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Here, we studied the infection of human blood monocytes with the intracellular pathogen C. pneumoniae and the effect on cytokine and chemokine profiles in comparison to stimulation with LPS. Monocytes purified from peripheral blood mononuclear cells by negative depletion were infected with C. pneumoniae. While immunofluorescence confirmed the presence of chlamydial lipopolysaccharide (LPS) in the cytoplasm of infected monocytes, real-time PCR did not provide evidence for replication of the intracellular pathogen. Complementary to PCR, C. pneumoniae infection was confirmed by an oligonucleotide DNA microarray for the detection of intracellular pathogens. Raman microspectroscopy revealed different molecular fingerprints for infected and non-infected monocytes, which were mainly due to changes in lipid and fatty acid content. Stimulation of monocytes with C. pneumoniae or with LPS induced similar profiles of tumor necrosis factor-alpha (TNF-α) and interleukin (IL)-6, but higher levels of IL-1β, IL-12p40 and IL-12p70 for C. pneumoniae which were statistically significant. C. pneumoniae also induced release of the chemokines MCP-1, MIP-1α and MIP-1β, and CXCL-8, which correlated with TNF-α secretion. Infection of human blood monocytes with intracellular pathogens triggers altered cytokine and chemokine pattern as compared to stimulation with extracellular ligands such as LPS. Complementing conventional methods, an oligonucleotide DNA microarray for the detection of intracellular pathogens as well as Raman microspectroscopy provide useful tools to trace monocyte infection.",{"EN":172},"Human blood monocytes support persistence, but not replication of the intracellular pathogen C. pneumoniae",{"VOID":174},"[\"1944391662261674958\"]",{"VOID":176},"Finlay BB, McFadden G: Anti-immunology: evasion of the host immune system by bacterial and viral pathogens. Cell. 2006, 124 (4): 767-782. 10.1016\u002Fj.cell.2006.01.034.\nKhan N, Gowthaman U, Pahari S, Agrewala JN: Manipulation of costimulatory molecules by intracellular pathogens: veni, vidi, vici!!. PLoS Pathog. 2012, 8 (6): e1002676-10.1371\u002Fjournal.ppat.1002676.\nKern JM, Maass V, Maass M: Molecular pathogenesis of chronic Chlamydia pneumoniae infection: a brief overview. Clin Microbiol Infect. 2009, 15 (1): 36-41. 10.1111\u002Fj.1469-0691.2008.02631.x.\nSaikku P: Seroepidemiology in Chlamydia pneumoniae– atherosclerosis association. Eur Heart J. 2002, 23 (4): 263-264. 10.1053\u002Feuhj.2001.2913.\nVon HL: Role of persistent infection in the control and severity of asthma: focus on Chlamydia pneumoniae. Eur Respir J. 2002, 19 (3): 546-556. 10.1183\u002F09031936.02.00254402.\nContini C, Grilli A, Badia L, Guardigni V, Govoni M, Seraceni S: Detection of Chlamydophila pneumoniae in patients with arthritis: significance and diagnostic value. Rheumatol Int. 2011, 31 (10): 1307-1313. 10.1007\u002Fs00296-010-1460-z.\nTang YW, Sriram S, Li H, Yao SY, Meng S, Mitchell WM, Stratton CW: Qualitative and quantitative detection of Chlamydophila pneumoniae DNA in cerebrospinal fluid from multiple sclerosis patients and controls. PloS one. 2009, 4 (4): e5200-10.1371\u002Fjournal.pone.0005200.\nBalin BJ, Little CS, Hammond CJ, Appelt DM, Whittum-Hudson JA, Gerard HC, Hudson AP: Chlamydophila pneumoniae and the etiology of late-onset Alzheimer's disease. J Alzheimers Dis. 2008, 13 (4): 371-380.\nDi Pietro M, Schiavoni G, Sessa V, Pallotta F, Costanzo G, Sessa R: Chlamydia pneumoniae and osteoporosis-associated bone loss: a new risk factor?. Osteoporos Int. 2013, 24 (5): 1677-1682. 10.1007\u002Fs00198-012-2217-1.\nRizzo A, Di Domenico M, Carratelli CR, Mazzola N, Paolillo R: Induction of proinflammatory cytokines in human osteoblastic cells by Chlamydia pneumoniae. Cytokine. 2011, 56 (2): 450-457. 10.1016\u002Fj.cyto.2011.06.027.\nWyrick PB: Chlamydia trachomatis persistence in vitro: an overview. J Infect Dis. 2010, 201 (Suppl 2): S88-95. 10.1086\u002F652394.\nSchachter J: Biology of Chlamydia trachomatis. Sexually Transmitted Diseases. Edited by: Holmes KK SP, Mård PA, Lemon SM, Stamm WE, Piot P, Wasserheit JN. 1999, McGraw-Hill, New York, 391-405.\nGaydos CA, Summersgill JT, Sahney NN, Ramirez JA, Quinn TC: Replication of Chlamydia pneumoniae in vitro in human macrophages, endothelial cells, and aortic artery smooth muscle cells. Infect Immun. 1996, 64 (5): 1614-1620.\nByrne GI, Kalayoglu MV: Chlamydia pneumoniae and atherosclerosis: links to the disease process. Am Heart J. 1999, 138 (5 Pt 2): S488-490. 10.1016\u002FS0002-8703(99)70282-6.\nLin TM, Campbell LA, Rosenfeld ME, Kuo CC: Monocyte-endothelial cell coculture enhances infection of endothelial cells with Chlamydia pneumoniae. J Infect Dis. 2000, 181 (3): 1096-1100. 10.1086\u002F315349.\nQuinn TC, Gaydos CA: In vitro infection and pathogenesis of Chlamydia pneumoniae in endovascular cells. Am Heart J. 1999, 138 (5 Pt 2): S507-511. 10.1016\u002FS0002-8703(99)70287-5.\nRupp J, Koch M, van Zandbergen G, Solbach W, Brandt E, Maass M: Transmission of Chlamydia pneumoniae infection from blood monocytes to vascular cells in a novel transendothelial migration model. FEMS Microbiol Lett. 2005, 242 (2): 203-208. 10.1016\u002Fj.femsle.2004.11.010.\nMoazed TC, Kuo CC, Grayston JT, Campbell LA: Evidence of systemic dissemination of Chlamydia pneumoniae via macrophages in the mouse. J Infect Dis. 1998, 177 (5): 1322-1325. 10.1086\u002F515280.\nContini C, Seraceni S, Cultrera R, Castellazzi M, Granieri E, Fainardi E: Chlamydophila pneumoniae Infection and Its Role in Neurological Disorders. Interdiscip Perspect Infect Dis. 2010, 2010: 273573-\nDi Pietro M, Filardo S, Cazzavillan S, Segala C, Bevilacqua P, Bonoldi E, D'Amore ES, Rassu M, Sessa R: Could past Chlamydial vascular infection promote the dissemination of Chlamydia pneumoniae to the brain?. J Biol Regul Homeost Agents. 2013, 27 (1): 155-164.\nPeters RP, van Agtmael MA, Danner SA, Savelkoul PH, Vandenbroucke-Grauls CM: New developments in the diagnosis of bloodstream infections. The Lancet infectious diseases. 2004, 4 (12): 751-760. 10.1016\u002FS1473-3099(04)01205-8.\nMaass M, Harig U: Evaluation of culture conditions used for isolation of Chlamydia pneumoniae. Am J Clin Pathol. 1995, 103 (2): 141-148.\nWiesinger-Mayr H, Vierlinger K, Pichler R, Kriegner A, Hirschl AM, Presterl E, Bodrossy L, Noehammer C: Identification of human pathogens isolated from blood using microarray hybridisation and signal pattern recognition. BMC microbiology. 2007, 7: 78-10.1186\u002F1471-2180-7-78.\nMovasaghi Z, Rehman S, Rehman IS: Raman spectroscopy of biological tissues. Appl Spectrosc Rev. 2007, 42 (5): 493-541. 10.1080\u002F05704920701551530.\nRupp J, Pfleiderer L, Jugert C, Moeller S, Klinger M, Dalhoff K, Solbach W, Stenger S, Laskay T, van Zandbergen G: Chlamydia pneumoniae hides inside apoptotic neutrophils to silently infect and propagate in macrophages. PloS one. 2009, 4 (6): e6020-10.1371\u002Fjournal.pone.0006020.\nWolf K, Fischer E, Hackstadt T: Degradation of Chlamydia pneumoniae by peripheral blood monocytic cells. Infect Immun. 2005, 73 (8): 4560-4570. 10.1128\u002FIAI.73.8.4560-4570.2005.\nAirenne S, Surcel HM, Alakarppa H, Laitinen K, Paavonen J, Saikku P, Laurila A: Chlamydia pneumoniae infection in human monocytes. Infect Immun. 1999, 67 (3): 1445-1449.\nMarangoni A, Bergamini C, Fato R, Cavallini C, Donati M, Nardini P, Foschi C, Cevenini R: Infection of human monocytes by Chlamydia pneumoniae and Chlamydia trachomatis: an in vitro comparative study. BMC research notes. 2014, 7: 230-10.1186\u002F1756-0500-7-230.\nSzaszak M, Chang JC, Leng W, Rupp J, Ojcius DM, Kelley AM: Characterizing the intracellular distribution of metabolites in intact Chlamydia-infected cells by Raman and two-photon microscopy. Microbes and infection\u002FInstitut Pasteur. 2013, 15 (6–7): 461-469. 10.1016\u002Fj.micinf.2013.03.005.\nHeinemann M, Susa M, Simnacher U, Marre R, Essig A: Growth of Chlamydia pneumoniae induces cytokine production and expression of CD14 in a human monocytic cell line. Infect Immun. 1996, 64 (11): 4872-4875.\nMamata Y, Hakki A, Newton C, Burdash N, Klein TW, Friedman H: Differential effects of Chlamydia pneumoniae infection on cytokine levels in human T lymphocyte- and monocyte-derived cell cultures. Int J Med Microbiol. 2007, 297 (2): 109-115. 10.1016\u002Fj.ijmm.2006.11.004.