Литература/References
1. Hashimoto T., Shibasaki F. Hypoxia-Inducible Factor as an angiogenic master switch. Front. Pediatr. 2015; 3: 33.
URL: https://www.ncbi.nlm.nih.gov/pubmed/25964891
doi: 10.3389/fped.2015.00033
2. Ratcliffe P., Koivunen P., Myllyharju J., Ragoussis J., et al. Update on hypoxia-inducible factors and hydroxylases in oxygen regulatory pathways: from physiology to therapeutics. Hypoxia. 2017; 5: 11-20.
URL: https://www.ncbi.nlm.nih.gov/pubmed/28352643
doi: 10.2147/HP.S127042
3. Chen R., Lai U.H., Zhu L., Singh A., et al. Reactive oxygen species formation in the brain at different oxygen levels: the role of hypoxia inducible factors. Front. Cell Dev. Biol. 2018; 6: 132.
URL: https://www.ncbi.nlm.nih.gov/pubmed/30364203
doi: 10.3389/fcell.2018.00132
4. Koyasu S., Kobayashi M., Goto Y., Hiraoka M., et al. Regulatory mechanisms of hypoxia-inducible factor 1 activity: two decades of knowledge. Cancer Sci. 2018; 109 (3): 560-71.
URL: https://www.ncbi.nlm.nih.gov/pubmed/29285833
doi: 10.1111/cas.13483
5. Watts E.R., Walmsley S.R. Inflammation and hypoxia: HIF and PHD isoform selectivity. Trends Mol. Med. 2019; 25 (1): 33-46.
URL: https://www.ncbi.nlm.nih.gov/pubmed/30442494
doi: 10.1016/j.molmed.2018.10.006
6. Semenza G.L., Wang G.L. A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol. Cell. Biol. 1992; 12 (12): 5447-54.
7. Wang G.L., Jiang B.H., Rue E.A., Semenza G.L. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl Acad. Sci. USA. 1995; 92 (12): 5510-4.
8. Fratantonio D., Cimino F., Speciale A., Virgili F. Need (more than) two to Tango: Multiple tools to adapt to changes in oxygen availability. Biofactors. 2018; 44 (3): 207-18.
URL: https://digitalcommons.unl.edu/cgi/viewcontent.cgi?referer=https://www.google.com/&httpsredir=1&article=1159&context=nutritionfacpub
doi: 10.1002/biof.1419
9. Stothers C.L., Luan L., Fensterheim B.A., Bohannon J.K. Hypoxia-inducible factor-1α regulation of myeloid cells. J. Mol. Med. 2018; 96 (12): 1293-306
URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6292431/
doi: 10.1007/s00109-018-1710-1
10. Ivan M., Kondo K., Yang H., Kim W., et al. HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science. 2001; 292 (5516): 464-8.
11. Jaakkola P., Mole D.R., Tian Y.M., Wilson M.I., et al. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science. 2001; 292 (5516): 468-72.
12. Mahon P.C., Hirota K., Semenza G.L. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 2001; 15 (20): 2675-86.
13. Epstein A.C., Gleadle J.M., McNeill L.A., Hewitson K.S., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001; 107 (1): 43-54.
14. Frede S., Stockmann C., Freitag P., Fandrey J. Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kB. Biochem. J. 2006; 396 (3): 517-27.
15. Schofield C.J., Zhang, Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 1999; 9 (6): 722-31.
16. Schodel J., Oikonomopoulos S., Ragoussis J., Pugh C.W., et al. High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood. 2011; 117 (23): e207-17.
URL: https://www.ncbi.nlm.nih.gov/pubmed/21447827
doi: 10.1182/blood-2010-10-314427
17. Semenza G.L. Hypoxia-inducible factors in physiology and medicine. Cell. 2012; 148 (3): 399-408.
URL: https://www.ncbi.nlm.nih.gov/pubmed/22304911
doi: 10.1016/j.cell.2012.01.021
18. Kletsas D., Pratsinis H., Mariatos G., Zacharatos P., et al. The proinflammatory phenotype of senescent cells: the p53-mediated ICAM-1 expression. Ann. N. Y. Acad. Sci. 2004; 1019: 330-2.
19. Hayden M.S., Ghosh S. NF-kB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 2012; 26 (3): 203-34.
20. Liu T., Zhang L., Joo D., Sun S.C. NF-kB signaling in inflammation. Signal Transduct. Target. Ther. 2017; 2: e17023.
URL: https://www.ncbi.nlm.nih.gov/pubmed/29158945
doi: 10.1038/sigtrans.2017.23
21. Mitchell S., Vargas J., Hoffmann A. Signaling via the NFκB system. Wiley Interdiscip. Rev. Syst. Biol. Med. 2016; 8 (3): 227-41.
