Fatty acid-binding protein 5 limits ILC2-mediated allergic lung inflammation in a murine asthma model.
Alveolar Epithelial Cells
/ metabolism
Animals
Asthma
/ genetics
Diet, High-Fat
/ adverse effects
Disease Models, Animal
Fatty Acid-Binding Proteins
/ genetics
Gene Expression
Inflammation
/ immunology
Interleukin-1 Receptor-Like 1 Protein
/ genetics
Lipid Metabolism
Lung
/ immunology
Lymphocytes
/ immunology
Mice, Inbred C57BL
Molecular Targeted Therapy
Neoplasm Proteins
/ genetics
Obesity
/ etiology
Tretinoin
/ metabolism
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
06 10 2020
06 10 2020
Historique:
received:
06
06
2020
accepted:
09
09
2020
entrez:
7
10
2020
pubmed:
8
10
2020
medline:
11
3
2021
Statut:
epublish
Résumé
Dietary obesity is regarded as a problem worldwide, and it has been revealed the strong linkage between obesity and allergic inflammation. Fatty acid-binding protein 5 (FABP5) is expressed in lung cells, such as alveolar epithelial cells (ECs) and alveolar macrophages, and plays an important role in infectious lung inflammation. However, we do not know precise mechanisms on how lipid metabolic change in the lung affects allergic lung inflammation. In this study, we showed that Fabp5
Identifiants
pubmed: 33024217
doi: 10.1038/s41598-020-73935-y
pii: 10.1038/s41598-020-73935-y
pmc: PMC7538993
doi:
Substances chimiques
Fabp5 protein, mouse
0
Fatty Acid-Binding Proteins
0
Il1rl1 protein, mouse
0
Interleukin-1 Receptor-Like 1 Protein
0
Neoplasm Proteins
0
Tretinoin
5688UTC01R
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
16617Références
Beasley, R., Crane, J., Lai, C. K. & Pearce, N. Prevalence and etiology of asthma. J. Allergy Clin. Immunol. 105, S466-472. https://doi.org/10.1016/s0091-6749(00)90044-7 (2000).
doi: 10.1016/s0091-6749(00)90044-7
pubmed: 10669525
Beuther, D. A. & Sutherland, E. R. Overweight, obesity, and incident asthma: A meta-analysis of prospective epidemiologic studies. Am. J. Respir. Crit. Care Med. 175, 661–666. https://doi.org/10.1164/rccm.200611-1717OC (2007).
doi: 10.1164/rccm.200611-1717OC
pubmed: 17234901
pmcid: 1899288
Shore, S. A. & Johnston, R. A. Obesity and asthma. Pharmacol. Ther. 110, 83–102. https://doi.org/10.1016/j.pharmthera.2005.10.002 (2006).
doi: 10.1016/j.pharmthera.2005.10.002
pubmed: 16297979
Artis, D. & Spits, H. The biology of innate lymphoid cells. Nature 517, 293–301. https://doi.org/10.1038/nature14189 (2015).
doi: 10.1038/nature14189
pubmed: 25592534
Halim, T. Y., Krauss, R. H., Sun, A. C. & Takei, F. Lung natural helper cells are a critical source of Th2 cell-type cytokines in protease allergen-induced airway inflammation. Immunity 36, 451–463. https://doi.org/10.1016/j.immuni.2011.12.020 (2012).
doi: 10.1016/j.immuni.2011.12.020
pubmed: 22425247
Kim, B. S. et al. TSLP elicits IL-33-independent innate lymphoid cell responses to promote skin inflammation. Sci. Transl. Med. 5, 170ra116. https://doi.org/10.1126/scitranslmed.3005374 (2013).
doi: 10.1126/scitranslmed.3005374
Moro, K. et al. Interferon and IL-27 antagonize the function of group 2 innate lymphoid cells and type 2 innate immune responses. Nat. Immunol. 17, 76–86. https://doi.org/10.1038/ni.3309 (2016).
doi: 10.1038/ni.3309
pubmed: 26595888
Duerr, C. U. et al. Type I interferon restricts type 2 immunopathology through the regulation of group 2 innate lymphoid cells. Nat. Immunol. 17, 65–75. https://doi.org/10.1038/ni.3308 (2016).
doi: 10.1038/ni.3308
pubmed: 26595887
Doherty, T. A. & Broide, D. H. Lipid regulation of group 2 innate lymphoid cell function: Moving beyond epithelial cytokines. J. Allergy Clin. Immunol. 141, 1587–1589. https://doi.org/10.1016/j.jaci.2018.02.034 (2018).
doi: 10.1016/j.jaci.2018.02.034
pubmed: 29522852
pmcid: 5967253
Seehus, C. R. et al. Alternative activation generates IL-10 producing type 2 innate lymphoid cells. Nat. Commun. 8, 1900. https://doi.org/10.1038/s41467-017-02023-z (2017).
