The Potential Importance of CXCL1 in the Physiological State and in Noncancer Diseases of the Cardiovascular System, Respiratory System and Skin
Abstract
:1. Introduction
2. Research Methodology
3. Cardiovascular System
3.1. The Physiology of Blood Vessels
3.2. Atherosclerosis
3.3. Atrial Fibrillation
3.4. Chronic Oschemic Heart Disease
3.5. Heart Failure
3.6. Hypertension
3.7. Sepsis
4. Respiratory System
4.1. Asthma
4.2. Chronic Obstructive Pulmonary Disease (COPD)
4.3. Chronic Rhinosinusitis
4.4. Coronavirus Disease 2019 (COVID-19)
4.5. Influenza
4.6. Lung Transplantation and Ischemic-Reperfusion Injury
4.7. Tuberculosis
5. Skin
5.1. Wound Healing
5.2. Psoriasis
5.3. Sunburn
5.4. Xeroderma Pigmentosum
5.5. Itchy Skin
6. Perspectives for Further Research
7. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Borish, L.C.; Steinke, J.W. 2. Cytokines and chemokines. J. Allergy Clin. Immunol. 2003, 111, S460–S475. [Google Scholar] [CrossRef]
- Hughes, C.E.; Nibbs, R.J.B. A guide to chemokines and their receptors. FEBS J. 2018, 285, 2944–2971. [Google Scholar] [CrossRef]
- Richmond, A.; Lawson, D.H.; Nixon, D.W.; Chawla, R.K. Characterization of autostimulatory and transforming growth factors from human melanoma cells. Cancer Res. 1985, 45, 6390–6394. [Google Scholar]
- Heidemann, J.; Ogawa, H.; Dwinell, M.B.; Rafiee, P.; Maaser, C.; Gockel, H.R.; Otterson, M.F.; Ota, D.M.; Lugering, N.; Domschke, W.; et al. Angiogenic effects of interleukin 8 (CXCL8) in human intestinal microvascular endothelial cells are mediated by CXCR2. J. Biol. Chem. 2003, 278, 8508–8515. [Google Scholar] [CrossRef] [Green Version]
- Singh, S.; Wu, S.; Varney, M.; Singh, A.P.; Singh, R.K. CXCR1 and CXCR2 silencing modulates CXCL8-dependent endothelial cell proliferation, migration and capillary-like structure formation. Microvasc. Res. 2011, 82, 318–325. [Google Scholar] [CrossRef] [Green Version]
- Jablonska, J.; Wu, C.F.; Andzinski, L.; Leschner, S.; Weiss, S. CXCR2-mediated tumor-associated neutrophil recruitment is regulated by IFN-β. Int. J. Cancer 2014, 134, 1346–1358. [Google Scholar] [CrossRef] [Green Version]
- Khaw, Y.M.; Cunningham, C.; Tierney, A.; Sivaguru, M.; Inoue, M. Neutrophil-selective deletion of Cxcr2 protects against CNS neurodegeneration in a mouse model of multiple sclerosis. J. Neuroinflammation 2020, 17, 49. [Google Scholar] [CrossRef]
- Moser, B.; Clark-Lewis, I.; Zwahlen, R.; Baggiolini, M. Neutrophil-activating properties of the melanoma growth-stimulatory activity. J. Exp. Med. 1990, 171, 1797–1802. [Google Scholar] [CrossRef]
- Anisowicz, A.; Messineo, M.; Lee, S.W.; Sager, R. An NF-kappa B-like transcription factor mediates IL-1/TNF-alpha induction of gro in human fibroblasts. J. Immunol. 1991, 147, 520–527. [Google Scholar]
- Issa, R.; Xie, S.; Lee, K.Y.; Stanbridge, R.D.; Bhavsar, P.; Sukkar, M.B.; Chung, K.F. GRO-alpha regulation in airway smooth muscle by IL-1beta and TNF-alpha: Role of NF-kappaB and MAP kinases. Am. J. Physiol. Lung. Cell. Mol. Physiol. 2006, 291, L66–L74. [Google Scholar] [CrossRef]
- Sun, D.; Novotny, M.; Bulek, K.; Liu, C.; Li, X.; Hamilton, T. Treatment with IL-17 prolongs the half-life of chemokine CXCL1 mRNA via the adaptor TRAF5 and the splicing-regulatory factor SF2 (ASF). Nat. Immunol. 2011, 12, 853–860. [Google Scholar] [CrossRef] [PubMed]
