},{"VI":1574},"Natacha Turck",{"id":1576,"sortIndex":236,"researcher":18,"roles":1577,"affiliations":1578,"properties":1587},"f6a0ec26-0ff8-4350-b608-c55249a38c08",[198],[1579],{"id":18,"sortIndex":19,"affiliation":1580,"properties":18},{"id":1581,"createTime":1582,"updateTime":1582,"relativeEntities":1583,"slug":18,"properties":1584,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"77bcb78e-d6a1-4fc8-9af9-c7ddd5f3cef7","2023-12-18T05:22:43.833+00:00",[],{"title":1585},{"VI":1586},"Department of Neurology, Stroke Unit, Nancy University Hospital Center, Nancy, France",{"title":1588},{"VI":1589},"Marc Debouverie",{"id":1591,"sortIndex":132,"researcher":18,"roles":1592,"affiliations":1593,"properties":1599},"bd2a0ac1-0679-41c0-9d99-f871c9a01e96",[198],[1594],{"id":18,"sortIndex":19,"affiliation":1595,"properties":18},{"id":1566,"createTime":1567,"updateTime":1567,"relativeEntities":1596,"slug":18,"properties":1597,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1598},{"VI":1571},{"title":1600},{"VI":1601},"Jean-Charles Sanchez",{"id":1603,"sortIndex":202,"researcher":18,"roles":1604,"affiliations":1605,"properties":1611},"500004c9-8277-4b12-aeee-ec698346f700",[198],[1606],{"id":18,"sortIndex":19,"affiliation":1607,"properties":18},{"id":1566,"createTime":1567,"updateTime":1567,"relativeEntities":1608,"slug":18,"properties":1609,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1610},{"VI":1571},{"title":1612},{"VI":1613},"Linnéa Lagerstedt",{"id":1615,"sortIndex":19,"researcher":18,"roles":1616,"affiliations":1617,"properties":1630},"b250f0bf-b69b-4980-9236-6e6906c0915e",[198],[1618,1623],{"id":18,"sortIndex":19,"affiliation":1619,"properties":18},{"id":1581,"createTime":1582,"updateTime":1582,"relativeEntities":1620,"slug":18,"properties":1621,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1622},{"VI":1586},{"id":1624,"sortIndex":202,"affiliation":1625,"properties":1629},"433a70f7-725b-4e8d-9c34-c48d1ec8e5c8",{"id":1566,"createTime":1567,"updateTime":1567,"relativeEntities":1626,"slug":18,"properties":1627,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1628},{"VI":1571},{},{"title":1631},{"VI":1632},"Sébastien Richard",{"id":1634,"sortIndex":116,"researcher":18,"roles":1635,"affiliations":1636,"properties":1645},"ec5b3929-e581-482b-81d3-5ab31d9e4c49",[198],[1637],{"id":18,"sortIndex":19,"affiliation":1638,"properties":18},{"id":1639,"createTime":1640,"updateTime":1640,"relativeEntities":1641,"slug":18,"properties":1642,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"4be8eeaa-6c3d-4b6d-a6a9-0333f33c8a15","2023-12-27T14:52:57.674+00:00",[],{"title":1643},{"VI":1644},"Department of Neurology, Geneva University Hospitals and Faculty of Medicine, University of Geneva, Geneva, Switzerland",{"title":1646},{"VI":1647},"Pierre