Expression profile analysis reveals hub genes that are associated with immune system dysregulation in primary myelofibrosis

References

• Tefferi A. Primary myelofibrosis: 2019 update on diagnosis, risk-stratification and management. Am J Hematol. 2018;93:1551–1560.
   PubMed Web of Science ®Google Scholar
• Mesa RA, Silverstein MN, Jacobsen SJ, et al. Population-based incidence and survival figures in essential thrombocythemia and agnogenic myeloid metaplasia: an olmsted county study, 1976–1995. Am J Hematol. 1999;61:10–15.
   PubMed Web of Science ®Google Scholar
• Vannucchi AM, Lasho TL, Guglielmelli P, et al. Mutations and prognosis in primary myelofibrosis. Leukemia. 2013;27:1861–1869.
   PubMed Web of Science ®Google Scholar
• Oon SF, Singh D, Tan TH, et al. Primary myelofibrosis: spectrum of imaging features and disease-related complications. Insights Imaging. 2019;10:71.
   PubMed Web of Science ®Google Scholar
• Lewis CM, Pegrum GD. Immune complexes in myeloproliferative disorders. Lancet. 1977;2:1151–1153.
   PubMed Web of Science ®Google Scholar
• Cervantes F, Dupriez B, Pereira A, et al. New prognostic scoring system for primary myelofibrosis based on a study of the international working group for myelofibrosis research and treatment. Blood. 2009;113:2895–2901.
   PubMed Web of Science ®Google Scholar
• Passamonti F, Cervantes F, Vannucchi AM, et al. A dynamic prognostic model to predict survival in primary myelofibrosis: A study by the IWG-MRT (international working group for myeloproliferative neoplasms research and treatment). Blood. 2010;115:1703–1708.
   PubMed Web of Science ®Google Scholar
• Wang JC, Sindhu H, Chen C, et al. Immune derangements in patients with myelofibrosis: the role of Treg, Th17, and sIL2Rα. PLoS ONE. 2015;10:e0116723.
   PubMed Web of Science ®Google Scholar
• Tefferi A, Vaidya R, Caramazza D, et al. Circulating interleukin (IL)-8, IL-2R, IL-12, and IL-15 levels are independently prognostic in primary myelofibrosis: a comprehensive cytokine profiling study. J Clin Oncol. 2011;29:1356–1363.
   PubMed Web of Science ®Google Scholar
• Vaidya R, Gangat N, Jimma T, et al. Plasma cytokines in polycythemia vera: phenotypic correlates, prognostic relevance, and com-parison with myelofibrosis. Am J Hematol. 2012;87:1003–1005.
   PubMed Web of Science ®Google Scholar
• Massa M, Campanelli R, Fois G, et al. Reduced frequency of circulating CD4+CD25brightCD127low FOXP3+ regulatory T cells in primary myelofibrosis. Blood. 2016;128:1660–1662.
   PubMed Web of Science ®Google Scholar
• Keohane C, Kordasti S, Seidl T, et al. JAK inhibition induces silencing of T helper cytokine secretion and a profound reduction in T regulatory cells. Br J Haematol. 2015;171:60–73.
   PubMed Web of Science ®Google Scholar
• Wilkins BS, Radia D, Woodley C, et al. Resolution of bone marrow fibrosis in a patient receiving JAK1/JAK2 inhibitor treatment with ruxolitinib. Haematologica. 2013;98:1872–1876.
   PubMed Web of Science ®Google Scholar
• Zhu YQ, Wu LY. Identification of latent core genes and pathways associated with myelodysplastic syndromes based on integrated bioinformatics analysis. Hematology. 2020;25(1):299–308.
   PubMed Web of Science ®Google Scholar
• Aran D, Hu ZC, Butte AJ. Xcell: digitally portraying the tissue cellular heterogeneity landscape. Genome Biol. 2017;18:220.
   PubMed Web of Science ®Google Scholar
• Fan YN, Xia JG. Mirnet-functional analysis and visual exploration of mirna-target interactions in a network context. Methods Mol Biol. 2018;1819:215–233.