doi: 10.1038/s41467-017-02023-z
pubmed: 29196657
pmcid: 5711851
Morita, H. et al. Induction of human regulatory innate lymphoid cells from group 2 innate lymphoid cells by retinoic acid. J. Allergy Clin. Immunol. 143, 2190-2201.e2199. https://doi.org/10.1016/j.jaci.2018.12.1018 (2019).
doi: 10.1016/j.jaci.2018.12.1018
pubmed: 30682454
Moore, S. M., Holt, V. V., Malpass, L. R., Hines, I. N. & Wheeler, M. D. Fatty acid-binding protein 5 limits the anti-inflammatory response in murine macrophages. Mol. Immunol. 67, 265–275. https://doi.org/10.1016/j.molimm.2015.06.001 (2015).
doi: 10.1016/j.molimm.2015.06.001
pubmed: 26105806
pmcid: 4565774
Kitanaka, N. et al. Epidermal-type fatty acid binding protein as a negative regulator of IL-12 production in dendritic cells. Biochem. Biophys. Res. Commun. 345, 459–466. https://doi.org/10.1016/j.bbrc.2006.04.114 (2006).
doi: 10.1016/j.bbrc.2006.04.114
pubmed: 16684508
Li, B., Reynolds, J. M., Stout, R. D., Bernlohr, D. A. & Suttles, J. Regulation of Th17 differentiation by epidermal fatty acid-binding protein. J. Immunol. 182, 7625–7633. https://doi.org/10.4049/jimmunol.0804192 (2009).
doi: 10.4049/jimmunol.0804192
pubmed: 19494286
pmcid: 2707838
Gally, F. et al. FABP5 deficiency enhances susceptibility to H1N1 influenza A virus-induced lung inflammation. Am. J. Physiol. Lung Cell Mol. Physiol. 305, L64-72. https://doi.org/10.1152/ajplung.00276.2012 (2013).
doi: 10.1152/ajplung.00276.2012
pubmed: 23624787
pmcid: 4888543
Rao, D. M. et al. Impact of fatty acid binding protein 5-deficiency on COPD exacerbations and cigarette smoke-induced inflammatory response to bacterial infection. Clin. Transl. Med. 8, 7. https://doi.org/10.1186/s40169-019-0227-8 (2019).
doi: 10.1186/s40169-019-0227-8
pubmed: 30877402
pmcid: 6420539
Gally, F., Chu, H. W. & Bowler, R. P. Cigarette smoke decreases airway epithelial FABP5 expression and promotes Pseudomonas aeruginosa infection. PLoS ONE 8, e51784. https://doi.org/10.1371/journal.pone.0051784 (2013).
doi: 10.1371/journal.pone.0051784
pubmed: 23349676
pmcid: 3551956
Rao, D., Perraud, A. L., Schmitz, C. & Gally, F. Cigarette smoke inhibits LPS-induced FABP5 expression by preventing c-Jun binding to the FABP5 promoter. PLoS ONE 12, e0178021. https://doi.org/10.1371/journal.pone.0178021 (2017).
doi: 10.1371/journal.pone.0178021
pubmed: 28542209
pmcid: 5436865
Owada, Y. et al. Altered water barrier function in epidermal-type fatty acid binding protein-deficient mice. J. Investig. Dermatol. 118, 430–435. https://doi.org/10.1046/j.0022-202x.2001.01616.x (2002).
doi: 10.1046/j.0022-202x.2001.01616.x
pubmed: 11874481
Wittke, A., Weaver, V., Mahon, B. D., August, A. & Cantorna, M. T. Vitamin D receptor-deficient mice fail to develop experimental allergic asthma. J. Immunol. 173, 3432–3436. https://doi.org/10.4049/jimmunol.173.5.3432 (2004).
doi: 10.4049/jimmunol.173.5.3432
pubmed: 15322208
Liu, Y. et al. IRAK-M associates with susceptibility to adult-onset asthma and promotes chronic airway inflammation. J. Immunol. 202, 899–911. https://doi.org/10.4049/jimmunol.1800712 (2019).
doi: 10.4049/jimmunol.1800712
pubmed: 30617222
pmcid: 6344301
Suojalehto, H. et al. Level of fatty acid binding protein 5 (FABP5) is increased in sputum of allergic asthmatics and links to airway remodeling and inflammation. PLoS ONE 10, e0127003. https://doi.org/10.1371/journal.pone.0127003 (2015).
doi: 10.1371/journal.pone.0127003
pubmed: 26020772
pmcid: 4447257
Hind, M. & Maden, M. Retinoic acid induces alveolar regeneration in the adult mouse lung. Eur. Respir. J. 23, 20–27. https://doi.org/10.1183/09031936.03.00119103 (2004).