\nAbdul-Sater AA, Said-Sadier N, Padilla EV, Ojcius DM: Chlamydial infection of monocytes stimulates IL-1beta secretion through activation of the NLRP3 inflammasome. Microbes and infection\u002FInstitut Pasteur. 2010, 12 (8–9): 652-661. 10.1016\u002Fj.micinf.2010.04.008.\nEitel J, Meixenberger K, van Laak C, Orlovski C, Hocke A, Schmeck B, Hippenstiel S, N'Guessan PD, Suttorp N, Opitz B: Rac1 regulates the NLRP3 inflammasome which mediates IL-1beta production in Chlamydophila pneumoniae infected human mononuclear cells. PloS one. 2012, 7 (1): e30379-10.1371\u002Fjournal.pone.0030379.\nNetea MG, Nold-Petry CA, Nold MF, Joosten LA, Opitz B, van der Meer JH, van de Veerdonk FL, Ferwerda G, Heinhuis B, Devesa I: Differential requirement for the activation of the inflammasome for processing and release of IL-1beta in monocytes and macrophages. Blood. 2009, 113 (10): 2324-2335. 10.1182\u002Fblood-2008-03-146720.\nTrinchieri G: Interleukin-12 and the regulation of innate resistance and adaptive immunity. Nat Rev Immunol. 2003, 3 (2): 133-146. 10.1038\u002Fnri1001.\nNetea MG, Selzman CH, Kullberg BJ, Galama JM, Weinberg A, Stalenhoef AF, Van der Meer JW, Dinarello CA: Acellular components of Chlamydia pneumoniae stimulate cytokine production in human blood mononuclear cells. Eur J Immunol. 2000, 30 (2): 541-549. 10.1002\u002F1521-4141(200002)30:2\u003C541::AID-IMMU541>3.0.CO;2-X.\nRoblin PM, Dumornay W, Hammerschlag MR: Use of HEp-2 cells for improved isolation and passage of Chlamydia pneumoniae. J Clin Microbiol. 1992, 30 (8): 1968-1971.\nCampbell LA, Kuo CC: Cultivation and laboratory maintenance of Chlamydia pneumoniae. Curr Protoc Microbiol. 2009, 11 (11B): 11-\nWolf HM, Fischer MB, Puhringer H, Samstag A, Vogel E, Eibl MM: Human serum IgA downregulates the release of inflammatory cytokines (tumor necrosis factor-alpha, interleukin-6) in human monocytes. Blood. 1994, 83 (5): 1278-1288.\nDatta B, Njau F, Thalmann J, Haller H, Wagner AD: Differential infection outcome of Chlamydia trachomatis in human blood monocytes and monocyte-derived dendritic cells. BMC microbiology. 2014, 14: 209-10.1186\u002Fs12866-014-0209-3.\nSommer K, Njau F, Wittkop U, Thalmann J, Bartling G, Wagner A, Klos A: Identification of high- and low-virulent strains of Chlamydia pneumoniae by their characterization in a mouse pneumonia model. FEMS immunology and medical microbiology. 2009, 55 (2): 206-214. 10.1111\u002Fj.1574-695X.2008.00503.x.\nGoldschmidt P, Rostane H, Sow M, Goepogui A, Batellier L, Chaumeil C: Detection by broad-range real-time PCR assay of Chlamydia species infecting human and animals. Br J Ophthalmol. 2006, 90 (11): 1425-1429. 10.1136\u002Fbjo.2006.096420.\nLudwig W, Strunk O, Westram R, Richter L, Meier H, Yadhukumar , Buchner A, Lai T, Steppi S, Jobb G: ARB: a software environment for sequence data. Nucleic acids research. 2004, 32 (4): 1363-1371. 10.1093\u002Fnar\u002Fgkh293.",{"VOID":178},"10.1186\u002Fs12865-014-0060-1","PUBLICATION","VERIFIED","2024-09-13T08:37:46.269+00:00","Auto Verify","https:\u002F\u002Fbmcimmunol.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12865-014-0060-1",[185,201,217,231,247,263,286],{"id":186,"sortIndex":21,"researcher":20,"roles":187,"affiliations":189,"properties":198},"e5e60b54-98f4-4bbc-9c46-06cd84d3851a",[188],"AUTHOR",[190],{"id":191,"sortIndex":21,"affiliation":192,"properties":20},"26e92ee0-53bd-4fed-af3e-48c5b2801d18",{"id":191,"createTime":20,"updateTime":20,"relativeEntities":193,"slug":20,"properties":194,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":197,"statistic":20},[],{"title":195},{"VI":196},"Christian Doppler Laboratory for Innovative Therapy Approaches in Sepsis, Danube University Krems, Krems, 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Rüger",{"id":248,"sortIndex":249,"researcher":20,"roles":250,"affiliations":251,"properties":260},"ead2d376-553e-49eb-8086-f2c77114b9ef",4,[188],[252],{"id":253,"sortIndex":21,"affiliation":254,"properties":20},"44cd9569-d003-4675-b7b1-5a24c1211df7",{"id":253,"createTime":20,"updateTime":20,"relativeEntities":255,"slug":20,"properties":256,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":259,"statistic":20},[],{"title":257},{"VI":258},"Institute for Hygiene and Applied Immunology, Medical University of Vienna, Vienna, Austria",[],{"title":261},{"VI":262},"Gerold 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study was performed to evaluate anti-inflammatory and immune modulating properties of the probiotic, spore-forming bacterial strain: Bacillus coagulans: GBI-30, (PTA-6086, GanedenBC30TM). In addition, cell wall and metabolite fractions were assayed separately to address whether biological effects were due to cell wall components only, or whether secreted compounds from live bacteria had additional biological properties. The spores were heat-activated, and bacterial cultures were grown. The culture supernatant was harvested as a source of metabolites (MTB), and the bacteria were used to isolate cell wall fragments (CW). Both of these fractions were compared in a series of in vitro assays. Both MTB and CW inhibited spontaneous and oxidative stress-induced ROS formation in human PMN cells and increased the phagocytic activity of PMN cells in response to bacteria-like carboxylated fluorospheres. Both fractions supported random PMN and f-MLP-directed PMN cell migration, indicating a support of immune surveillance and antibacterial defense mechanisms. In contrast, low doses of both fractions inhibited PMN cell migration towards the inflammatory mediators IL-8 and LTB4. The anti-inflammatory activity was strongest for CW, where the PMN migration towards IL-8 was inhibited down to dilutions of 1010. Both MTB and CW induced the expression of the CD69 activation marker on human CD3- CD56+ NK cells, and enhanced the expression of CD107a when exposed to K562 tumor cells in vitro. The fractions directly modulated cytokine production, inducing production of the Th2 cytokines IL-4, IL-6, and IL-10, and inhibiting production of IL-2. Both fractions further modulated mitogen-induced cytokine production in the following manner: Both fractions enhanced the PHA-induced production of IL-6 and reduced the PHA-induced production of TNF-alpha. Both fractions enhanced the PWM-induced production of TNF-alpha and IFN-gamma. In addition, MTB also enhanced both the PHA- and the PWM-induced expression of IL-10. The data suggest that consumption of GanedenBC30TM may introduce both cell wall components and metabolites that modulate inflammatory processes in the gut. Both the cell wall and the supernatant possess strong immune modulating properties in vitro. The anti-inflammatory effects, combined with direct induction of IL-10, are of interest with respect to possible treatment of inflammatory bowel diseases as well as in support of a healthy immune system.",{"EN":373},"GanedenBC30™ cell wall and metabolites: anti-inflammatory and immune modulating effects in vitro",{"VOID":375},"[\"5578420256027301410\"]",{"EN":377},"",{"VOID":379},"Rescigno M, Lopatin U, Chieppa M: Interactions among dendritic cells, macrophages, and epithelial cells in the gut: implications for immune tolerance. Curr Opin Immunol. 2008, 20: 669-75. 10.1016\u002Fj.coi.2008.09.007.\nRuemmele FM, Bier D, Marteau P, Rechkemmer G, Bourdet-Sicard R, Walker WA, Goulet O: Clinical evidence for immunomodulatory effects of probiotic bacteria. J Pediatr Gastroenterol Nutr. 2009, 48: 126-41. 10.1097\u002FMPG.0b013e31817d80ca.\nKim YS, Young MR, Bobe G, Colburn NH, Milner JA: Bioactive food components, inflammatory targets, and cancer prevention. Cancer Prev Res (Phila Pa). 2009, 2: 200-8.\nTurnbaugh PJ, Ley RE, Mahowald MA, Magrini V, Mardis ER, Gordon JI: An obesity-associated gut microbiome with increased capacity for energy harvest. Nature. 2006, 444: 1027-31. 10.1038\u002Fnature05414.\nKushner I, Rzewnicki D, Samols D: What does minor elevation of C-reactive protein signify?. Am J Med. 2006, 119: e17-28. 10.1016\u002Fj.amjmed.2005.06.057.\nKarin M, Lawrence T, Nizet V: Innate immunity gone awry: linking microbial infections to chronic inflammation and cancer. Cell. 2006, 124: 823-35. 10.1016\u002Fj.cell.2006.02.016.\nHormannsperger G, Haller D: Molecular crosstalk of probiotic bacteria with the intestinal immune system: Clinical relevance in the context of inflammatory bowel disease. Int J Med Microbiol. 