   PubMedGoogle Scholar
• Masarova L, Verstovsek S, Kantarjian H, et al. Immunotherapy based approaches in myelofibrosis. Expert Rev Hematol. 2017;10:903–914.
   PubMed Web of Science ®Google Scholar
• Jia MF, Zhang H, Wang LN, et al. Identification of mast cells as a candidatesignificant target of immunotherapy for acute myeloid leukemia. Hematology. 2021;26(1):284–294.
   PubMed Web of Science ®Google Scholar
• Wang JW, Geiger H, Rudolph KL. Immunoaging induced by hematopoietic stem cell aging. Curr Opin Immunol. 2011;23:532–536.
   PubMed Web of Science ®Google Scholar
• Spivak JL. Myeloproliferative neoplasms. N Engl J Med. 2017;376:2168–2181.
   PubMed Web of Science ®Google Scholar
• Dobryszycka W. Biological functions of haptoglobin–new pieces to an old puzzle. Eur J Clin Chem Clin Biochem. 1997;35:647–654.
   PubMedGoogle Scholar
• Langlois MR, Delanghe JR. Biological and clinical significance of haptoglobin polymorphism in human. Clin Chem. 1996;42:1589–1600.
   PubMed Web of Science ®Google Scholar
• Masi AD, Simone GD, Ciaccio C, et al. Haptoglobin: from hemoglobin scavenging to human health. Mol Aspects Med. 2020;73:100851.
   PubMed Web of Science ®Google Scholar
• Kolarova H, Klinke A, Kremserova S, et al. Myeloperoxidase induces the priming of platelets. Free Radic Biol Med. 2013;61:357–369.
   PubMed Web of Science ®Google Scholar
• Klinke A, Nussbaum C, Kubala L, et al. Myeloperoxidase attracts neutrophils by physical forces. Blood. 2011;117:1350–1358.
   PubMed Web of Science ®Google Scholar
• Lau D, Mollnau H, Eiserich JP, et al. Myeloperoxidase mediates neutrophil activation by association with CD11b/CD18 integrins. Proc Natl Acad Sci USA. 2005;102:431–436.
   PubMed Web of Science ®Google Scholar
• Gorudko IV, Sokolov AV, Shamova EV, et al. Binding of human myeloperoxidase to red blood cells: molecular targets and biophysical consequences at the plasma membrane level. Arch Biochem Biophys. 2016;591:87–97.
   PubMed Web of Science ®Google Scholar
• Benson TW, Weintraub NL, Kim HW, et al. A single high-fat meal provokes pathological erythrocyte remodeling and increases myeloperoxidase levels: implications for acute coronary syndrome. Lab Invest. 2018;98:1300–1310.
   PubMed Web of Science ®Google Scholar
• Panasenko OM, Gorudko IV, Sokolov AV. Hypochlorous acid as a precursor of free radicals in living systems. Biochemistry. 2013;78:1466–1489.
   PubMed Web of Science ®Google Scholar
• Yap YW, Whiteman M, Cheung NS. Chlorinative stress: an under appreciated mediator of neurodegeneration? Cell Signal. 2007;19:219–228.
   PubMed Web of Science ®Google Scholar
• Vorchheimer DA, Becker R. Platelets in atherothrombosis. Mayo Clin Proc. 2006;81:59–68.
   PubMed Web of Science ®Google Scholar
• Gorudko IV, Sokolov AV, Shamova EV, et al. Myeloperoxidase modulates human platelet aggregation via actin cytoskeleton reorganization and store-operated calcium entry. Biol Open. 2013;2:916–923.
   PubMed Web of Science ®Google Scholar
• Mondal S, Adhikari N, Banerjee S, et al. Matrix metalloproteinase-9 (MMP-9) and its inhibitors in cancer: A minireview. Eur J Med Chem. 2020;194:112260.
   PubMed Web of Science ®Google Scholar
• Bradley LM, Douglass MF, Chatterjee D, et al. Matrix metalloprotease 9 mediates neutrophil migration into the airways in response to influenza virus-induced toll-like receptor signaling. PLoS Pathog. 2012;8:e1002641.