URL: https://www.ncbi.nlm.nih.gov/pubmed/26990581
doi: 10.1002/wsbm.1331
22. Ghosh S., May M.J., Kopp E.B. NF-κB and Rel proteins: evolutionary conserved mediators of immune responses. Annu. Rev. Immunol. 1998; 16: 225-60.
23. Karin M. Nuclear factor-κB in cancer development and progression. Nature. 2006; 441 (7092): 431-6.
24. Sakai J., Cammarota E., Wright J.A., Cicuta P., et al. Lipopolysaccharide-induced NF-κB nuclear translocation is primarily dependent on MyD88, but TNFα expression requires TRIF and MyD88. Sci. Rep. 2017; 7 (1): 1428.
URL: https://www.ncbi.nlm.nih.gov/pubmed/28469251
doi: 10.1038/s41598-017-01600-y
25. Hirota K. Involvement of hypoxia-inducible factors in the dysregulation of oxygen homeostasis in sepsis. Cardiovasc. Hematol. Disord. Drug Targets. 2015; 15 (1): 29-40.
26. Kiers H.D., Scheffer G.-J., van der Hoeven J.G., Eltzschig H.K., et al. Immunologic Consequences of hypoxia during critical illness. Anesthesiology. 2016; 125 (1): 237-49.
URL: https://www.ncbi.nlm.nih.gov/pubmed/27183167
doi: 10.1097/ALN.0000000000001163
27. Devraj G., Beerlage C., Brune B., Kempf V.A. Hypoxia and HIF-1 activation in bacterial infections. Microbes Infect. 2017; 19 (3): 144-56.
URL: https://www.ncbi.nlm.nih.gov/pubmed/27903434
doi: 10.1016/j.micinf.2016.11.003
28. Eltzschig H.K., Carmeliet P. Hypoxia and inflammation. N. Engl. J. Med. 2011; 364 (7): 656-65.
29. van der Flier M., Stockhammer G., Vonk G.J., Nikkels P.G., et al. Vascular endothelial growth factor in bacterial meningitis: detection in cerebrospinal fluid and localization in postmortem brain. J. Infect. Dis. 2001; 183 (1): 149-53.
URL: https://www.ncbi.nlm.nih.gov/pubmed/11106541
doi: 10.1086/317643
30. Riess T., Andersson S.G.E., Lupas A., Schaller M., et al. Bartonella adhesin a mediates a proangiogenic host cell response. J. Exp. Med. 2004; 200 (10): 1267-78.
URL: https://rupress.org/jem/article/200/10/1267/52512/Bartonella-Adhesin-A-Mediates-a-Proangiogenic-Host
doi: 10.1084/jem.20040500
31. Kempf V.A., Lebiedziejewski M., Alitalo K., Walzlein J.H., et al. Activation of hypoxia-inducible factor-1 in bacillary angiomatosis: evidence for a role of hypoxia-inducible factor-1 in bacterial infections. Circulation. 2005; 111 (8): 1054-62.
URL: https://www.ncbi.nlm.nih.gov/pubmed/15723970
doi: 10.1161/01.CIR.0000155608.07691.B7
32. Charpentier T., Hammami A., Stager S. Hypoxia inducible factor 1α: a critical factor for the immune response to pathogens and Leishmania. Cell. Immunol. 2016; 309: 42-9.
URL: https://www.sciencedirect.com/science/article/abs/pii/S0008874916300478?via%3Dihub
doi: 10.1016/j.cellimm.2016.06.002
33. Schaffer K., Taylor C.T. The impact of hypoxia on bacterial infection. FEBS J. 2015; 282 (12): 2260-6.
34. Rius J., Guma M., Schachtrup C., Akassoglou K., et al. NF-kappaB links innate immunity to the hypoxic response through transcriptional regulation of HIF-1alpha. Nature. 2008; 453 (7196): 807-11.
URL: https://www.ncbi.nlm.nih.gov/pubmed/18432192
doi: 10.1038/nature06905
35. van Uden P., Kenneth N.S., Rocha S. Regulation of hypoxia-inducible factor-1alpha by NF-kappaB. Biochem. J. 2008; 412 (3): 477-84.
URL: https://www.ncbi.nlm.nih.gov/pubmed/18393939
doi: 10.1042/BJ20080476
36. van Uden P., Kenneth N.S., Webster R., Muller H.A., et al. Evolutionary conserved regulation of HIF-1beta by NF-kappaB. PLoS Genet. 2011; 7 (1): e1001285.