2010, 300 (1): 63-73. 10.1016\u002Fj.ijmm.2009.08.006.\nde Vrese M, Schrezenmeir J: Probiotics, prebiotics, and synbiotics. Adv Biochem Eng Biotechnol. 2008, 111: 1-66.\nNg SC, Hart AL, Kamm MA, Stagg AJ, Knight SC: Mechanisms of action of probiotics: recent advances. Inflamm Bowel Dis. 2009, 15: 300-10. 10.1002\u002Fibd.20602.\nDuerkop BA, Vaishnava S, Hooper LV: Immune responses to the microbiota at the intestinal mucosal surface. Immunity. 2009, 31: 368-76. 10.1016\u002Fj.immuni.2009.08.009.\nDominguez-Bello MG, Blaser MJ: Do you have a probiotic in your future?. Microbes Infect. 2008, 10: 1072-6. 10.1016\u002Fj.micinf.2008.07.036.\nBezkorovainy A: Probiotics: determinants of survival and growth in the gut. Am J Clin Nutr. 2001, 73: 399S-405S.\nGraff S, Chaumeil JC, Boy P, Lai-Kuen R, Charrueau C: Formulations for protecting the probiotic Saccharomyces boulardii from degradation in acidic condition. Biol Pharm Bull. 2008, 31: 266-72. 10.1248\u002Fbpb.31.266.\nLjungh A, Wadstrom T: Lactic acid bacteria as probiotics. Curr Issues Intest Microbiol. 2006, 7: 73-89.\nCasula G, Cutting SM: Bacillus probiotics: spore germination in the gastrointestinal tract. Appl Environ Microbiol. 2002, 68: 2344-52. 10.1128\u002FAEM.68.5.2344-2352.2002.\nEndres JR, Clewell A, Jade KA, Farber T, Hauswirth J, Schauss AG: Safety assessment of a proprietary preparation of a novel Probiotic, Bacillus coagulans, as a food ingredient. Food Chem Toxicol. 2009, 47: 1231-8. 10.1016\u002Fj.fct.2009.02.018.\nSanders ME, Morelli L, Tompkins TA: Sporeformers as human probiotics: Bacillus, Sporolactobacillus, and Brevibacillus. Compr Rev Food Sci Food Saf. 2003, 2: 101-110. 10.1111\u002Fj.1541-4337.2003.tb00017.x.\nHun L: Bacillus coagulans significantly improved abdominal pain and bloating in patients with IBS. Postgrad Med. 2009, 121: 119-24. 10.3810\u002Fpgm.2009.03.1984.\nBaron M: A patented strain of Bacillus coagulans increased immune response to viral challenge. Postgrad Med. 2009, 121: 114-8. 10.3810\u002Fpgm.2009.03.1971.\nOstad SN, Salarian AA, Ghahramani MH, Fazeli MR, Samadi N, Jamalifar H: Live and heat-inactivated lactobacilli from feces inhibit Salmonella typhi and Escherichia coli adherence to Caco-2 cells. Folia Microbiol (Praha). 2009, 54: 157-60. 10.1007\u002Fs12223-009-0024-7.\nDelcenserie V, Martel D, Lamoureux M, Amiot J, Boutin Y, Roy D: Immunomodulatory effects of probiotics in the intestinal tract. Curr Issues Mol Biol. 2008, 10: 37-54.\nNeish AS: Microbes in gastrointestinal health and disease. Gastroenterology. 2009, 136: 65-80. 10.1053\u002Fj.gastro.2008.10.080.\nDraing C, Sigel S, Deininger S, Traub S, Munke R, Mayer C, Hareng L, Hartung T, von Aulock S, Hermann C: Cytokine induction by Gram-positive bacteria. Immunobiology. 2008, 213: 285-96. 10.1016\u002Fj.imbio.2007.12.001.\nLi WI, Brackett BG, Halper J: Culture supernatant of Lactobacillus acidophilus stimulates proliferation of embryonic cells. Exp Biol Med (Maywood). 2005, 230: 494-500.\nHonzel D, Carter SG, Redman KA, Schauss AG, Endres JR, Jensen GS: Comparison of Chemical and Cell-Based Antioxidant Methods for Evaluation of Foods and Natural Products: Generating Multifaceted Data by Parallel Testing Using Erythrocytes and Polymorphonuclear Cells. J Agric Food Chem. 2008, 56: 8319-8325. 10.1021\u002Fjf800401d.\nJensen GS, Patterson KM, Barnes J, Schauss AG, Beaman R, Reeves SG, Robinson LE: A Double-Blind Placebo-Controlled, Randomized Pilot Study: Consumption of a High-Metabolite Immunogen from Yeast Culture has Beneficial Effects on Erythrocyte Health and Mucosal Immune Protection in Healthy Subjects. Open Nutrition Journal. 2008, 2: 68-75. 10.2174\u002F1874288200802010068.\nHart AN, Zaske LA, Patterson KM, Drapeau C, Jensen GS: Natural killer cell activation and modulation of chemokine receptor profile in vitro by an extract from the cyanophyta Aphanizomenon flos-aquae. J Med Food. 2007, 10: 435-41. 10.1089\u002Fjmf.2007.401.\nJensen GS, Hart AN, Schauss AG: An antiinflammatory immunogen from yeast culture induces activation and alters chemokine receptor expression on human natural killer cells and B lymphocytes in vitro. Nutrition Research. 2007, 27: 327-335. 10.1016\u002Fj.nutres.2007.04.008.\nAlter G, Malenfant JM, Altfeld M: CD107a as a functional marker for the identification of natural killer cell activity. J Immunol Methods. 2004, 294: 15-22. 10.1016\u002Fj.jim.2004.08.008.\nClausen J, Vergeiner B, Enk M, Petzer AL, Gastl G, Gunsilius E: Functional significance of the activation-associated receptors CD25 and CD69 on human NK-cells and NK-like T-cells. Immunobiology. 2003, 207: 85-93. 10.1078\u002F0171-2985-00219.\nHarris G, KuoLee R, Chen W: Role of Toll-like receptors in health and diseases of gastrointestinal tract. World J Gastroenterol. 2006, 12: 2149-60.\nNeurath MF, Finotto S, Glimcher LH: The role of Th1\u002FTh2 polarization in mucosal immunity. Nat Med. 2002, 8: 567-73. 10.1038\u002Fnm0602-567.\nNicholson LB, Raveney BJ, Munder M: Monocyte dependent regulation of autoimmune inflammation. Curr Mol Med. 2009, 9: 23-9. 10.2174\u002F156652409787314499.\nBraat H, Rottiers P, Hommes DW, Huyghebaert N, Remaut E, Remon JP, van Deventer SJ, Neirynck S, Peppelenbosch MP, Steidler L: A phase I trial with transgenic bacteria expressing interleukin-10 in Crohn's disease. Clin Gastroenterol Hepatol. 2006, 4: 754-9. 10.1016\u002Fj.cgh.2006.03.028.\nMoretto MM, Weiss LM, Combe CL, Khan IA: IFN-gamma-producing dendritic cells are important for priming of gut intraepithelial lymphocyte response against intracellular parasitic infection. 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As a critical downstream mediator of PI3K signaling, mTOR is important for lymphocyte development and function of mature T and B-cells. Most studies of mTOR in immune responses have relied on the use of pharmacological inhibitors, such as rapamycin. Rapamycin-FKBP12 complex exerts its immunosuppressive and anti-proliferative effect by binding outside the kinase domain of mTOR, and subsequently inhibiting downstream mTOR signaling.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>Results\u003C\u002Fjats:title>\u003Cjats:p>To determine the requirement for mTOR kinase activity in the immune system function, we generated knock-in mice carrying a mutation (D2338) in the catalytic domain of mTOR. While homozygous mTOR kd\u002Fkd embryos died before embryonic day 6.5, heterozygous mTOR+\u002Fkd mice appeared entirely normal and are fertile. mTOR +\u002Fkd mice exhibited normal T and B cell development and unaltered proliferative responses of splenocytes to IL-2 and TCR\u002FCD28. In addition, heterozygousity for the mTOR kinase-dead allele did not sensitize T cells to rapamycin in a CD3-mediated proliferation assay. Unexpectedly, mTOR kinase activity towards its substrate 4E-BP1 was not decreased in hearts and livers from heterozygous animals.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>Conclusion\u003C\u002Fjats:title>\u003Cjats:p>Altogether, our findings indicate that mTOR kinase activity is indispensable for the early development of mouse embryos. Moreover, a single wild type mTOR allele is sufficient to maintain normal postnatal growth and lymphocyte development and proliferation.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>",{"EN":902},"A kinase-dead knock-in mutation in mTOR leads to early embryonic lethality and is dispensable for the immune system in heterozygous mice",{"VOID":904},"19457267",{"VOID":906},"10.1186\u002F1471-2172-10-28","2024-05-15T12:42:51.213+00:00",[515],"https:\u002F\u002Fbmcimmunol.biomedcentral.com\u002Farticles\u002F10.1186\u002F1471-2172-10-28",[911,928,945],{"id":912,"sortIndex":21,"researcher":20,"roles":913,"affiliations":914,"properties":923},"ad5bcb92-699b-4ed1-b3ec-81ce24eba079",[],[915],{"id":916,"sortIndex":21,"affiliation":917,"properties":20},"6f4cc76d-d0a6-4f08-92e1-1f44dd62ea7b",{"id":916,"createTime":20,"updateTime":20,"relativeEntities":918,"slug":20,"properties":919,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":922,"statistic":20},[],{"title":920},{"EN":921},"Inflammation Research Team, Drug Discovery, Johnson and Johnson Pharmaceutical Research and Development, LLC, Raritan, NJ, USA",[],{"title":924,"openalex":926},{"EN":925},"Boris Shor",{"VOID":927},"A5062994795",{"id":929,"sortIndex":203,"researcher":20,"roles":930,"affiliations":931,"properties":938},"90dd0892-889c-4b9b-8783-3ec97f165741",[],[932],{"id":916,"sortIndex":21,"affiliation":933,"properties":20},{"id":916,"createTime":20,"updateTime":20,"relativeEntities":934,"slug":20,"properties":935,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":937,"statistic":20},[],{"title":936},{"EN":921},[],{"title":939,"gsAuthor":941,"openalex":943},{"EN":940},"Druie Cavender",{"VOID":942},"[\"zdWDTwcAAAAJ\"]",{"VOID":944},"A5004005249",{"id":946,"sortIndex":219,"researcher":20,"roles":947,"affiliations":948,"properties":955},"3656bf44-8298-4ef3-921f-38d5a3fbdcde",[],[949],{"id":916,"sortIndex":21,"affiliation":950,"properties":20},{"id":916,"createTime":20,"updateTime":20,"relativeEntities":951,"slug":20,"properties":952,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":954,"statistic":20},[],{"title":953},{"EN":921},[],{"title":956,"openalex":958},{"EN":957},"Crafford A. 