R. Burkhard",{"url":1558,"publisher":1649,"properties":1676},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1650,"slug":10,"properties":1651,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1654,"manageAffiliations":1655,"indexDatabases":1656,"url":18,"thumbnailPath":18,"statistic":1671,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"eissn":1652,"title":1653},{"VOID":13},{"EN":15},[],[],[1657,1664],{"id":62,"indexDatabase":1658,"url":75,"indexYears":76,"academicFieldIds":1663,"indexDatabaseRanking":80},{"id":64,"createTime":65,"updateTime":66,"relativeEntities":1659,"label":1660,"description":1661,"key":72,"publicationTags":1662,"standard":18},[],{"EN":69,"VI":69},{"EN":69,"VI":71},[74],[78,79],{"id":82,"indexDatabase":1665,"url":97,"indexYears":18,"academicFieldIds":1670,"indexDatabaseRanking":18},{"id":84,"createTime":85,"updateTime":86,"relativeEntities":1666,"label":1667,"description":1668,"key":93,"publicationTags":1669,"standard":18},[],{"EN":89,"VI":89},{"VI":91,"EN":92},[95,96],[99],{"impactFactor":19,"impactFactorByYear":1672,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":1673,"totalCitation":133,"totalCitationByYear":1674,"totalCitationPerPublication":150,"totalCitationPerPublicationByYear":1675,"hindexLast5Year":170,"hindex":170},{"2012":102,"2013":103,"2014":104,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":110,"2022":111,"2023":104},{"2004":116,"2005":117,"2006":58,"2007":118,"2008":119,"2009":120,"2010":121,"2011":122,"2012":123,"2013":124,"2014":125,"2015":126,"2016":127,"2017":128,"2018":129,"2019":128,"2020":122,"2021":128,"2022":130,"2023":131,"2024":132},{"2005":135,"2006":136,"2007":137,"2008":138,"2009":139,"2010":140,"2011":141,"2012":142,"2013":143,"2014":144,"2015":145,"2016":146,"2017":138,"2018":147,"2019":148,"2020":149,"2021":125,"2022":58},{"2005":152,"2006":153,"2007":154,"2008":155,"2009":156,"2010":157,"2011":158,"2012":159,"2013":160,"2014":161,"2015":162,"2016":163,"2017":164,"2018":165,"2019":166,"2020":167,"2021":168,"2022":169},{"volume":1677,"pages":1678},{"VOID":380},{"VOID":382},"2015-11-04",{"id":1681,"createTime":1682,"updateTime":1683,"relativeEntities":1684,"slug":1685,"properties":1686,"entityType":190,"verifyStatus":191,"verifyTime":1695,"verifyNote":192,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1696,"fullTextUrl":18,"authors":1697,"publicationType":349,"publisherRelationship":1729,"citationCount":19,"citationInfo":1762,"publishDate":1764,"publishYear":1765,"citationAnalyzeStatus":17,"lastCitationAnalyze":1766,"indexDatabases":18,"openAccess":18,"references":1767,"isForceReanalyzing":385},"97cf8fc0-ea7a-453d-805c-754c8b149a5f","2024-02-07T00:44:58.230+00:00","2026-05-05T23:38:10.993+00:00",[],"Riboflavin-along-with-antibiotics-balances-reactive-oxygen-species-and-inflammatory-cytokines-and-controls-Staphylococcus-aureus-infection-by-boosting-murine-macrophage-function-and-regulates-inflammation",{"abstract":1687,"title":1689,"doi":1691,"gsPaper":1693},{"EN":1688},"Macrophages serve as intracellular reservoirs of S. aureus. Recent in vitro studies have confirmed high level resistance by S. aureus to macrophage mediated killing and the intracellular persistence of Staphylococci may play an important role in the pathogenesis. Since this localization protects them from both cell-mediated and humoral immune responses, therefore, a successful anti-staphylococcal therapy should include the elimination of intracellular bacteria, further protecting the host cells from staphylococci-induced cell death. So, only antibiotic therapy may not be helpful, successful therapy needs combination of drugs not only for elimination of pathogen but also for rescuing the host cell for S. aureus induced cell death. In keeping with this idea an