URL: https://www.ncbi.nlm.nih.gov/pubmed/21298084
doi: 10.1371/journal.pgen.1001285
37. Bonello S., Zahringer C., BelAiba R.S., Djordjevic T., et al. Reactive oxygen species activate the HIF-1alpha promoter via a functional NFkappaB site. Arterioscler. Thromb. Vasc. Biol. 2007; 27 (4): 755-61.
38. BelAiba R.S., Bonello S., Zahringer C., Schmidt S., et al. Hypoxia up-regulates hypoxia-inducible factor-1alpha transcription by involving phosphatidylinositol 3-kinase and nuclear factor kappaB in pulmonary artery smooth muscle cells. Mol. Biol. Cell. 2007; 18 (12): 4691-7.
URL: https://www.ncbi.nlm.nih.gov/pubmed/17898080
doi: 10.1091/mbc.e07-04-0391
39. Nishi K., Oda T., Takabuchi S., Oda S., et al. LPS induces hypoxia-inducible factor 1 activation in macrophage-differentiated cells in a reactive oxygen species-dependent manner. Antioxid. Redox Signal. 2008; 10 (5): 983-95.
URL: https://www.ncbi.nlm.nih.gov/pubmed/18199003
doi: 10.1089/ars.2007.1825
40. Bandarra D., Rocha S. HIF-1α a novel piece in the NF-κB puzzle. Inflamm Cell Signal. 2015; 2: e792.
URL: https://www.researchgate.net/publication/277329952_HIF-1a_a_novel_piece_in_the_NF-kB_puzzle
doi: 10.14800/ics.792
41. Halligan D.N., Murphy S.J.E., Taylor C.T. The hypoxia-inducible factor (HIF) couples immunity with metabolism. Semin. Immunol. 2016; 28 (5): 469-77.
42. Taylor C.T, Colgan S.P. Regulation of immunity and inflammation by hypoxia in immunological niches. Nat. Rev. Immunol. 2017; 17 (12): 774-85.
URL: https://www.ncbi.nlm.nih.gov/pubmed/28972206
doi: 10.1038/nri.2017.103
43. Hellwig-Burgel T., Rutkowski K., Metzen E., Fandrey J., et al. Interleukin-1beta and tumor necrosis factor-alpha stimulate DNA binding of hypoxia-inducible factor-1. Blood. 1999; 94 (5): 1561-7.
44. Tannahill G.M., Curtis A.M., Adamik J., Palsson-McDermott E.M., et al. Succinate is an inflammatory signal that induces IL-1β through HIF-1α. Nature. 2013; 496 (7444): 238-42.
45. Dehne N., Brune B. HIF-1 in the inflammatory microenvironment. Exp. Cell Res. 2009; 315 (11): 1791-7.
46. Jantsch J., Wiese M., Schodel J., Castiglione K., et al. Toll-like receptor activation and hypoxia use distinct signaling pathways to stabilize hypoxia-inducible factor 1α (HIF1A) and result in differential HIF1A-dependent gene expression. J. Leukoc. Biol. 2011; 90 (3): 551-62.
47. Oliver K.M., Taylor C.T., Cummins E.P. Hypoxia. Regulation of NFkappaB signalling during inflammation: the role of hydroxylases. Arthritis Res. Ther. 2009; 11 (1): 215.
URL: https://www.ncbi.nlm.nih.gov/pubmed/19291263
doi: 10.1186/ar2575
48. Kruger B., Krick S., Dhillon N., Lerner S.M., et al. Donor Toll-like receptor 4 contributes to ischemia and reperfusion injury following human kidney transplantation. Proc. Natl Acad. Sci. USA. 2009; 106 (9): 3390-5.
49. Ferguson N.D., Fan E., Camporota L., Antonelli M., et al. The Berlin definition of ARDS: an expanded rationale, justification, and supplementary material. Intensive Care Med. 2012; 38 (10): 1573-82.
50. Suganami T., Ogawa Y. Adipose tissue macrophages: their role in adipose tissue remodeling. J. Leukoc. Biol. 2010; 88 (1): 33-9.
51. Wang J.S., Liu H.C. Systemic hypoxia enhances bactericidal activities of human polymorphonuclear leuocytes. Clin. Sci. (Lond.). 2009; 116 (11): 805-17.
URL: https://www.ncbi.nlm.nih.gov/pubmed/19053944
doi: 10.1042/CS20080224
52. Fritzenwanger M., Jung C., Goebel B., Lauten A., et al. Impact of short-term systemic hypoxia on phagocytosis, cytokine production, and transcription factor activation in peripheral blood cells. Mediators Inflamm. 2011; 2011: 429501.