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Int J Immunopharmacol. 1998, 20: 241-52. 10.1016\u002FS0192-0561(98)00029-0.",{"doi":1162},"10.1016\u002FS0192-0561(98)00029-0",{"id":20,"text":1164,"url":20,"identifiers":1165},"Dumont FJ, Staruch MJ, Koprak SL, Melino MR, Sigal NH: Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin. J Immunol. 1990, 144: 251-8.",{"doi":1166},"10.4049\u002Fjimmunol.144.1.251",{"id":1168,"createTime":1169,"updateTime":1170,"relativeEntities":1171,"slug":1172,"properties":1173,"entityType":179,"verifyStatus":180,"verifyTime":1186,"verifyNote":182,"languages":20,"translateLanguages":1187,"viewCount":21,"primaryUrl":1189,"fullTextUrl":20,"authors":1190,"publicationType":306,"publisherRelationship":1280,"citationCount":1327,"citationInfo":1328,"publishDate":1332,"publishYear":1329,"citationAnalyzeStatus":19,"lastCitationAnalyze":1333,"indexDatabases":1334,"openAccess":20,"references":1335,"isForceReanalyzing":362},"102908d1-58a0-416f-8019-32b67e2ef223","2024-01-14T20:28:13.405+00:00","2026-07-13T14:45:57.140+00:00",[],"BMP-6-inhibits-growth-of-mature-human-B-cells-induction-of-Smad-phosphorylation-and-upregulation-of-Id1",{"abstract":1174,"title":1177,"gsPaper":1180,"keywords":1182,"doi":1184},{"EN":1175,"VI":1176},"Bone morphogenetic proteins (BMPs) belong to the TGF-β superfamily and are secreted proteins with pleiotropic roles in many different cell types. A potential role of BMP-6 in the immune system has been implied by various studies of malignant and rheumatoid diseases. In the present study, we explored the role of BMP-6 in normal human peripheral blood B cells. The B cells were found to express BMP type I and type II receptors and BMP-6 rapidly induced phosphorylation of Smad1\u002F5\u002F8. Furthermore, Smad-phosphorylation was followed by upregulation of Id1 mRNA and Id1 protein, whereas Id2 and Id3 expression was not affected. Furthermore, we found that BMP-6 had an antiproliferative effect both in naïve (CD19+CD27-) and memory B cells (CD19+CD27+) stimulated with anti-IgM alone or the combined action of anti-IgM and CD40L. Additionally, BMP-6 induced cell death in activated memory B cells. Importantly, the antiproliferative effect of BMP-6 in B-cells was completely neutralized by the natural antagonist, noggin. Furthermore, B cells were demonstrated to upregulate BMP-6 mRNA upon stimulation with anti-IgM. In mature human B cells, BMP-6 inhibited cell growth, and rapidly induced phosphorylation of Smad1\u002F5\u002F8 followed by an upregulation of Id1.","Protein tạo hình xương (BMP) thuộc siêu họ TGF-β và là các protein được tiết ra với nhiều vai trò khác nhau ở nhiều loại tế bào. Một vai trò tiềm năng của BMP-6 trong hệ miễn dịch đã được ngụ ý qua nhiều nghiên cứu về các bệnh ác tính và viêm khớp. Trong nghiên cứu này, chúng tôi đã khám phá vai trò của BMP-6 trong các tế bào B ngoại vi máu ở người bình thường. Các tế bào B được phát hiện có biểu hiện thụ thể loại I và loại II của BMP, và BMP-6 nhanh chóng kích thích phosphoryl hóa Smad1\u002F5\u002F8. Hơn nữa, việc phosphoryl hóa Smad dẫn đến việc tăng cường mRNA Id1 và protein Id1, trong khi biểu hiện Id2 và Id3 không bị ảnh hưởng. Thêm vào đó, chúng tôi phát hiện rằng BMP-6 có tác động ức chế sinh sản đối với cả tế bào B chưa trưởng thành (CD19+CD27-) và tế bào B ghi nhớ (CD19+CD27+) khi được kích thích bằng anti-IgM hoặc sự kết hợp của anti-IgM và CD40L. Ngoài ra, BMP-6 đã gây ra cái chết tế bào trong các tế bào B ghi nhớ đã được kích hoạt. Quan trọng hơn, tác động ức chế sinh sản của BMP-6 trong các tế bào B đã bị trung hòa hoàn toàn bởi đối kháng tự nhiên, noggin. Thêm vào đó, các tế bào B được chứng minh là tăng cường mRNA BMP-6 khi được kích thích bằng anti-IgM. Ở các tế bào B trưởng thành của người, BMP-6 đã ức chế sự phát triển tế bào và nhanh chóng kích thích phosphoryl hóa Smad1\u002F5\u002F8, tiếp theo là tăng cường biểu hiện Id1.",{"EN":1178,"VI":1179},"BMP-6 inhibits growth of mature human B cells; induction of Smad phosphorylation and upregulation of Id1","BMP-6 ức chế sự phát triển của các tế bào B trưởng thành ở người; kích thích phosphorylation Smad và tăng cường biểu hiện Id1",{"VOID":1181},"[\"6116852634650652659\"]",{"VI":1183},"BMP-6, tế bào B trưởng thành, phosphoryl hóa Smad, Id1, hệ miễn dịch",{"VOID":1185},"10.1186\u002F1471-2172-6-9","2024-04-27T00:52:15.539+00:00",[1188],"VI","https:\u002F\u002Fbmcimmunol.biomedcentral.com\u002Farticles\u002F10.1186\u002F1471-2172-6-9",[1191,1206,1219,1232,1245,1267],{"id":1192,"sortIndex":21,"researcher":20,"roles":1193,"affiliations":1194,"properties":1203},"c25e84ae-0802-454a-9c7c-46dc735c93a8",[188],[1195],{"id":1196,"sortIndex":21,"affiliation":1197,"properties":20},"b3e1f7cd-74dd-4bae-a671-97972a279557",{"id":1196,"createTime":20,"updateTime":20,"relativeEntities":1198,"slug":20,"properties":1199,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1202,"statistic":20},[],{"title":1200},{"VI":1201},"Department of Immunology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo, Norway",[],{"title":1204},{"VI":1205},"Christian Kersten",{"id":1207,"sortIndex":203,"researcher":20,"roles":1208,"affiliations":1209,"properties":1216},"d73fa62a-6c4e-4d0c-a614-477a17cb5b1c",[188],[1210],{"id":1196,"sortIndex":21,"affiliation":1211,"properties":20},{"id":1196,"createTime":20,"updateTime":20,"relativeEntities":1212,"slug":20,"properties":1213,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1215,"statistic":20},[],{"title":1214},{"VI":1201},[],{"title":1217},{"VI":1218},"Einar A 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Norway",[],{},{"title":1265},{"VI":1266},"Erlend B Smeland",{"id":1268,"sortIndex":265,"researcher":20,"roles":1269,"affiliations":1270,"properties":1277},"0bb824b8-4983-431b-b64c-984b28908e15",[188],[1271],{"id":1196,"sortIndex":21,"affiliation":1272,"properties":20},{"id":1196,"createTime":20,"updateTime":20,"relativeEntities":1273,"slug":20,"properties":1274,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1276,"statistic":20},[],{"title":1275},{"VI":1201},[],{"title":1278},{"VI":1279},"June H 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D, Zhao M, Harris SE, Mi Z: Signal transduction and biological functions of bone morphogenetic proteins. Front Biosci. 2004, 9 (349-58): 349-358.","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":1341},"10.1007\u002Fs10440-022-00541-7",{"id":1337,"text":1343,"url":1339,"identifiers":1344},"Urist MR: Bone: formation by autoinduction. Science. 1965, 150: 893-899.",{"doi":1341},{"id":1337,"text":1346,"url":1339,"identifiers":1347},"Wozney JM, Rosen V, Celeste AJ, Mitsock LM, Whitters MJ, Kriz RW, Hewick RM, Wang EA: Novel regulators of bone formation: molecular clones and activities. Science. 1988, 242: 1528-1534.",{"doi":1341},{"id":20,"text":1349,"url":1350,"identifiers":1351},"Kim SJ, Letterio J: Transforming growth factor-beta signaling in normal and malignant hematopoiesis. Leukemia. 2003, 17: 1731-1737. 10.1038\u002Fsj.leu.2403069.","http:\u002F\u002Fdx.doi.org\u002F10.1038\u002Fsj.leu.2403069",{"doi":1352},"10.1038\u002Fsj.leu.2403069",{"id":20,"text":1354,"url":1355,"identifiers":1356},"Bhatia M, Bonnet D, Wu D, Murdoch B, Wrana J, Gallacher L, Dick JE: Bone morphogenetic proteins regulate the developmental program of human hematopoietic stem cells. J Exp Med. 1999, 189: 1139-1148. 