in vitro study has been done to examine the effect of Riboflavin along with antibiotics on phagocytosis, hydorgen peroxide, superoxide production, antioxidant enzyme levels, and cytokine levels in mouse macrophages for amelioration of the Staphylococcus aureus burden. The immune boosting effects of Riboflavin have been validated through perturbations of redox homeostasis and pro-inflammatory cytokines measurements. It was observed that the supplementation of Vitamin B-2 (Riboflavin) not only enhances macrophage function as previously reported but also decreases pro-inflammatory responses in Staphylococcus aureus infected macrophages. The observed influence of Riboflavin on enhanced antimicrobial effects such as enhanced phagocytosis of macrophages exposed to S. aureus, hydrogen peroxide or superoxide production when combined with either ciprofloxacin (CIP) or Azithromycin (AZM) and decrease in pro-inflammatory responses of IFN-γ, IL-6, IL-1β. Riboflavin treatment also decreased NO and TNF-α level possibly by inhibiting the NF-κβ pathway. The increased antioxidant enzymes like glutathione reductase, SOD and GSH level helped in maintaining a stable redox state in the cell. Riboflavin plus antibiotic pretreatment not only enhances macrophage functions but also decreases proinflammatory responses in Staphylococcus aureus infected macrophages indicating better bacterial clearance and regulated inflammation which may be considered as a novel and important therapeutic intervention.",{"EN":1690},"Riboflavin along with antibiotics balances reactive oxygen species and inflammatory cytokines and controls Staphylococcus aureus infection by boosting murine macrophage function and regulates inflammation",{"VOID":1692},"10.1186\u002Fs12950-016-0145-0",{"VOID":1694},"[\"13404234301555912\"]","2024-05-06T18:08:18.235+00:00","https:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12950-016-0145-0",[1698,1715],{"id":1699,"sortIndex":19,"researcher":18,"roles":1700,"affiliations":1701,"properties":1710},"f5b98af9-c0c3-488a-aee4-53856b8e8d85",[198],[1702],{"id":18,"sortIndex":19,"affiliation":1703,"properties":18},{"id":1704,"createTime":1705,"updateTime":1705,"relativeEntities":1706,"slug":18,"properties":1707,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"bf50ba98-8b00-4068-96f2-eea1f3f6d896","2024-01-01T12:08:21.636+00:00",[],{"title":1708},{"VI":1709},"Department of Physiology, Immunology Laboratory, University of Calcutta, University Colleges of Science and Technology, Calcutta, India",{"title":1711,"gsAuthor":1713},{"VI":1712},"Somrita Dey",{"VOID":1714},"[\"LxF32T8AAAAJ\"]",{"id":1716,"sortIndex":202,"researcher":18,"roles":1717,"affiliations":1718,"properties":1724},"0bd4ebf9-7fe2-4945-9253-e071ef7faeca",[198],[1719],{"id":18,"sortIndex":19,"affiliation":1720,"properties":18},{"id":1704,"createTime":1705,"updateTime":1705,"relativeEntities":1721,"slug":18,"properties":1722,"entityType":47,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1723},{"VI":1709},{"title":1725,"gsAuthor":1727},{"VI":1726},"Biswadev