doi: 10.1183/09031936.03.00119103
pubmed: 14738226
Spencer, S. P. et al. Adaptation of innate lymphoid cells to a micronutrient deficiency promotes type 2 barrier immunity. Science 343, 432–437. https://doi.org/10.1126/science.1247606 (2014).
doi: 10.1126/science.1247606
pubmed: 24458645
pmcid: 4313730
Owada, Y. et al. Localization of epidermal-type fatty acid binding protein in alveolar macrophages and some alveolar type II epithelial cells in mouse lung. Histochem. J. 33, 453–457. https://doi.org/10.1023/a:1014420330284 (2001).
doi: 10.1023/a:1014420330284
pubmed: 11931385
Guillot, L. et al. Alveolar epithelial cells: Master regulators of lung homeostasis. Int. J. Biochem. Cell Biol. 45, 2568–2573. https://doi.org/10.1016/j.biocel.2013.08.009 (2013).
doi: 10.1016/j.biocel.2013.08.009
pubmed: 23988571
Manicone, A. M. Role of the pulmonary epithelium and inflammatory signals in acute lung injury. Expert. Rev. Clin. Immunol. 5, 63–75. https://doi.org/10.1586/177666X.5.1.63 (2009).
doi: 10.1586/177666X.5.1.63
pubmed: 19885383
pmcid: 2745180
Szatmari, I. et al. PPARgamma controls CD1d expression by turning on retinoic acid synthesis in developing human dendritic cells. J. Exp. Med. 203, 2351–2362. https://doi.org/10.1084/jem.20060141 (2006).
doi: 10.1084/jem.20060141
pubmed: 16982809
pmcid: 2118109
Everaere, L. et al. Innate lymphoid cells contribute to allergic airway disease exacerbation by obesity. J. Allergy Clin. Immunol. 138, 1309-1318.e1311. https://doi.org/10.1016/j.jaci.2016.03.019 (2016).
doi: 10.1016/j.jaci.2016.03.019
pubmed: 27177781
Zheng, H. et al. Leptin promotes allergic airway inflammation through targeting the unfolded protein response pathway. Sci. Rep. 8, 8905. https://doi.org/10.1038/s41598-018-27278-4 (2018).
doi: 10.1038/s41598-018-27278-4
pubmed: 29891850
pmcid: 5995879
Trasino, S. E., Tang, X. H., Jessurun, J. & Gudas, L. J. Obesity leads to tissue, but not serum vitamin A deficiency. Sci. Rep. 5, 15893. https://doi.org/10.1038/srep15893 (2015).
doi: 10.1038/srep15893
pubmed: 26522079
pmcid: 4629132
Rausch, M. E., Weisberg, S., Vardhana, P. & Tortoriello, D. V. Obesity in C57BL/6J mice is characterized by adipose tissue hypoxia and cytotoxic T-cell infiltration. Int. J. Obes. (Lond.) 32, 451–463. https://doi.org/10.1038/sj.ijo.0803744 (2008).
doi: 10.1038/sj.ijo.0803744
Lumeng, C. N., Bodzin, J. L. & Saltiel, A. R. Obesity induces a phenotypic switch in adipose tissue macrophage polarization. J. Clin. Investig. 117, 175–184. https://doi.org/10.1172/JCI29881 (2007).
doi: 10.1172/JCI29881
pubmed: 17200717
Shore, S. A. Obesity and asthma: Possible mechanisms. J. Allergy Clin. Immunol. 121, 1087–1093. https://doi.org/10.1016/j.jaci.2008.03.004 (2008) (quiz 1094–1085).
doi: 10.1016/j.jaci.2008.03.004
pubmed: 18405959
Maeda, K. et al. Role of the fatty acid binding protein mal1 in obesity and insulin resistance. Diabetes 52, 300–307. https://doi.org/10.2337/diabetes.52.2.300 (2003).
doi: 10.2337/diabetes.52.2.300
pubmed: 4027060
pmcid: 4027060
Shibue, K. et al. Fatty acid-binding protein 5 regulates diet-induced obesity via GIP secretion from enteroendocrine K cells in response to fat ingestion. Am. J. Physiol. Endocrinol. Metab. 308, E583-591. https://doi.org/10.1152/ajpendo.00543.2014 (2015).
doi: 10.1152/ajpendo.00543.2014
pubmed: 25628425
Tyagi, S., Gupta, P., Saini, A. S., Kaushal, C. & Sharma, S. The peroxisome proliferator-activated receptor: A family of nuclear receptors role in various diseases. J. Adv. Pharm. Technol. Res. 2, 236–240. https://doi.org/10.4103/2231-4040.90879 (2011).
doi: 10.4103/2231-4040.90879
pubmed: 22247890
pmcid: 3255347
Lehrke, M. & Lazar, M. A. The many faces of PPARgamma. Cell 123, 993–999. https://doi.org/10.1016/j.cell.2005.11.026 (2005).