   PubMed Web of Science ®Google Scholar
• Takahashi K. Microbiological, pathological, inflammatory, immunological and molecular biological aspects of periradicular disease. Int Endod J. 1998;31:311–325.
   PubMed Web of Science ®Google Scholar
• Reif S, Somech R, Brazovski E, et al. Matrix metalloproteinases 2 and 9 are markers of inflammation but not of the degree of fibrosis in chronic hepatitis C. Digestion. 2005;71:124–130.
   PubMed Web of Science ®Google Scholar
• Esparza J, Kruse M, Lee J, et al. MMP-2 null mice exhibit an early onset and severe experimental autoimmune encephalomyelitis due to an increase in MMP-9 expression and activity. FASEB J. 2004;18:1682–1691.
   PubMed Web of Science ®Google Scholar
• Halade GV, Jin YF, Lindsey ML. Matrix metalloproteinase (MMP)-9: a proximal biomarker for cardiac remodeling and a distal biomarker for inflammation. Pharmacol Therap. 2013;139:32–40.
   PubMed Web of Science ®Google Scholar
• Xu MJ, Bruno E, Chao J, et al. Constitutive mobilization of CD34+ cells into the peripheral blood in idiopathic myelofibrosis may be due to the action of a number of proteases. Blood. 2005;105:4508–4515.
   PubMed Web of Science ®Google Scholar
• Jensen MK, Holten-Andersen MN, Riisbro R, et al. Elevated plasma levels of TIMP-1 correlate with plasma suPAR/uPA in patients with chronic myeloproliferative disorders. Eur J Haematol. 2003;71:377–384.
   PubMed Web of Science ®Google Scholar
• Yabluchanskiy A, Ma YG, Iyer RP, et al. Matrix metalloproteinase-9: many shades of function in cardiovascular disease. Physiology (Bethesda). 2013;28:391–403.
   PubMed Web of Science ®Google Scholar
• Youn MY, Huang HG, Chen C, et al. MMP9 inhibition increases erythropoiesis in RPS14-deficient del(5q) MDS models through suppression of TGF-β pathways. Blood Adv. 2019;3:2751–2763.
   PubMed Web of Science ®Google Scholar
• Karacay B, Chang LS. Induction of erythrocyte protein 4.2 gene expression during differentiation of murine erythroleukemia cells. Genomics. 1999;59:6–17.
   PubMed Web of Science ®Google Scholar
• Rocca DB, Etchebest C, Guizouarn H. Structural model of the anion exchanger 1 (SLC4A1) and identification of transmembrane segments forming the transport site. J Biol Chem. 2013;288:26372–26384.
   PubMed Web of Science ®Google Scholar
• Reithmeier RA, Casey JR, Kalli AC, et al. Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context. Biochim Biophys Acta. 2016;1858:1507–1532.
   PubMed Web of Science ®Google Scholar
• McCranor BJ, Kim MJ, Cruz NM, et al. Interleukin-6 directly impairs the erythroid development of human TF-1 erythroleukemic cells. Blood Cells Mol Dis. 2014;52:126–133.
   PubMed Web of Science ®Google Scholar
• Kawamoto S, Kamesaki T, Masutani R, et al. Ectopic expression of band 3 anion transport protein in colorectal cancer revealed in an autoimmune hemolytic anemia patient. Hum Pathol. 2019;83:193–198.
   PubMed Web of Science ®Google Scholar
• Kitao A, Kawamoto S, Kurata K, et al. Band 3 ectopic expression in colorectal cancer induces an increase in erythrocyte membrane-bound IgG and may cause immune-related anemia. Int J Hematol. 2020;111:657–666.
   PubMed Web of Science ®Google Scholar
• AlFadhli S, Ghanem AA, Nizam R. Genome-wide differential expression reveals candidate genes involved in the pathogenesis of lupus and lupus nephritis. Int J Rheum Dis. 2016;19:55–64.
   PubMed Web of Science ®Google Scholar
• Kafina MD, Paw BH. Intracellular iron and hemetrafficking and metabolism in developing erythroblasts. Metallomics. 2017;9:1193–1203.