- Herjan, T.; Yao, P.; Qian, W.; Li, X.; Liu, C.; Bulek, K.; Sun, D.; Yang, W.P.; Zhu, J.; He, A.; et al. HuR is required for IL-17-induced Act1-mediated CXCL1 and CXCL5 mRNA stabilization. J. Immunol. 2013, 191, 640–649. [Google Scholar] [CrossRef] [PubMed]
- Herjan, T.; Hong, L.; Bubenik, J.; Bulek, K.; Qian, W.; Liu, C.; Li, X.; Chen, X.; Yang, H.; Ouyang, S.; et al. IL-17-receptor-associated adaptor Act1 directly stabilizes mRNAs to mediate IL-17 inflammatory signaling. Nat. Immunol. 2018, 19, 354–365. [Google Scholar] [CrossRef] [PubMed]
- Pitanga, T.N.; de Aragão França, L.; Rocha, V.C.; Meirelles, T.; Borges, V.M.; Gonçalves, M.S.; Pontes-de-Carvalho, L.C.; Noronha-Dutra, A.A.; dos-Santos, W.L. Neutrophil-derived microparticles induce myeloperoxidase-mediated damage of vascular endothelial cells. BMC Cell. Biol. 2014, 15, 21. [Google Scholar] [CrossRef] [Green Version]
- Glennon-Alty, L.; Hackett, A.P.; Chapman, E.A.; Wright, H.L. Neutrophils and redox stress in the pathogenesis of autoimmune disease. Free Radic. Biol. Med. 2018, 125, 25–35. [Google Scholar] [CrossRef]
- Shimoda, N.; Fukazawa, N.; Nonomura, K.; Fairchild, R.L. Cathepsin g is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys. Am. J. Pathol. 2007, 170, 930–940. [Google Scholar] [CrossRef] [Green Version]
- Pérez-Figueroa, E.; Torres, J.; Sánchez-Zauco, N.; Contreras-Ramos, A.; Alvarez-Arellano, L.; Maldonado-Bernal, C. Activation of NLRP3 inflammasome in human neutrophils by Helicobacter pylori infection. Innate. Immun. 2016, 22, 103–112. [Google Scholar] [CrossRef] [Green Version]
- Loetscher, P.; Seitz, M.; Clark-Lewis, I.; Baggiolini, M.; Moser, B. Both interleukin-8 receptors independently mediate chemotaxis. Jurkat cells transfected with IL-8R1 or IL-8R2 migrate in response to IL-8, GRO alpha and NAP-2. FEBS Lett. 1994, 341, 187–192. [Google Scholar] [CrossRef] [Green Version]
- Ahuja, S.K.; Murphy, P.M. The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. J. Biol. Chem. 1996, 271, 20545–20550. [Google Scholar] [CrossRef] [Green Version]
- Wuyts, A.; Proost, P.; Lenaerts, J.P.; Ben-Baruch, A.; van Damme, J.; Wang, J.M. Differential usage of the CXC chemokine receptors 1 and 2 by interleukin-8, granulocyte chemotactic protein-2 and epithelial-cell-derived neutrophil attractant-78. Eur. J. Biochem. 1998, 255, 67–73. [Google Scholar] [CrossRef]
- Korbecki, J.; Kupnicka, P.; Chlubek, M.; Gorący, J.; Gutowska, I.; Baranowska-Bosiacka, I. CXCR2 Receptor: Regulation of Expression, Signal Transduction, and Involvement in Cancer. Int. J. Mol. Sci. 2022, 23, 2168. [Google Scholar] [CrossRef] [PubMed]
- Damaj, B.B.; McColl, S.R.; Mahana, W.; Crouch, M.F.; Naccache, P.H. Physical association of Gi2α with interleukin-8 receptors. J. Biol. Chem. 1996, 271, 12783–12789. [Google Scholar] [CrossRef] [PubMed]
- Kuwano, Y.; Adler, M.; Zhang, H.; Groisman, A.; Ley, K. Gαi2 and Gαi3 differentially regulate arrest from flow and chemotaxis in mouse neutrophils. J. Immunol. 2016, 196, 3828–3833. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Stephens, L.R.; Eguinoa, A.; Erdjument-Bromage, H.; Lui, M.; Cooke, F.; Coadwell, J.; Smrcka, A.S.; Thelen, M.; Cadwallader, K.; Tempst, P.; et al. The Gβγ sensitivity of a PI3K is dependent upon a tightly associated adaptor, p101. Cell 1997, 89, 105–114. [Google Scholar] [CrossRef] [Green Version]