Bishayi",{"VOID":1728},"[\"TDdGMcMAAAAJ\"]",{"url":1696,"publisher":1730,"properties":1757},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1731,"slug":10,"properties":1732,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1735,"manageAffiliations":1736,"indexDatabases":1737,"url":18,"thumbnailPath":18,"statistic":1752,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"eissn":1733,"title":1734},{"VOID":13},{"EN":15},[],[],[1738,1745],{"id":62,"indexDatabase":1739,"url":75,"indexYears":76,"academicFieldIds":1744,"indexDatabaseRanking":80},{"id":64,"createTime":65,"updateTime":66,"relativeEntities":1740,"label":1741,"description":1742,"key":72,"publicationTags":1743,"standard":18},[],{"EN":69,"VI":69},{"EN":69,"VI":71},[74],[78,79],{"id":82,"indexDatabase":1746,"url":97,"indexYears":18,"academicFieldIds":1751,"indexDatabaseRanking":18},{"id":84,"createTime":85,"updateTime":86,"relativeEntities":1747,"label":1748,"description":1749,"key":93,"publicationTags":1750,"standard":18},[],{"EN":89,"VI":89},{"VI":91,"EN":92},[95,96],[99],{"impactFactor":19,"impactFactorByYear":1753,"i10Index":112,"i10IndexLast5Year":113,"totalPublication":114,"totalPublicationByYear":1754,"totalCitation":133,"totalCitationByYear":1755,"totalCitationPerPublication":150,"totalCitationPerPublicationByYear":1756,"hindexLast5Year":170,"hindex":170},{"2012":102,"2013":103,"2014":104,"2015":104,"2016":105,"2017":106,"2018":107,"2019":108,"2020":109,"2021":110,"2022":111,"2023":104},{"2004":116,"2005":117,"2006":58,"2007":118,"2008":119,"2009":120,"2010":121,"2011":122,"2012":123,"2013":124,"2014":125,"2015":126,"2016":127,"2017":128,"2018":129,"2019":128,"2020":122,"2021":128,"2022":130,"2023":131,"2024":132},{"2005":135,"2006":136,"2007":137,"2008":138,"2009":139,"2010":140,"2011":141,"2012":142,"2013":143,"2014":144,"2015":145,"2016":146,"2017":138,"2018":147,"2019":148,"2020":149,"2021":125,"2022":58},{"2005":152,"2006":153,"2007":154,"2008":155,"2009":156,"2010":157,"2011":158,"2012":159,"2013":160,"2014":161,"2015":162,"2016":163,"2017":164,"2018":165,"2019":166,"2020":167,"2021":168,"2022":169},{"volume":1758,"pages":1760},{"VOID":1759},"13",{"VOID":1761},"1-21",{"total":19,"publishYear":19,"statisticByYear":1763},{},"2016-11-28",2016,"2026-05-05T23:38:10.992+00:00",[1768,1771,1777,1780,1783,1786,1789,1792,1795,1798,1804,1807,1810,1813,1816,1819,1822,1825,1828,1834,1837,1840,1846,1849,1852,1855,1858,1861,1864,1867,1870,1873,1876,1879,1882,1885,1888,1891,1894,1899,1902,1905,1908,1917,1920,1923,1929,1932,1935,1938,1944,1947,1950,1953,1956,1959,1962,1965,1968,1974,1977,1980,1983,1989,1995,1998,2001,2004],{"id":18,"text":1769,"url":18,"identifiers":1770},"Archer GL. Staphylococcus aureus: A well-armed pathogen. Clin Infect Dis. 1998;26:1179–81.",{},{"id":1772,"text":1773,"url":1774,"identifiers":1775},"4c68646b-0035-4279-8000-0006b275d4fa","Staali L, Bauer S, Morgelin M, et al. Streptococcus pyogenesbacteria modulate membrane traffic in human neutrophils and selectively inhibit azurophilic granule fusion with phagosomes. Cell Microbiol. 2006;8:690–703.","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":1776},"10.1007\u002Fs10440-022-00541-7",{"id":1772,"text":1778,"url":1774,"identifiers":1779},"Voyich JM, Braughton KR, Sturdevant DE, Whitney AR, Said-Salim B, Porcella SF, Long RD, Dorward DW, Gardner DJ, Kreiswirth BN, Musser JM, DeLeo FR. Insights into mechanisms used by Staphylococcus aureus to avoid destruction by human neutrophils. J Immunol. 