10.1084\u002Fjem.189.7.1139.","https:\u002F\u002Fdoi.org\u002F10.1084\u002Fjem.189.7.1139",{"mag":1357,"pmc":1358,"openalex":1359,"pm":1360,"doi":1361},"1972124518","2193014","W1972124518","10190905","10.1084\u002Fjem.189.7.1139",{"id":1337,"text":1363,"url":1339,"identifiers":1364},"Hager-Theodorides AL, Outram SV, Shah DK, Sacedon R, Shrimpton RE, Vicente A, Varas A, Crompton T: Bone morphogenetic protein 2\u002F4 signaling regulates early thymocyte differentiation. J Immunol. 2002, 169: 5496-5504.",{"doi":1341},{"id":20,"text":1366,"url":1367,"identifiers":1368},"Graf D, Nethisinghe S, Palmer DB, Fisher AG, Merkenschlager M: The developmentally regulated expression of Twisted gastrulation reveals a role for bone morphogenetic proteins in the control of T cell development. J Exp Med. 2002, 196: 163-171. 10.1084\u002Fjem.20020276.","https:\u002F\u002Fdoi.org\u002F10.1084\u002Fjem.20020276",{"mag":1369,"pmc":1370,"openalex":1371,"pm":1372,"doi":1373},"2127603688","2193926","W2127603688","12119341","10.1084\u002Fjem.20020276",{"id":1375,"text":1376,"url":1377,"identifiers":1378},"0df35a6e-871a-4b0b-92d1-5fd58a4975c0","Ahmed N, Sammons J, Carson RJ, Khokher MA, Hassan HT: Effect of bone morphogenetic protein-6 on haemopoietic stem cells and cytokine production in normal human bone marrow stroma. Cell Biol Int. 2001, 25: 429-435. 10.1006\u002Fcbir.2000.0662.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1065699500906620",{"doi":1379},"10.1006\u002Fcbir.2000.0662",{"id":1337,"text":1381,"url":1339,"identifiers":1382},"Kawamura C, Kizaki M, Yamato K, Uchida H, Fukuchi Y, Hattori Y, Koseki T, Nishihara T, Ikeda Y: Bone morphogenetic protein-2 induces apoptosis in human myeloma cells with modulation of STAT3. Blood. 2000, 96: 2005-2011.",{"doi":1341},{"id":1384,"text":1385,"url":1386,"identifiers":1387},"63b84a60-d0fa-4850-aec5-0f5e41f32729","Hjertner O, Hjorth-Hansen H, Borset M, Seidel C, Waage A, Sundan A: Bone morphogenetic protein-4 inhibits proliferation and induces apoptosis of multiple myeloma cells. Blood. 2001, 97: 516-522. 10.1182\u002Fblood.V97.2.516.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006497120660190",{"doi":1388},"10.1182\u002Fblood.v97.2.516",{"id":20,"text":1390,"url":1391,"identifiers":1392},"Baade RT, Utne HR, Brenne AT, Hjorth-Hansen H, Waage A, Hjertner O, Sundan A, Borset M: Bone morphogenetic protein-5, -6 and -7 inhibit growth and induce apoptosis in human myeloma cells. Oncogene. 2004, 23 (17): 3024-3032. 10.1038\u002Fsj.onc.1207386.","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsj.onc.1207386",{"mag":1393,"openalex":1394,"pm":1395,"doi":1396},"1983672040","W1983672040","14691444","10.1038\u002Fsj.onc.1207386",{"id":20,"text":1398,"url":1399,"identifiers":1400},"Rosenwald A, Wright G, Chan WC, Connors JM, Campo E, Fisher RI, Gascoyne RD, Muller-Hermelink HK, Smeland EB, Giltnane JM, Hurt EM, Zhao H, Averett L, Yang L, Wilson WH, Jaffe ES, Simon R, Klausner RD, Powell J, Duffey PL, Longo DL, Greiner TC, Weisenburger DD, Sanger WG, Dave BJ, Lynch JC, Vose J, Armitage JO, Montserrat E, Lopez-Guillermo A, Grogan TM, Miller TP, LeBlanc M, Ott G, Kvaloy S, Delabie J, Holte H, Krajci P, Stokke T, Staudt LM: The use of molecular profiling to predict survival after chemotherapy for diffuse large-B-cell lymphoma. N Engl J Med. 2002, 346: 1937-1947. 10.1056\u002FNEJMoa012914.","https:\u002F\u002Fdoi.org\u002F10.1056\u002Fnejmoa012914",{"mag":1401,"openalex":1402,"pm":1403,"doi":1404},"1976564639","W1976564639","12075054","10.1056\u002Fnejmoa012914",{"id":20,"text":1406,"url":1407,"identifiers":1408},"Waite KA, Eng C: From developmental disorder to heritable cancer: it's all in the BMP\u002FTGF-beta family. Nat Rev Genet. 2003, 4: 763-773. 10.1038\u002Fnrg1178.","http:\u002F\u002Fdx.doi.org\u002F10.1038\u002Fnrg1178",{"doi":1409},"10.1038\u002Fnrg1178",{"id":20,"text":1411,"url":1412,"identifiers":1413},"Ying QL, Nichols J, Chambers I, Smith A: BMP induction of Id proteins suppresses differentiation and sustains embryonic stem cell self-renewal in collaboration with STAT3. Cell. 2003, 115: 281-292. 10.1016\u002FS0092-8674(03)00847-X.","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0092-8674(03)00847-x",{"mag":1414,"openalex":1415,"pm":1416,"doi":1417},"1992949513","W1992949513","14636556","10.1016\u002Fs0092-8674(03)00847-x",{"id":20,"text":1419,"url":1420,"identifiers":1421},"Klein U, Rajewsky K, Kuppers R: Human immunoglobulin (Ig)M+IgD+ peripheral blood B cells expressing the CD27 cell surface antigen carry somatically mutated variable region genes: CD27 as a general marker for somatically mutated (memory) B cells. J Exp Med. 1998, 188: 1679-1689. 10.1084\u002Fjem.188.9.1679.","https:\u002F\u002Fdoi.org\u002F10.1084\u002Fjem.188.9.1679",{"mag":1422,"pmc":1423,"openalex":1424,"pm":1425,"doi":1426},"2086703018","2212515","W2086703018","9802980","10.1084\u002Fjem.188.9.1679",{"id":1337,"text":1428,"url":1339,"identifiers":1429},"Aoki H, Fujii M, Imamura T, Yagi K, Takehara K, Kato M, Miyazono K: Synergistic effects of different bone morphogenetic protein type I receptors on alkaline phosphatase induction. J Cell Sci. 2001, 114: 1483-1489.",{"doi":1341},{"id":20,"text":1431,"url":1432,"identifiers":1433},"Miyazawa K, Shinozaki M, Hara T, Furuya T, Miyazono K: Two major Smad pathways in TGF-beta superfamily signalling. Genes Cells. 2002, 7: 1191-1204. 10.1046\u002Fj.1365-2443.2002.00599.x.","http:\u002F\u002Fdx.doi.org\u002F10.1046\u002Fj.1365-2443.2002.00599.x",{"doi":1434},"10.1046\u002Fj.1365-2443.2002.00599.x",{"id":1337,"text":1436,"url":1339,"identifiers":1437},"Grimsrud CD, Romano PR, D'Souza M, Puzas JE, Reynolds PR, Rosier RN, O'Keefe RJ: BMP-6 is an autocrine stimulator of chondrocyte differentiation. J Bone Miner Res. 1999, 14: 475-482.",{"doi":1341},{"id":20,"text":1439,"url":1440,"identifiers":1441},"Shepherd TG, Nachtigal MW: Identification of a putative autocrine bone morphogenetic protein-signaling pathway in human ovarian surface epithelium and ovarian cancer cells. Endocrinology. 2003, 144: 3306-3314. 10.1210\u002Fen.2003-0185.","https:\u002F\u002Fdoi.org\u002F10.1210\u002Fen.2003-0185",{"mag":1442,"openalex":1443,"pm":1444,"doi":1445},"2032084074","W2032084074","12865307","10.1210\u002Fen.2003-0185",{"id":20,"text":1447,"url":20,"identifiers":1448},"Detmer K, Steele TA, Shoop MA, Dannawi H: Lineage-restricted expression of bone morphogenetic protein genes in human hematopoietic cell lines. Blood Cells Mol Dis. 1999, 25: 310-323. 10.1006\u002Fbcmd.1999.0259.",{"doi":1449},"10.1006\u002Fbcmd.1999.0259",{"id":20,"text":1451,"url":1452,"identifiers":1453},"Winkler DG, Yu C, Geoghegan JC, Ojala EW, Skonier JE, Shpektor D, Sutherland MK, Latham JA: Noggin and sclerostin bone morphogenetic protein antagonists form a mutually inhibitory complex. 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Leukemia. 2003, 17: 789-795. 10.1038\u002Fsj.leu.2402880.","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsj.leu.2402880",{"mag":1666,"openalex":1667,"pm":1668,"doi":1669},"1982060052","W1982060052","12682640","10.1038\u002Fsj.leu.2402880",{"id":1671,"createTime":1672,"updateTime":1673,"relativeEntities":1674,"slug":1675,"properties":1676,"entityType":179,"verifyStatus":180,"verifyTime":1687,"verifyNote":182,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1688,"fullTextUrl":20,"authors":1689,"publicationType":306,"publisherRelationship":1879,"citationCount":20,"citationInfo":20,"publishDate":1926,"publishYear":1927,"citationAnalyzeStatus":19,"lastCitationAnalyze":1928,"indexDatabases":1929,"openAccess":20,"references":20,"isForceReanalyzing":362},"671207e8-7045-4399-8161-ed345782c17a","2024-01-11T07:25:18.622+00:00","2026-07-11T14:51:27.488+00:00",[],"Down-regulation-of-granulocyte-macrophage-colony-stimulating-factor-by-3C-like-proteinase-in-transfected-A549-human-lung-carcinoma-cells",{"abstract":1677,"title":1679,"gsPaper":1681,"references":1683,"doi":1685},{"EN":1678},"Severe Acute Respiratory Syndrome (SARS) is a severe respiratory illness caused by a novel virus, the SARS coronavirus (SARS-CoV). 