- Boyer, J.L.; Graber, S.G.; Waldo, G.L.; Harden, T.K.; Garrison, J.C. Selective activation of phospholipase C by recombinant G-protein alpha- and beta gamma-subunits. J. Biol. Chem. 1994, 269, 2814–2819. [Google Scholar] [CrossRef]
- Metzner, B.; Elsner, J.; Dobos, G.; Kownatzki, E.; Parlow, F.; Schraufstätter, I.; Norgauer, J. [Ca2+]i-transients and actin polymerization in human neutrophils under stimulation with GRO α and complement fragment C5a. Agents Actions 1994, 42, 101–106. [Google Scholar] [CrossRef]
- Raman, D.; Neel, N.F.; Sai, J.; Mernaugh, R.L.; Ham, A.J.; Richmond, A.J. Characterization of chemokine receptor CXCR2 interacting proteins using a proteomics approach to define the CXCR2 “chemosynapse”. Methods Enzymol. 2009, 460, 315–330. [Google Scholar]
- Neel, N.F.; Sai, J.; Ham, A.J.; Sobolik-Delmaire, T.; Mernaugh, R.L.; Richmond, A. IQGAP1 is a novel CXCR2-interacting protein and essential component of the “chemosynapse”. PLoS ONE 2011, 6, e23813. [Google Scholar] [CrossRef] [Green Version]
- Nomiyama, H.; Mera, A.; Ohneda, O.; Miura, R.; Suda, T.; Yoshie, O. Organization of the chemokine genes in the human and mouse major clusters of CC and CXC chemokines: Diversification between the two species. Genes Immun. 2001, 2, 110–113. [Google Scholar] [CrossRef] [Green Version]
- Nomiyama, H.; Osada, N.; Yoshie, O. Systematic classification of vertebrate chemokines based on conserved synteny and evolutionary history. Genes Cells 2013, 18, 1–16. [Google Scholar] [CrossRef] [Green Version]
- Strieter, R.M.; Polverini, P.J.; Kunkel, S.L.; Arenberg, D.A.; Burdick, M.D.; Kasper, J.; Dzuiba, J.; Van Damme, J.; Walz, A.; Marriott, D.; et al. The functional role of the ELR motif in CXC chemokine-mediated angiogenesis. J. Biol. Chem. 1995, 270, 27348–27357. [Google Scholar] [CrossRef] [Green Version]
- Addison, C.L.; Daniel, T.O.; Burdick, M.D.; Liu, H.; Ehlert, J.E.; Xue, Y.Y.; Buechi, L.; Walz, A.; Richmond, A.; Strieter, R.M. The CXC chemokine receptor 2, CXCR2, is the putative receptor for ELR+ CXC chemokine-induced angiogenic activity. J. Immunol. 2000, 165, 5269–5277. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Karl, E.; Warner, K.; Zeitlin, B.; Kaneko, T.; Wurtzel, L.; Jin, T.; Chang, J.; Wang, S.; Wang, C.Y.; Strieter, R.M.; et al. Bcl-2 acts in a proangiogenic signaling pathway through nuclear factor-kappaB and CXC chemokines. Cancer Res. 2005, 65, 5063–5069. [Google Scholar] [CrossRef] [PubMed]
- Karl, E.; Zhang, Z.; Dong, Z.; Neiva, K.G.; Soengas, M.S.; Koch, A.E.; Polverini, P.J.; Núñez, G.; Nör, J.E. Unidirectional crosstalk between Bcl-xL and Bcl-2 enhances the angiogenic phenotype of endothelial cells. Cell Death Differ. 2007, 14, 1657–1666. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Grosser, M.; Magdolen, V.; Baretton, G.; Luther, T.; Albrecht, S. Gene expression analysis of HUVEC in response to TF-binding. Thromb. Res. 2011, 127, 259–263. [Google Scholar] [CrossRef]
- Hristov, M.; Zernecke, A.; Bidzhekov, K.; Liehn, E.A.; Shagdarsuren, E.; Ludwig, A.; Weber, C. Importance of CXC chemokine receptor 2 in the homing of human peripheral blood endothelial progenitor cells to sites of arterial injury. Circ. Res. 2007, 100, 590–597. [Google Scholar] [CrossRef] [Green Version]
- Kanzler, I.; Tuchscheerer, N.; Steffens, G.; Simsekyilmaz, S.; Konschalla, S.; Kroh, A.; Simons, D.; Asare, Y.; Schober, A.; Bucala, R.; et al. Differential roles of angiogenic chemokines in endothelial progenitor cell-induced angiogenesis. Basic Res. Cardiol. 2013, 108, 310. [Google Scholar] [CrossRef] [Green Version]