2005;175:3907–19.",{"doi":1776},{"id":1772,"text":1781,"url":1774,"identifiers":1782},"Flannagan RS, Cosío G, Grinstein S. Antimicrobial mechanisms of phagocytes and bacterial evasion strategies. Nat Rev Microbiol. 2009;7:355–66.",{"doi":1776},{"id":1772,"text":1784,"url":1774,"identifiers":1785},"Sorci G, Faivre B. Inflammation and oxidative stress in vertebrate host-parasite systems. Philos Trans R SocLond B Biol Sci. 2009;364:71–83.",{"doi":1776},{"id":1772,"text":1787,"url":1774,"identifiers":1788},"Petti CA, Fowler Jr VG. Staphylococcus aureus bacteremia and endocarditis. Cardiol Clin. 2003;21:219–33.",{"doi":1776},{"id":1772,"text":1790,"url":1774,"identifiers":1791},"Powers HJ. Riboflavin (vitamin B-2) and health. Am J Clin Nutr. 2003;77:1352–60.",{"doi":1776},{"id":1772,"text":1793,"url":1774,"identifiers":1794},"Mazur-Bialy AI, Majka A, Wojtas L, Kolaczkowska E, Plytycz B. Strain specific effects of Riboflavin supplementation on zymosaninducedperitonitis in C57BL\u002F6J, BALB\u002Fc and CBA mice. Life Sci. 2011;88:265–71.",{"doi":1776},{"id":1772,"text":1796,"url":1774,"identifiers":1797},"Nathan C, Cunningham-Bussel A. Beyond oxidative stress: an immunologist’s guide to reactive oxygen species. Nature Rev Immunol. 2013;13:349–61.",{"doi":1776},{"id":1799,"text":1800,"url":1801,"identifiers":1802},"eeca947b-7e12-49ca-abe4-932f1ea7ffea","Qureshi AA, Tan X, Reis JC, Badr MZ, Papasian CJ, Morrison DC, Qureshi N. Suppression of nitric oxide induction and pro-inflammatory cytokines by novel proteasome inhibitors in various experimental models. Lipids Health Dis. 2011;10:177.","https:\u002F\u002Flipidworld.biomedcentral.com\u002Farticles\u002F10.1186\u002F1476-511X-10-177",{"doi":1803},"10.1186\u002F1476-511X-10-177",{"id":1772,"text":1805,"url":1774,"identifiers":1806},"Toyosawa T, Suzuki M, Kodama K, Araki S. Effects of intravenous infusion of highly purified vitamin B2 on lipopolysaccharide-induced shock and bacterial infection in mice. Eur J Pharmacol. 2004;492:273–80.",{"doi":1776},{"id":1772,"text":1808,"url":1774,"identifiers":1809},"Araki S, Suzuki M, Fujimoto M, Kimura K. Enhancement of resistance to bacterial infection in mice by vitamin B2. J Vet Med Sci. 1995;57:599–602.",{"doi":1776},{"id":1772,"text":1811,"url":1774,"identifiers":1812},"Mal P, Ghosh D, Bandyopadhyay D, Dutta K, Bishayi B. Ampicillin alone and in combination with Riboflavin modulates Staphylococcus aureus infection induced septic arthritis in mice. Indian J Exp Biol. 2012;50:677–89.",{"doi":1776},{"id":1772,"text":1814,"url":1774,"identifiers":1815},"Yazdanpanah B, Wiegmann K, Tchikov V, Krut O, Pongratz C, Schramm M, Kleinridders A, Wunderlich T, Kashkar H, Utermöhlen O, Brüning JC, Schütze S, Krönke M. Riboflavin kinase couples TNF receptor 1 to NADPH oxidase. Nature. 2009;460:1159–63.",{"doi":1776},{"id":1772,"text":1817,"url":1774,"identifiers":1818},"Dröge W. Free radicals in the physiological control of cell functions. Physiol Rev. 2002;82:47–96.",{"doi":1776},{"id":1772,"text":1820,"url":1774,"identifiers":1821},"Haddad JJ. Glutathione depletion is associated with augmenting a proinflammatory signal: evidence for an antioxidant\u002Fpro-oxidant mechanism regulating cytokines in the alveolar epithelium. Cytokines Cell Mol Ther. 2000;6:177–87.",{"doi":1776},{"id":1772,"text":1823,"url":1774,"identifiers":1824},"Páez PL, Becerra MC, Albesa I. Chloramphenicol-induced oxidative stress in human neutrophils. Basic Clin Pharmacol Toxicol. 