3C-like protease (3CLpro) of SARS-CoV plays a role in processing viral polypeptide precursors and is responsible of viral maturation. However, the function of 3CLpro in host cells remains unknown. This study investigated how the 3CLpro affected the secretion of cytokines in the gene-transfected cells. From immunofluorescence microscopy, the localization of c-myc tagged 3CLpro was detected both in the cytoplasm and nucleus of transfected A549 cells. Expression of granulocyte-macrophage colony-stimulating factor (GM-CSF) was significantly decreased in 3CLpro-transfected cells by both RT-PCR and ELISA, but without changes in other cytokines, i.e., IL-1β, IL-6, IL-8, IL12p40, TNF-α, and TGF-β. Furthermore, the protein levels of NF-kB decreased in 3CLpro-transfected A549 cells when compared to EGFP transfected cells. Our results suggest that the 3CLpro may suppress expression of GM-CSF in transfected A549 cells through down-regulation of NF-kB production.",{"EN":1680},"Down-regulation of granulocyte-macrophage colony-stimulating factor by 3C-like proteinase in transfected A549 human lung carcinoma cells",{"VOID":1682},"[\"18128750802719736498\"]",{"VOID":1684},"Fouchier RA, Kuiken T, Schutten M, van Amerongen G, van Doornum GJ, van den Hoogen BG, Peiris M, Lim W, Stohr K, Osterhaus AD: Aetiology: Koch's postulates fulfilled for SARS virus. Nature. 2003, 423: 240-10.1038\u002F423240a.\nRota PA, Oberste MS, Monroe SS, Nix WA, Campagnoli R, Icenogle JP, Penaranda S, Bankamp B, Maher K, Chen MH, et al: Characterization of a novel coronavirus associated with severe acute respiratory syndrome. 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Science. 2003, 300: 1763-7. 10.1126\u002Fscience.1085658.\nHuang C, Wei P, Fan K, Liu Y, Lai L: 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism. Biochemistry. 2004, 43: 4568-74. 10.1021\u002Fbi036022q.\nLin CW, Lin KH, Hsieh TH, Shiu SY, Li JY: Severe acute respiratory syndrome coronavirus 3C-like protease-induced apoptosis. FEMS Immunol Med Microbiol. 2006, 46: 375-80. 10.1111\u002Fj.1574-695X.2006.00045.x.\nLin CW, Tsai FJ, Wan L, Lai CC, Lin KH, Hsieh TH, Shiu SY, Li JY: Binding interaction of SARS coronavirus 3CL(pro) protease with vacuolar-H+ ATPase G1 subunit. FEBS Lett. 2005, 579: 6089-94. 10.1016\u002Fj.febslet.2005.09.075.\nKiemer L, Lund O, Brunak S, Blom N: Coronavirus 3CLpro proteinase cleavage sites: possible relevance to SARS virus pathology. BMC Bioinformatics. 2004, 5: 72-10.1186\u002F1471-2105-5-72.\nNicholls JM, Poon LL, Lee KC, Ng WF, Lai ST, Leung CY, Chu CM, Hui PK, Mak KL, Lim W, et al: Lung pathology of fatal severe acute respiratory syndrome. Lancet. 2003, 361: 1773-8. 10.1016\u002FS0140-6736(03)13413-7.\nWang CH, Liu CY, Wan YL, Chou CL, Huang KH, Lin HC, Lin SM, Lin TY, Chung KF, Kuo HP: Persistence of lung inflammation and lung cytokines with high-resolution CT abnormalities during recovery from SARS. Respir Res. 2005, 6: 42-10.1186\u002F1465-9921-6-42.\nLo AW, Tang NL, To KF: How the SARS coronavirus causes disease: host or organism?. J Pathol. 2006, 208: 142-51. 10.1002\u002Fpath.1897.\nWong CK, Lam CW, Wu AK, Ip WK, Lee NL, Chan IH, Lit LC, Hui DS, Chan MH, Chung SS, et al: Plasma inflammatory cytokines and chemokines in severe acute respiratory syndrome. Clin Exp Immunol. 2004, 136: 95-103. 10.1111\u002Fj.1365-2249.2004.02415.x.\nZhu M: SARS Immunity and Vaccination. Cell Mol Immunol. 2004, 1: 193-8.\nXu X, Gao X: Immunological responses against SARS-coronavirus infection in humans. Cell Mol Immunol. 2004, 1: 119-22.\nCheung CY, Poon LL, Ng IH, Luk W, Sia SF, Wu MH, Chan KH, Yuen KY, Gordon S, Guan Y, et al: Cytokine responses in severe acute respiratory syndrome coronavirus-infected macrophages in vitro: possible relevance to pathogenesis. J Virol. 2005, 79: 7819-26. 10.1128\u002FJVI.79.12.7819-7826.2005.\nJiang Y, Xu J, Zhou C, Wu Z, Zhong S, Liu J, Luo W, Chen T, Qin Q, Deng P: Characterization of cytokine\u002Fchemokine profiles of severe acute respiratory syndrome. Am J Respir Crit Care Med. 2005, 171: 850-7. 10.1164\u002Frccm.200407-857OC.\nLin YS, Lin CF, Fang YT, Kuo YM, Liao PC, Yeh TM, Hwa KY, Shieh CC, Yen JH, Wang HJ, et al: Antibody to severe acute respiratory syndrome (SARS)-associated coronavirus spike protein domain 2 cross-reacts with lung epithelial cells and causes cytotoxicity. Clin Exp Immunol. 2005, 141: 500-8. 10.1111\u002Fj.1365-2249.2005.02864.x.\nYang YH, Huang YH, Chuang YH, Peng CM, Wang LC, Lin YT, Chiang BL: Autoantibodies against human epithelial cells and endothelial cells after severe acute respiratory syndrome (SARS)-associated coronavirus infection. J Med Virol. 2005, 77: 1-7. 10.1002\u002Fjmv.20407.\nGriego SD, Weston CB, Adams JL, Tal-Singer R, Dillon SB: Role of p38 mitogen-activated protein kinase in rhinovirus-induced cytokine production by bronchial epithelial cells. J Immunol. 2000, 165: 5211-20.\nMunoz C, Pascual-Salcedo D, Castellanos MC, Alfranca A, Aragones J, Vara A, Redondo JM, de Landazuri MO: Pyrrolidine dithiocarbamate inhibits the production of interleukin-6, interleukin-8, and granulocyte-macrophage colony-stimulating factor by human endothelial cells in response to inflammatory mediators: modulation of NF-kappa B and AP-1 transcription factors activity. Blood. 1996, 88: 3482-90.\nZiegler T, Matikainen S, Ronkko E, Osterlund P, Sillanpaa M, Siren J, Fagerlund R, Immonen M, Melen K, Julkunen I: Severe acute respiratory syndrome coronavirus fails to activate cytokine-mediated innate immune responses in cultured human monocyte-derived dendritic cells. J Virol. 2005, 79: 13800-5. 10.1128\u002FJVI.79.21.13800-13805.2005.\nWoltman AM, van der Kooij SW, Coffer PJ, Offringa R, Daha MR, van Kooten C: Rapamycin specifically interferes with GM-CSF signaling in human dendritic cells, leading to apoptosis via increased p27KIP1 expression. Blood. 2003, 101: 1439-45. 10.1182\u002Fblood-2002-06-1688.\nEager R, Nemunaitis J: GM-CSF gene-transduced tumor vaccines. Mol Ther. 2005, 12: 18-27. 10.1016\u002Fj.ymthe.2005.02.012.\nLeVine AM, Reed JA, Kurak KE, Cianciolo E, Whitsett JA: GM-CSF-deficient mice are susceptible to pulmonary group B streptococcal infection. J Clin Invest. 1999, 103: 563-9. 10.1172\u002FJCI5212.\nTrapnell BC, Whitsett JA: Gm-CSF regulates pulmonary surfactant homeostasis and alveolar macrophage-mediated innate host defense. Annu Rev Physiol. 2002, 64: 775-802. 10.1146\u002Fannurev.physiol.64.090601.113847.\nMoore BB, Coffey MJ, Christensen P, Sitterding S, Ngan R, Wilke CA, McDonald R, Phare SM, Peters-Golden M, Paine R, et al: GM-CSF regulates bleomycin-induced pulmonary fibrosis via a prostaglandin-dependent mechanism. J Immunol. 2000, 165: 4032-9.\nChristensen PJ, Bailie MB, Goodman RE, O'Brien AD, Toews GB, Paine R: Role of diminished epithelial GM-CSF in the pathogenesis of bleomycin-induced pulmonary fibrosis. Am J Physiol Lung Cell Mol Physiol. 2000, 279: L487-95.\nTrapnell BC, Whitsett JA, Nakata K: Pulmonary alveolar proteinosis. N Engl J Med. 2003, 349: 2527-39. 10.1056\u002FNEJMra023226.\nKiemer L, Lund O, Brunak S, Blom N: Coronavirus 3CLpro proteinase cleavage sites: Possible relevance to SARS virus pathology. BMC Bioinformatics. 2004, 5: 72-10.1186\u002F1471-2105-5-72.\nHegyi A, Ziebuhr J: Conservation of substrate specificities among coronavirus main proteases. J Gen Virol. 2002, 83: 595-599.\nHideshi N, Yoshiki U, Makoto K, Ryoji H, Hirokuni T: Cyclooxygenase-2 inhibitor NS-398 suppresses cell growth and constitutive production of granulocyte-colony stimulating factor and granulocyte macrophage-colony stimulating factor in lung cancer cells. Cancer Science. 2003, 94: 173-180. 10.1111\u002Fj.1349-7006.2003.tb01415.x.\nHongsachart P, Huang-Liu R, Sinchaikul S, Pan FM, Phutrakul S, Chuang YM, Yu CJ, Chen ST: Glycoproteomic analysis of WGA-bound glycoprotein biomarkers in sera from patients with lung adenocarcinoma. Electrophoresis. 2009, 30: 1206-20. 