- Liehn, E.A.; Schober, A.; Weber, C. Blockade of keratinocyte-derived chemokine inhibits endothelial recovery and enhances plaque formation after arterial injury in ApoE-deficient mice. Arterioscler. Thromb. Vasc. Biol. 2004, 24, 1891–1896. [Google Scholar] [CrossRef] [Green Version]
- Yu, B.; Wong, M.M.; Potter, C.M.; Simpson, R.M.; Karamariti, E.; Zhang, Z.; Zeng, L.; Warren, D.; Hu, Y.; Wang, W.; et al. Vascular Stem/Progenitor Cell Migration Induced by Smooth Muscle Cell-Derived Chemokine (C-C Motif) Ligand 2 and Chemokine (C-X-C motif) Ligand 1 Contributes to Neointima Formation. Stem. Cells 2016, 34, 2368–2380. [Google Scholar] [CrossRef] [Green Version]
- Hagiwara, H.; Mitsumata, M.; Yamane, T.; Jin, X.; Yoshida, Y. Laminar shear stress-induced GRO mRNA and protein expression in endothelial cells. Circulation 1998, 98, 2584–2590. [Google Scholar] [CrossRef] [Green Version]
- Vries, M.H.; Wagenaar, A.; Verbruggen, S.E.; Molin, D.G.; Dijkgraaf, I.; Hackeng, T.H.; Post, M.J. CXCL1 promotes arteriogenesis through enhanced monocyte recruitment into the peri-collateral space. Angiogenesis 2015, 18, 163–171. [Google Scholar] [CrossRef] [PubMed]
- Troidl, C.; Jung, G.; Troidl, K.; Hoffmann, J.; Mollmann, H.; Nef, H.; Schaper, W.; Hamm, C.W.; Schmitz-Rixen, T. The temporal and spatial distribution of macrophage subpopulations during arteriogenesis. Curr. Vasc. Pharmacol. 2013, 11, 5–12. [Google Scholar] [CrossRef] [PubMed]
- Zhu, H.; Zhang, M.; Liu, Z.; Xing, J.; Moriasi, C.; Dai, X.; Zou, M.H. AMP-Activated Protein Kinase α1 in Macrophages Promotes Collateral Remodeling and Arteriogenesis in Mice In Vivo. Arterioscler. Thromb. Vasc. Biol. 2016, 36, 1868–1878. [Google Scholar] [CrossRef] [PubMed]
- Hopkins, P.N. Molecular biology of atherosclerosis. Physiol. Rev. 2013, 93, 1317–1542. [Google Scholar] [CrossRef] [PubMed]
- Libby, P.; Buring, J.E.; Badimon, L.; Hansson, G.K.; Deanfield, J.; Bittencourt, M.S.; Tokgözoğlu, L.; Lewis, E.F. Atherosclerosis. Nat. Rev. Dis. Primers. 2019, 5, 56. [Google Scholar] [CrossRef] [PubMed]
- Papadopoulou, C.; Corrigall, V.; Taylor, P.R.; Poston, R.N. The role of the chemokines MCP-1, GRO-alpha, IL-8 and their receptors in the adhesion of monocytic cells to human atherosclerotic plaques. Cytokine 2008, 43, 181–186. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lei, Z.B.; Zhang, Z.; Jing, Q.; Qin, Y.W.; Pei, G.; Cao, B.Z.; Li, X.Y. OxLDL upregulates CXCR2 expression in monocytes via scavenger receptors and activation of p38 mitogen-activated protein kinase. Cardiovasc. Res. 2002, 53, 524–532. [Google Scholar] [CrossRef] [Green Version]
- Wezel, A.; Lagraauw, H.M.; van der Velden, D.; de Jager, S.C.; Quax, P.H.; Kuiper, J.; Bot, I. Mast cells mediate neutrophil recruitment during atherosclerotic plaque progression. Atherosclerosis 2015, 241, 289–296. [Google Scholar] [CrossRef]
- Tucureanu, M.M.; Butoi, E.; Gan, A.M.; Stan, D.; Constantinescu, C.A.; Calin, M.; Simionescu, M.; Manduteanu, I. Amendment of the cytokine profile in macrophages subsequent to their interaction with smooth muscle cells: Differential modulation by fractalkine and resistin. Cytokine 2016, 83, 250–261. [Google Scholar] [CrossRef]