   PubMed Web of Science ®Google Scholar
• Rio S, Gastou M, Karboul N, et al. Regulation of globin-heme balance in diamond- blackfan anemia by HSP70 / GATA1. Blood. 2019;133:1358–1370.
   PubMed Web of Science ®Google Scholar
• La P, Oved JH, Ghiaccio V, et al. Mitochondria biogenesis modulates iron-sulfur cluster synthesis to increase cellular iron uptake. DNA Cell Biol. 2020;39:756–765.
   PubMed Web of Science ®Google Scholar
• Pellagatti A, Cazzola M, Giagounidis AAN, et al. Gene expression profiles of CD34+ cells in myelodysplastic syndromes: involvement of interferon-stimulated genes and correlation to FAB subtype and karyotype. Blood. 2016;108:337–345.
   Google Scholar
• Saha D, Patgaonkar M, Shroff A, et al. Hemoglobin expression in nonerythroid cells: novel or ubiquitous? Int J Inflam. 2014;2014:803237.
   PubMedGoogle Scholar
• Liu L, Zeng M, Stamler JS. Hemoglobin induction in mouse macrophages. Proc Natl Acad Sci USA. 1999;96:6643–6647.
   PubMed Web of Science ®Google Scholar
• Dutra FF, Bozza MT. Heme on innate immunity and inflammation. Front Pharm. 2014;5:115.
   PubMed Web of Science ®Google Scholar
• Wherry EJ. T cell exhaustion. Nat Immunol. 2011;12:492–499.
   PubMed Web of Science ®Google Scholar
• Baseler MW, Burrell R. Purification of haptoglobin and its effects on lymphocyte and alveolar macrophage responses. Inflammation. 1983;7:387–400.
   PubMed Web of Science ®Google Scholar
• Xie Y, Li Y, Zhang Q, et al. Haptoglobin is a natural regulator of Langerhans cell function in the skin. J Dermatol Sci. 2000;24:25–37.
   PubMed Web of Science ®Google Scholar
• Arredouani M, Matthijs P, Hoeyveld EV, et al. Haptoglobin directly affects T cells and suppresses T helper cell type 2 cytokine release. Immunology. 2003;108:144–151.
   PubMed Web of Science ®Google Scholar
• Odobasic D, Kitching AR, Semple TJ, et al. Endogenous myeloperoxidase promotes neutrophil-mediated renal injury, but attenuates T cell immunity inducing crescentic glomerulonephritis. J Am Soc Nephrol. 2007;18:760–770.
   PubMed Web of Science ®Google Scholar
• Brennan M, Gaur A, Pahuja A, et al. Mice lacking myeloperoxidase are more susceptible to experimental autoimmune encephalomyelitis. J Neuroimmunol. 2001;112:97–105.
   PubMed Web of Science ®Google Scholar
• Odobasic D, Kitching AR, Yang Y, et al. Neutrophil myeloperoxidase regulates T-cell-driven tissue inflammation in mice by inhibiting dendritic cell function. Blood. 2013;121:4195–4204.
   PubMed Web of Science ®Google Scholar
• Heissig B, Hattori K, Dias S, et al. Recruitment of stem and progenitor cells from the bone marrow niche requires MMP-9 mediated release of kit-ligand. Cell. 2002;109:625–637.
   PubMed Web of Science ®Google Scholar
• Qi X, Jiang HJ, Liu P, et al. Increased myeloid-derived suppressor cells in patients with myelodysplastic syndromes suppress CD8+ T lymphocyte function through the STAT3-ARG1 pathway. Leuk Lymphoma. 2020;26:1–6.
   Google Scholar
• Lu SL, Yadav A K, Qiao XH. Identification of potential miRNA-mRNA interaction network in bone marrow T cells of acquired aplastic anemia. Hematology. 2020;25:168–175.
   PubMed Web of Science ®Google Scholar
• Kim NH, Kim HS, Kim NG, et al. P53 and MicroRNA-34 are suppressors of canonical Wnt signaling. Sci Signal. 2011;4:ra71.
   PubMed Web of Science ®Google Scholar