URL: https://www.ncbi.nlm.nih.gov/pubmed/21765619
doi: 10.1155/2011/429501
53. Richard N.A., Sahota I.S., Widmer N., Ferguson S., et al. Acute mountain sickness, chemosensitivity and cardio-respiratory responses in humans exposed to hypobaric and normobaric hypoxia. J. Appl. Physiol. 2014; 116 (7): 945-52.
54. Grocott M., Montgomery H., Vercueil A. High-altitude physiology and pathophysiology: implications and relevance for intensive care medicine. Crit. Care. 2007; 11 (1): 203.
55. Hartmann G., Tschop M., Fischer R., Bidlingmaier C., et al. High altitude increases circulating interleukin-6, interleukin-1 receptor antagonist and C-reactive protein. Cytokine. 2000; 12 (3): 246-52.
56. Cummins E.P., Berra E., Comerford K.M., Ginouves A., et al. Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity. Proc. Natl Acad. Sci. USA. 2006; 103 (48): 18 154-9.
57. Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S., et al. Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH). Proc. Natl Acad. Sci. USA. 2006; 103: 14 767-72.
58. Dzhalilova D.Sh., Kosyreva A.M., Diatroptov M.E., Ponomarenko E.A., et al. Dependence of the severity of the systemic inflammatory response on resistance to hypoxia in male Wistar rats. J Inflamm Res. 2019; 12: 73-86.
59. Walmsley S.R., Print C., Farahi N., Peyssonnaux C., et al. Hypoxia-induced neutrophil survival is mediated by HIF-1alphadependent NF-kappaB activity. J. Exp. Med. 2005; 201 (1): 105-15.
60. Peyssonnaux C., Datta V., Cramer T., Doedens A., et al. HIF-1alpha expression regulates the bactericidal capacity of phagocytes. J. Clin. Invest. 2005; 115: 1806-15.
61. Ben-Shoshan J., Afek A., Maysel-Auslender S., Barzelay A., et al. HIF-1alpha overexpression and experimental murine atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 2009; 29 (5): 665-70.
URL: https://www.ncbi.nlm.nih.gov/pubmed/19251587
doi: 10.1161/ATVBAHA.108.183319
62. Clambey E.T., McNamee E.N., Westrich J.A., Glover L.E., et al. Hypoxia-inducible factor-1 alpha-dependent induction of FoxP3 drives regulatory T-cell abundance and function during inflammatory hypoxia of the mucosa. Proc. Natl Acad. Sci. USA. 2012; 109 (41): E2784-93.
URL: https://www.ncbi.nlm.nih.gov/pubmed/22988108
doi: 10.1073/pnas.1202366109
63. Campbell E.L., Bruyninckx W.J., Kelly C.J., Glover L.E., et al. et al. Transmigrating neutrophils shape the mucosal microenvironment through localized oxygen depletion to influence resolution of inflammation. Immunity. 2014; 40 (1): 66-77.
URL: https://www.ncbi.nlm.nih.gov/pubmed/24412613
doi: 10.1016/j.immuni.2013.11.020
64. Barbi J., Pardoll D., Pan F. Metabolic control of the Treg/Th17 axis. Immunol. Rev. 2013; 252 (1): 52-77.
URL: https://www.ncbi.nlm.nih.gov/pubmed/23405895
doi: 10.1111/imr.12029
65. Sadiku P., Walmsley S.R. Hypoxia and the regulation of myeloid cell metabolic imprinting: consequences for the inflammatory response. EMBO Rep. 2019; 20 (5): e47388.
URL: https://www.ncbi.nlm.nih.gov/pubmed/30872317
doi: 10.15252/embr.201847388
66. Thompson A.A., Binham J., Plant T., Whyte M.K., et al. Hypoxia, the HIF pathway and neutrophilic inflammatory responses. Biol. Chem. 2013; 394 (4): 471-7.
67. Krzywinska E., Stockmann C. Hypoxia, metabolism and immune cell function. Biomedicines. 2018; 6 (2): E56.
URL: https://www.ncbi.nlm.nih.gov/pubmed/29762526
doi: 10.3390/biomedicines6020056
68. Kojima H., Jones B.T., Chen J., Cascalho M., et al. Hypoxia-inducible factor 1alpha-deficient chimeric mice as a model to study abnormal B lymphocyte development and autoimmunity. Methods Enzymol. 2004; 381: 218-29.
69. Hartmann H., Eltzschig H.K., Wurz H., Hantke K., et al. Hypoxia-independent activation of HIF-1 by Enterobacteriaceae and their siderophores. Gastroenterology. 2008; 134 (3): 756-67.