doi: 10.1016/j.cell.2005.11.026
pubmed: 16360030
Lee, K. S. et al. PPAR-gamma modulates allergic inflammation through up-regulation of PTEN. FASEB J. 19, 1033–1035. https://doi.org/10.1096/fj.04-3309fje (2005).
doi: 10.1096/fj.04-3309fje
pubmed: 15788448
Keen, H. L. et al. Gene expression profiling of potential PPARgamma target genes in mouse aorta. Physiol. Genom. 18, 33–42. https://doi.org/10.1152/physiolgenomics.00027.2004 (2004).
doi: 10.1152/physiolgenomics.00027.2004
Hontecillas, R. et al. Immunoregulatory mechanisms of macrophage PPAR-γ in mice with experimental inflammatory bowel disease. Mucosal Immunol. 4, 304–313. https://doi.org/10.1038/mi.2010.75 (2011).
doi: 10.1038/mi.2010.75
pubmed: 21068720
Ng-Blichfeldt, J. P. et al. Retinoic acid signaling balances adult distal lung epithelial progenitor cell growth and differentiation. EBioMedicine 36, 461–474. https://doi.org/10.1016/j.ebiom.2018.09.002 (2018).
doi: 10.1016/j.ebiom.2018.09.002
pubmed: 30236449
pmcid: 6197151
Oliveira, L. M., Teixeira, F. M. E. & Sato, M. N. Impact of retinoic acid on immune cells and inflammatory diseases. Mediat. Inflamm. 2018, 3067126. https://doi.org/10.1155/2018/3067126 (2018).
doi: 10.1155/2018/3067126
Czarnewski, P., Das, S., Parigi, S. M. & Villablanca, E. J. Retinoic acid and its role in modulating intestinal innate immunity. Nutrients. https://doi.org/10.3390/nu9010068 (2017).
doi: 10.3390/nu9010068
pubmed: 28098786
pmcid: 5295112
Marquez, H. A. & Cardoso, W. V. Vitamin A-retinoid signaling in pulmonary development and disease. Mol. Cell Pediatr. 3, 28. https://doi.org/10.1186/s40348-016-0054-6 (2016).
doi: 10.1186/s40348-016-0054-6
pubmed: 27480876
pmcid: 4969253
Liu, Z. M., Wang, K. P., Ma, J. & Guo Zheng, S. The role of all-trans retinoic acid in the biology of Foxp3+ regulatory T cells. Cell Mol. Immunol. 12, 553–557. https://doi.org/10.1038/cmi.2014.133 (2015).
doi: 10.1038/cmi.2014.133
pubmed: 25640656
pmcid: 4579645
Yamamoto, Y. et al. FABP3 in the anterior cingulate cortex modulates the methylation status of the glutamic acid decarboxylase. J. Neurosci. 38, 10411–10423. https://doi.org/10.1523/JNEUROSCI.1285-18.2018 (2018).
doi: 10.1523/JNEUROSCI.1285-18.2018
pubmed: 30341178
pmcid: 6596254
Chen, Z., Li, S., Subramaniam, S., Shyy, J. Y. & Chien, S. Epigenetic regulation: A new frontier for biomedical engineers. Annu. Rev. Biomed. Eng. 19, 195–219. https://doi.org/10.1146/annurev-bioeng-071516-044720 (2017).
doi: 10.1146/annurev-bioeng-071516-044720
pubmed: 28301736
Kucharski, R., Maleszka, J., Foret, S. & Maleszka, R. Nutritional control of reproductive status in honeybees via DNA methylation. Science 319, 1827–1830. https://doi.org/10.1126/science.1153069 (2008).
doi: 10.1126/science.1153069
pubmed: 18339900
Gerhauser, C. Impact of dietary gut microbial metabolites on the epigenome. Philos. Trans. R. Soc. Lond. B Biol. Sci. https://doi.org/10.1098/rstb.2017.0359 (2018).
doi: 10.1098/rstb.2017.0359
pubmed: 29685968
pmcid: 5915727
Garaeva, A. A., Kovaleva, I. E., Chumakov, P. M. & Evstafieva, A. G. Mitochondrial dysfunction induces SESN2 gene expression through Activating Transcription Factor 4. Cell Cycle 15, 64–71. https://doi.org/10.1080/15384101.2015.1120929 (2016).
doi: 10.1080/15384101.2015.1120929
pubmed: 26771712
pmcid: 4825760
Field, C. S. et al. Mitochondrial integrity regulated by lipid metabolism is a cell-intrinsic checkpoint for treg suppressive function. Cell Metab. https://doi.org/10.1016/j.cmet.2019.11.021 (2019).
doi: 10.1016/j.cmet.2019.11.021
pubmed: 31883840
pmcid: 6688828