2008;103:349–53.",{"doi":1776},{"id":1772,"text":1826,"url":1774,"identifiers":1827},"Carryn S, Chanteux H, Seral C, Mingeot-Leclercq MP, Van Bambeke F, Tulkens PM. Intracellular pharmacodynamics of antibiotics. Infect Dis Clin North Am. 2003;17:615–34.",{"doi":1776},{"id":1829,"text":1830,"url":1831,"identifiers":1832},"db96324f-1953-4392-a558-3a6d274d6c50","Majhi A, Kundu K, Adhikary R, Banerjee M, Mahanti S, Basu A, Bishayi B. Combination therapy with ampicillin and azithromycin down regulates Streptococcus pneumoniae induced inflammation in mice. J Inflamm. 2011;11:5. doi:10.1186\u002F1476-9255-11-5.","https:\u002F\u002Fjournal-inflammation.biomedcentral.com\u002Farticles\u002F10.1186\u002F1476-9255-11-5",{"doi":1833},"10.1186\u002F1476-9255-11-5",{"id":1772,"text":1835,"url":1774,"identifiers":1836},"Dey S, Majhi A, Mahanti S, Dey I, Bishayi B. In vitro anti-inflammatory and immunomodulatory effects of ciprofloxacin or azithromycin in Staphylococcus aureus-stimulated murine macrophages are beneficial in the presence of cytochalasin D. Inflammation. 2015;38(3):1050–69.",{"doi":1776},{"id":1772,"text":1838,"url":1774,"identifiers":1839},"Cigana C, Assael BM, Melotti P. Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells. Antimicrob Agents Chemother. 2007;51:975–81.",{"doi":1776},{"id":1841,"text":1842,"url":1843,"identifiers":1844},"22f13565-a605-4036-904b-f27e6f093f5a","Culic O, Erakovic I, Cepelak K, Barisic K, Brajsa K, Ferencic Z, Galović R, Glojnarić I, Manojlović Z, Munić V, Novak-Mircetić R, Pavicić-Beljak V, Sucić M, Veljaca M, Zanić-Grubisić T, Parnham MJ. Azithromycin modulates neutrophil function and circulating inflammatory mediators in healthy human subjects. Eur J Pharmacol. 2002;450:277–89.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0014299902020423",{"doi":1845},"10.1016\u002Fs0014-2999(02)02042-3",{"id":1772,"text":1847,"url":1774,"identifiers":1848},"Aghai ZH, Kode A, Saslow JG, Nakhla T, Farhath S, Stahl GE, Eydelman R, Strande L, Leone P, Rahman I. Azithromycin suppresses activation of nuclear factor kappa B and synthesis of pro-inflammatory cytokines in tracheal aspirate cells from premature infants. Pediatr Res. 2007;62:483–8.",{"doi":1776},{"id":18,"text":1850,"url":18,"identifiers":1851},"Mal P, Dutta S, Bandyopadhyay D, Dutta K, Basu A, Bishayi B. Gentamicin in combination with ascorbic acid regulates the severity of Staphylococcus aureus infection-induced septic arthritis in mice. Scand J Immunol. 2012;76:528–40.",{},{"id":1772,"text":1853,"url":1774,"identifiers":1854},"Bishayi B, Bandyopadhyay D, Majhi A, Adhikary R. Possible role of Toll-like receptor-2 in the intracellular survival of Staphylococcus aureus in murine peritoneal macrophages: involvement of cytokines and anti-oxidant enzymes. Scand J Immunol. 2014;80:127–43.",{"doi":1776},{"id":1772,"text":1856,"url":1774,"identifiers":1857},"Krut O, Utermöhlen O, Schlossherr X, Krönke M. Strain-specific association of cytotoxic activity and virulence of clinical Staphylococcus aureus isolates. 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