10.1002\u002Felps.200800405.",{"VOID":1686},"10.1186\u002F1471-2172-12-16","2024-06-26T14:53:42.332+00:00","https:\u002F\u002Fbmcimmunol.biomedcentral.com\u002Farticles\u002F10.1186\u002F1471-2172-12-16",[1690,1723,1752,1767,1790,1813,1842,1864],{"id":1691,"sortIndex":21,"researcher":20,"roles":1692,"affiliations":1693,"properties":1720},"7223a8f6-5dc1-49e7-8934-e5eebf64cffe",[188],[1694,1702,1711],{"id":1695,"sortIndex":21,"affiliation":1696,"properties":20},"4d135ec0-1326-45c1-8eac-9e8c40b41c03",{"id":1695,"createTime":20,"updateTime":20,"relativeEntities":1697,"slug":20,"properties":1698,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1701,"statistic":20},[],{"title":1699},{"VI":1700},"Institute of Medicine, Chung Shan Medical University, Taichung, 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cancer is the second most frequently diagnosed cancer worldwide. Weak immunogenicity helps cancer cells escape from immune elimination and grow into predominant subpopulations. This study aimed to investigate the effect of Zinc finger and BTB domain containing 7B (Zbtb7b, Alias ThPOK) on T cell activation after coculture with gastric cancer cells. Cell Counting Kit-8 assay (CCK-8) was performed to explore the viability of gastric cancer cells. Flow cytometry analysis was used to measure CD3+ T cell proliferation and the ratio of activated IFN-γ+ T cells which were co-incubated with gastric cancer cells (HGC-27, SNU-1). The binding between ThPOK and the promoter of its target sperm tail PG-rich repeat containing 1 (STPG1) was explored using ChIP and luciferase reporter assays. Relative gene expression was quantified using RT-qPCR. ThPOK was expressed at a low level in gastric cancer tissues and cells at mRNA and protein levels. Gastric cancer patients with lower ThPOK expression had poorer prognosis. ThPOK overexpression suppressed gastric cancer cell viability and increased T cell activation. ThPOK served as a transcription factor for STPG1. STPG1 expression was also at a low level in the tissues and cells of gastric cancer. ThPOK positively regulated the mRNA and protein levels of STPG1 in gastric cancer cells. Moreover, ThPOK was demonstrated to bind with STPG1 promoter. STPG1 upregulation also exerted inhibitory effects on gastric cancer cell viability and T cell activation. Additionally, ThPOK and STPG1 were revealed to inactivate the ERK pathway in gastric cancer cells. ThPOK inhibits gastric cancer cell viability and increases T cell activation by inducing STPG1 to inactivate the ERK pathway.",{"EN":1940},"ThPOK inhibits the immune escape of gastric cancer cells by inducing STPG1 to inactivate the ERK pathway",{"VOID":1942},"[\"6018824290327223556\"]",{"VOID":1944},"Smyth EC, Nilsson M, Grabsch HI, van Grieken NC, Lordick F. Gastric cancer. Lancet (London, England). 2020;396(10251):635–48.\nSchistosomes, liver flukes and Helicobacter pylori. IARC working group on the evaluation of carcinogenic risks to humans. Lyon, 7–14 June 1994. IARC Monogr Eval Carcinog Risks Hum. 1994;61:1–241.\nPlummer M, Franceschi S, Vignat J, Forman D, de Martel C. Global burden of gastric cancer attributable to Helicobacter pylori. Int J Cancer. 2015;136(2):487–90.\nInternational Agency for Research on Cancer. Personal habits and indoor combustions. Volume 100 E. A review of human carcinogens. IARC Monogr Eval Carcinog Risks Hum. 2012;100(1):1–538.\nBray F, Ferlay J, Soerjomataram I, Siegel RL, Torre LA, Jemal A. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin. 2018;68(6):394–424.\nYang Z, Yuan L, Yang L, Peng S, Yang P, He X, et al. 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Bioinformatics. 2005, 21 (18): 3674-6. 10.1093\u002Fbioinformatics\u002Fbti610.",{"doi":2435},"10.1093\u002Fbioinformatics\u002Fbti610",{"id":20,"text":2437,"url":20,"identifiers":2438},"Wickham H: Ggplot: Elegant graphics for data analysis. 2009, New York: Springer",{"doi":2439},"10.1007\u002F978-0-387-98141-3",{"id":20,"text":2441,"url":20,"identifiers":2442},"Sarkar D: Lattice: Multivariate Data Visualization with R. 2008, New York: Springer",{"doi":2443},"10.1007\u002F978-0-387-75969-2",{"id":2445,"createTime":2446,"updateTime":2447,"relativeEntities":2448,"slug":2449,"properties":2450,"entityType":179,"verifyStatus":180,"verifyTime":2459,"verifyNote":182,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":2460,"fullTextUrl":20,"authors":2461,"publicationType":306,"publisherRelationship":2542,"citationCount":21,"citationInfo":2588,"publishDate":2591,"publishYear":2589,"citationAnalyzeStatus":19,"lastCitationAnalyze":2592,"indexDatabases":2593,"openAccess":20,"references":2594,"isForceReanalyzing":362},"fb744e3e-6a94-437b-800d-c42b31d69868","2024-01-21T05:16:33.648+00:00","2026-04-21T17:20:23.469+00:00",[],"Allo-HSCT-compared-with-immunosuppressive-therapy-for-acquired-aplastic-anemia-a-system-review-and-meta-analysis",{"abstract":2451,"title":2453,"gsPaper":2455,"doi":2457},{"EN":2452},"Allogeneic hematopoietic stem cell transplantation (allo-HSCT) and immunosuppressive therapy (IST) are two major competing treatment strategies for acquired aplastic anemia (AA). Whether allo-HSCT is superior to IST as a front-line treatment for patients with AA has been a subject of debate. To compare the efficacy and safety of allo-HSCT with that of IST as a front-line treatment for patients with AA, we performed a meta-analysis of available studies that examined the impact of the two major competing treatment strategies for AA. Fifteen studies including a total of 5336 patients were included in the meta-analysis. The pooled hazard ratio (HR) for overall survival (OS) was 0.4 (95% CI 0.074–0.733, P = 0.016, I2 = 58.8%) and the pooled HR for failure-free survival (FFS) was 1.962 (95% CI 1.43–2.493, P = 0.000, I2 = 0%). The pooled relative risk (RR) for overall response rate (ORR) was 1.691 (95% CI 1.433–1.996, P = 0.000, I2 = 11.6%). Although survival was significantly longer among AA patients undergoing first-line allo-HSCT compared to those undergoing first-line IST, the selection of initial treatment for patients with newly diagnosed AA still requires comprehensive evaluation of donor availability, patient age, expected quality of life, risk of disease relapse or clonal evolution after IST, and potential use of adjunctive eltrombopag.",{"EN":2454},"Allo-HSCT compared with immunosuppressive therapy for acquired aplastic anemia: a system review and 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S. Why is the incidence of aplastic anemia higher in Asia? Expert Rev Hematol. 2017;10:277–9.",{"doi":1341},{"id":1337,"text":2599,"url":1339,"identifiers":2600},"Kaufman DW, Kelly JP, Issaragrisil S, Laporte JR, Anderson T, Levy M, Shapiro S, Young NS. Relative incidence of agranulocytosis and aplastic anemia. Am J Hematol. 2006;81:65–7.",{"doi":1341},{"id":1337,"text":2602,"url":1339,"identifiers":2603},"Young NS. Acquired aplastic anemia. Ann Intern Med. 2002;136:534–46.",{"doi":1341},{"id":1337,"text":2605,"url":1339,"identifiers":2606},"Young NS, Maciejewski J. The pathophysiology of acquired aplastic anemia. N Engl J Med. 1997;336:1365–72.",{"doi":1341},{"id":1337,"text":2608,"url":1339,"identifiers":2609},"Killick SB, Bown N, Cavenagh J, Dokal I, Foukaneli T, Hill A, Hillmen P, Ireland R, Kulasekararaj A, Mufti G, et al. Guidelines for the diagnosis and management of adult aplastic anaemia. Br J Haematol. 2016;172:187–207.",{"doi":1341},{"id":1337,"text":2611,"url":1339,"identifiers":2612},"Kulasekararaj AG, Jiang J, Smith AE, Mohamedali AM, Mian S, Gandhi S, Gaken J, Czepulkowski B, Marsh JC, Mufti GJ. Somatic mutations identify a subgroup of aplastic anemia patients who progress to myelodysplastic syndrome. Blood. 2014;124:2698–704.",{"doi":1341},{"id":1337,"text":2614,"url":1339,"identifiers":2615},"Ades L, Mary JY, Robin M, Ferry C, Porcher R, Esperou H, Ribaud P, Devergie A, Traineau R, Gluckman E, et al. Long-term outcome after bone marrow transplantation for severe aplastic anemia. Blood. 2004;103:2490–7.",{"doi":1341},{"id":1337,"text":2617,"url":1339,"identifiers":2618},"Mortensen BK, Jacobsen N, Heilmann C, Sengelov H. Allogeneic hematopoietic cell transplantation for severe aplastic anemia: similar long-term overall survival after transplantation with related donors compared to unrelated donors. Bone Marrow Transplant. 2016;51:288–90.",{"doi":1341},{"id":1337,"text":2620,"url":1339,"identifiers":2621},"Dufour C, Veys P, Carraro E, Bhatnagar N, Pillon M, Wynn R, Gibson B, Vora AJ, Steward CG, Ewins AM, et al. Similar outcome of upfront-unrelated and matched sibling stem cell transplantation in idiopathic paediatric aplastic anaemia. A study on behalf of the UK Paediatric BMT Working Party, Paediatric Diseases Working Party and Severe Aplastic Anaemia Working Party of EBMT. Br J Haematol. 2015;171:585–94.",{"doi":1341},{"id":1337,"text":2623,"url":1339,"identifiers":2624},"DeZern AE, Zahurak M, Symons H, Cooke K, Jones RJ, Brodsky RA. Alternative donor transplantation with high-dose post-transplantation cyclophosphamide for refractory severe aplastic Anemia. Biol Blood Marrow Transplant. 2017;23:498–504.",{"doi":1341},{"id":1337,"text":2626,"url":1339,"identifiers":2627},"Kojima S, Horibe K, Inaba J, Yoshimi A, Takahashi Y, Kudo K, Kato K, Matsuyama T. Long-term outcome of acquired aplastic anaemia in children: comparison between immunosuppressive therapy and bone marrow transplantation. Br J Haematol. 