URL: https://www.ncbi.nlm.nih.gov/pubmed/18325389
doi: 10.1053/j.gastro.2007.12.008
70. Karhausen J., Furuta G.T., Tomaszewski J.E., Johnson R.S., et al. Epithelial hypoxia-inducible factor-1 is protective in murine experimental colitis. J. Clin. Invest. 2004; 114 (8): 1098-106.
71. Manresa M.C., Taylor C.T. Hypoxia inducible factor (HIF) hydroxylases as regulators of intestinal epithelial barrier function. Cell. Mol. Gastroenterol. Hepatol. 2017; 3: 303-15.
72. Sun M., He C., Wu W., Zhou G., et al. Hypoxia inducible factor-1α-induced interleukin-33 expression in intestinal epithelia contributesto mucosal homeostasis in inflammatory bowel disease. Clin. Exp. Immunol. 2017; 187 (3): 428-40.
URL: https://www.ncbi.nlm.nih.gov/pubmed/27921309
doi: 10.1111/cei.12896
73. Robinson A., Keely S., Karhausen J., Gerich M.E., et al. Mucosal protection by hypoxia-inducible factor prolyl hydroxylase inhibition. Gastroenterology. 2008; 134: 145-55.
74. Triner D., Shah Y.M. Hypoxia-inducible factors: a central link between inflammation and cancer. J. Clin. Invest. 2016; 126 (10): 3689-98.
URL: https://www.ncbi.nlm.nih.gov/pubmed/27525434
doi: 10.1172/JCI84430
75. Hirota S.A., Fines K., Ng J., Traboulsi D., et al. Hypoxia-inducible factor signaling provides protection in Clostridium difficile-induced intestinal injury. Gastroenterology. 2010; 139 (1): 259-69.e3.
URL: https://www.ncbi.nlm.nih.gov/pubmed/20347817
doi: 10.1053/j.gastro.2010.03.045
76. Peyssonnaux C., Boutin A.T., Zinkernagel A.S., Datta V., et al. Critical role of HIF-1alpha in keratinocyte defense against bacterial infection. J. Invest. Dermatol. 2008; 128 (8): 1964-8.
77. Schaible B., McClean S., Selfridge A., Broquet A., et al. Hypoxia modulates infection of epithelial cells by Pseudomonas aeruginosa. PLoS One. 2013; 8 (2): e56491.
URL: https://www.ncbi.nlm.nih.gov/pubmed/23418576
doi: 10.1371/journal.pone.0056491
78. Peyssonnaux C., Cejudo-Martin P., Doedens A., Zinkernagel A.S., et al. Cutting edge: essential role of hypoxia inducible factor-1alpha in development of lipopolysaccharide-induced sepsis. J. Immunol. 2007; 178 (12): 7516-9.
79. Werth N., Beerlage C., Rosenberger C., Yazdi A.S., et al. Activation of hypoxia inducible factor 1 is a general phenomenon in infections with human pathogens. PLoS One. 2010; 5 (7): e11576.
URL: https://www.ncbi.nlm.nih.gov/pubmed/20644645
doi: 10.1371/journal.pone.0011576
80. Mahabeleshwar G.H., Qureshi M.A., Takami Y., Sharma N., et al. A myeloid hypoxia- inducible factor 1a-Kruppel-like factor 2 pathway regulates gram-positive endotoxin-mediated sepsis. J. Biol. Chem. 2012; 287: 1448-57.
81. Ono S., Tsujimoto H., Hiraki S., Aosasa S. Mechanisms of sepsis-induced immunosuppression and immunological modification therapies for sepsis. Ann. Gastroenterol. Surg. 2018; 2 (5): 351-8.
URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6139715/
doi: 10.1002/ags3.12194
82. Textoris J., Beaufils N., Quintana G., Ben Lassoued A., et al. Hypoxia-inducible factor (HIF1a) gene expression in human shock states. Crit. Care. 2012; 16 (4): R120.
URL: https://www.ncbi.nlm.nih.gov/pubmed/22781303
doi: 10.1186/cc11414
83. Pan H., Wu X. Hypoxia attenuates inflammatory mediators production induced by Acanthamoeba via Toll-like receptor 4 signaling in human corneal epithelial cells. Biochem. Biophys. Res. Commun. 2012; 420 (3): 685-91.
84. Kiers H.D., Scheffer G.-J., van der Hoeven J.G., Eltzschig H.K., et al. Immunologic consequences of hypoxia during critical illness. Anesthesiology. 2016; 125 (1): 237-49.
URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5119461/
doi: 10.1097/ALN.0000000000001163