2000;111:321–8.",{"doi":1341},{"id":1337,"text":2629,"url":1339,"identifiers":2630},"Fouladi M, Herman R, Rolland-Grinton M, Jones-Wallace D, Blanchette V, Calderwood S, Doyle J, Halperin D, Leaker M, Saunders EF, et al. Improved survival in severe acquired aplastic anemia of childhood. Bone Marrow Transplant. 2000;26:1149–56.",{"doi":1341},{"id":1337,"text":2632,"url":1339,"identifiers":2633},"Choi YB, Yi ES, Lee JW, Sung KW, Koo HH, Yoo KH. Immunosuppressive therapy versus alternative donor hematopoietic stem cell transplantation for children with severe aplastic anemia who lack an HLA-matched familial donor. Bone Marrow Transplant. 2017;52:47–52.",{"doi":1341},{"id":1337,"text":2635,"url":1339,"identifiers":2636},"Yoshida N, Kobayashi R, Yabe H, Kosaka Y, Yagasaki H, Watanabe K, Kudo K, Morimoto A, Ohga S, Muramatsu H, et al. First-line treatment for severe aplastic anemia in children: bone marrow transplantation from a matched family donor versus immunosuppressive therapy. Haematologica. 2014;99:1784–91.",{"doi":1341},{"id":1337,"text":2638,"url":1339,"identifiers":2639},"Dufour C, Pillon M, Socie G, Rovo A, Carraro E, Bacigalupo A, Oneto R, Passweg J, Risitano A, Tichelli A, et al. Outcome of aplastic anaemia in children. A study by the severe aplastic anaemia and paediatric disease working parties of the European group blood and bone marrow transplant. Br J Haematol. 2015;169:565–73.",{"doi":1341},{"id":1337,"text":2641,"url":1339,"identifiers":2642},"Yang S, Yuan X, Ma R, Jiang L, Guo J, Zang Y, Shi J, Yang J, Lei P, Liu Z, et al. Comparison of outcomes of frontline immunosuppressive therapy and frontline Haploidentical hematopoietic stem cell transplantation for children with severe aplastic Anemia who lack an HLA-matched sibling donor. Biol Blood Marrow Transplant. 2019;25:975–80.",{"doi":1341},{"id":1337,"text":2644,"url":1339,"identifiers":2645},"Ahn MJ, Choi JH, Lee YY, Choi IY, Kim IS, Yoon SS, Park SY, Kim BK, Suh C, Son HJ, et al. Outcome of adult severe or very severe aplastic anemia treated with immunosuppressive therapy compared with bone marrow transplantation: multicenter trial. Int J Hematol. 2003;78:133–8.",{"doi":1341},{"id":1337,"text":2647,"url":1339,"identifiers":2648},"Kim I, Yoon SS, Park S, Kim BK, Kim NK. The treatment of severe aplastic anemia: outcomes of bone marrow transplantation and immunosuppressive therapy in a single institution of Korea. J Korean Med Sci. 2003;18:365–71.",{"doi":1341},{"id":1337,"text":2650,"url":1339,"identifiers":2651},"Ellis RJ, Kahn Q, Skikne BS, Mayo MS, Allgood JW, Bodensteiner DM, Deauna-Limayo D, Cook JD. A retrospective analysis of long-term survival in severe aplastic anemia patients treated with allogeneic bone marrow transplantation or immunosuppressive therapy with antithymocyte globulin and cyclosporin a at a single institution. Mil Med. 2002;167:541–5.",{"doi":1341},{"id":20,"text":2653,"url":20,"identifiers":2654},"Ghavamzadeh A, Iravani M, Vafaiezadeh F, Jahani M, Mousavi A. Bone marrow transplantation versus immunosuppressive therapy in severe aplastic anemia, 1990–2001. Arch Iranian Med. 2004;7:272–8.",{},{"id":2656,"text":2657,"url":2658,"identifiers":2659},"4a10d0a0-256f-4d64-9553-43c825e9a5eb","Viollier R, Passweg J, Gregor M, Favre G, Kuhne T, Nissen C, Gratwohl A, Tichelli A. Quality-adjusted survival analysis shows differences in outcome after immunosuppression or bone marrow transplantation in aplastic anemia. Ann Hematol. 2005;84:47–55.","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs00277-004-0930-3",{"doi":2660},"10.1007\u002Fs00277-004-0930-3",{"id":1337,"text":2662,"url":1339,"identifiers":2663},"Locasciulli A, Oneto R, Bacigalupo A, Socie G, Korthof E, Bekassy A, Schrezenmeier H, Passweg J, Fuhrer M. Outcome of patients with acquired aplastic anemia given first line bone marrow transplantation or immunosuppressive treatment in the last decade: a report from the European Group for Blood and Marrow Transplantation (EBMT). Haematologica. 2007;92:11–8.",{"doi":1341},{"id":1337,"text":2665,"url":1339,"identifiers":2666},"George B, Mathews V, Viswabandya A, Abraham A, Ganapule A, Fouzia NA, Korula A, Lakshmi KN, Chandy M, Srivastava A. Immunosuppressive therapy and bone marrow transplantation for aplastic Anaemia-the CMC experience. J Assoc Physicians India. 2015;63:36–40.",{"doi":1341},{"id":1337,"text":2668,"url":1339,"identifiers":2669},"Cheng Y, Xu Z, Zhang Y, Wu J, Wang F, Mo X, Chen Y, Han W, Jia J, Wang Y, et al. First-line choice for severe aplastic anemia in children: transplantation from a haploidentical donor vs immunosuppressive therapy. Clin Transpl. 2018;32.",{"doi":1341},{"id":1337,"text":2671,"url":1339,"identifiers":2672},"Xu ZL, Zhou M, Jia JS, Mo WJ, Zhang XH, Zhang YP, Wang Y, Li YM, Huang XJ, Wang SQ, et al. Immunosuppressive therapy versus haploidentical transplantation in adults with acquired severe aplastic anemia. Bone Marrow Transplant. 2019.",{"doi":1341},{"id":1337,"text":2674,"url":1339,"identifiers":2675},"Passweg JR, Marsh JC. Aplastic anemia: first-line treatment by immunosuppression and sibling marrow transplantation. Hematology Am Soc Hematol Educ Program. 2010;2010:36–42.",{"doi":1341},{"id":1337,"text":2677,"url":1339,"identifiers":2678},"Townsley DM, Scheinberg P, Winkler T, Desmond R, Dumitriu B, Rios O, Weinstein B, Valdez J, Lotter J, Feng X, et al. Eltrombopag added to standard immunosuppression for aplastic Anemia. N Engl J Med. 2017;376:1540–50.",{"doi":1341},{"id":1337,"text":2680,"url":1339,"identifiers":2681},"Georges GE, Doney K, Storb R. Severe aplastic anemia: allogeneic bone marrow transplantation as first-line treatment. Blood Adv. 2018;2:2020–8.",{"doi":1341},{"id":1337,"text":2683,"url":1339,"identifiers":2684},"Yoshizato T, Dumitriu B, Hosokawa K, Makishima H, Yoshida K, Townsley D, Sato-Otsubo A, Sato Y, Liu D, Suzuki H, et al. Somatic mutations and clonal hematopoiesis in aplastic Anemia. N Engl J Med. 2015;373:35–47.",{"doi":1341},{"id":1337,"text":2686,"url":1339,"identifiers":2687},"Scheinberg P, Nunez O, Wu C, Young NS. Treatment of severe aplastic anaemia with combined immunosuppression: anti-thymocyte globulin, ciclosporin and mycophenolate mofetil. Br J Haematol. 2006;133:606–11.",{"doi":1341},{"id":2689,"text":2690,"url":2691,"identifiers":2692},"960f8db5-a2fa-492b-a272-21bf42bd8866","Frickhofen N, Heimpel H, Kaltwasser JP, Schrezenmeier H. Antithymocyte globulin with or without cyclosporin a: 11-year follow-up of a randomized trial comparing treatments of aplastic anemia. Blood. 2003;101:1236–42.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006497120573813",{"doi":2693},"10.1182\u002Fblood-2002-04-1134",{"id":1337,"text":2695,"url":1339,"identifiers":2696},"Jalaeikhoo H, Khajeh-Mehrizi A. Immunosuppressive therapy in patients with aplastic anemia: a single-center retrospective study. PLoS One. 2015;10:e0126925.",{"doi":1341},{"id":1337,"text":2698,"url":1339,"identifiers":2699},"Sanders JE, Hawley J, Levy W, Gooley T, Buckner CD, Deeg HJ, Doney K, Storb R, Sullivan K, Witherspoon R, et al. Pregnancies following high-dose cyclophosphamide with or without high-dose busulfan or total-body irradiation and bone marrow transplantation. Blood. 1996;87:3045–52.",{"doi":1341},{"id":1337,"text":2701,"url":1339,"identifiers":2702},"Gelber RD, Cole BF, Goldhirsch A, Bonadonna G, Howell A, McArdle CS, Mouridsen HT, Rubens RD, Welvaart K. Adjuvant chemotherapy for premenopausal breast cancer: a meta-analysis using quality-adjusted survival. Cancer J Sci Am. 1995;1:114–21.",{"doi":1341},{"id":1337,"text":2704,"url":1339,"identifiers":2705},"Wells GA, Shea B, Connell D, Peterson J, Welch V, Losos M, Tugwell P. The Newcastle-Ottawa Scale (NOS) for assessing the quality of nonrandomised studies in meta-analyses. Available from: http:\u002F\u002Fwww.ohri.ca\u002Fprograms\u002Fclinical_epidemiology\u002Foxford.asp.",{"doi":1341},{"id":2707,"text":2708,"url":2709,"identifiers":2710},"0f601596-693e-43f5-8f41-21e12eb11fd1","Tierney JF, Stewart LA, Ghersi D, Burdett S, Sydes MR. Practical methods for incorporating summary time-to-event data into meta-analysis. Trials. 2007;8:16.","https:\u002F\u002Ftrialsjournal.biomedcentral.com\u002Farticles\u002F10.1186\u002F1745-6215-8-16",{"doi":2711},"10.1186\u002F1745-6215-8-16"]