- Schwartz, D.; Andalibi, A.; Chaverri-Almada, L.; Berliner, J.A.; Kirchgessner, T.; Fang, Z.T.; Tekamp-Olson, P.; Lusis, A.J.; Gallegos, C.; Fogelman, A.M.; et al. Role of the GRO family of chemokines in monocyte adhesion to MM-LDL-stimulated endothelium. J. Clin. Investig. 1994, 94, 1968–1973. [Google Scholar] [CrossRef]
- Zhou, Z.; Subramanian, P.; Sevilmis, G.; Globke, B.; Soehnlein, O.; Karshovska, E.; Megens, R.; Heyll, K.; Chun, J.; Saulnier-Blache, J.S.; et al. Lipoprotein-derived lysophosphatidic acid promotes atherosclerosis by releasing CXCL1 from the endothelium. Cell Metab. 2011, 13, 592–600. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Breland, U.M.; Halvorsen, B.; Hol, J.; Øie, E.; Paulsson-Berne, G.; Yndestad, A.; Smith, C.; Otterdal, K.; Hedin, U.; Waehre, T.; et al. A potential role of the CXC chemokine GROalpha in atherosclerosis and plaque destabilization: Downregulatory effects of statins. Arterioscler. Thromb. Vasc. Biol. 2008, 28, 1005–1011. [Google Scholar] [CrossRef] [PubMed]
- Hartwig, H.; Silvestre Roig, C.; Daemen, M.; Lutgens, E.; Soehnlein, O. Neutrophils in atherosclerosis. A brief overview. Hamostaseologie 2015, 35, 121–127. [Google Scholar]
- Huo, Y.; Weber, C.; Forlow, S.B.; Sperandio, M.; Thatte, J.; Mack, M.; Jung, S.; Littman, D.R.; Ley, K. The chemokine KC, but not monocyte chemoattractant protein-1, triggers monocyte arrest on early atherosclerotic endothelium. J. Clin. Investig. 2001, 108, 1307–1314. [Google Scholar] [CrossRef] [PubMed]
- Smith, D.F.; Galkina, E.; Ley, K.; Huo, Y. GRO family chemokines are specialized for monocyte arrest from flow. Am. J. Physiol. Heart Circ. Physiol. 2005, 289, H1976–H1984. [Google Scholar] [CrossRef]
- Boisvert, W.A.; Rose, D.M.; Johnson, K.A.; Fuentes, M.E.; Lira, S.A.; Curtiss, L.K.; Terkeltaub, R.A. Up-regulated expression of the CXCR2 ligand KC/GRO-alpha in atherosclerotic lesions plays a central role in macrophage accumulation and lesion progression. Am. J. Pathol. 2006, 168, 1385–1395. [Google Scholar] [CrossRef] [Green Version]
- Lin, H.C.; Lii, C.K.; Chen, H.C.; Lin, A.H.; Yang, Y.C.; Chen, H.W. Andrographolide Inhibits Oxidized LDL-Induced Cholesterol Accumulation and Foam Cell Formation in Macrophages. Am. J. Chin. Med. 2018, 46, 87–106. [Google Scholar] [CrossRef]
- Jay, A.G.; Chen, A.N.; Paz, M.A.; Hung, J.P.; Hamilton, J.A. CD36 binds oxidized low density lipoprotein (LDL) in a mechanism dependent upon fatty acid binding. J. Biol. Chem. 2015, 290, 4590–4603. [Google Scholar] [CrossRef] [Green Version]
- Yao, L.; Heuser-Baker, J.; Herlea-Pana, O.; Iida, R.; Wang, Q.; Zou, M.H.; Barlic-Dicen, J. Bone marrow endothelial progenitors augment atherosclerotic plaque regression in a mouse model of plasma lipid lowering. Stem. Cells 2012, 30, 2720–2731. [Google Scholar] [CrossRef] [Green Version]
- Blum, S.; Meyre, P.; Aeschbacher, S.; Berger, S.; Auberson, C.; Briel, M.; Osswald, S.; Conen, D. Incidence and predictors of atrial fibrillation progression: A systematic review and meta-analysis. Heart Rhythm. 2019, 16, 502–510. [Google Scholar] [CrossRef]
- Zhang, Y.L.; Cao, H.J.; Han, X.; Teng, F.; Chen, C.; Yang, J.; Yan, X.; Li, P.B.; Liu, Y.; Xia, Y.L.; et al. Chemokine Receptor CXCR-2 Initiates Atrial Fibrillation by Triggering Monocyte Mobilization in Mice. Hypertension 2020, 76, 381–392. [Google Scholar] [CrossRef] [PubMed]
- Fan, G.; Wei, J. Identification of potential novel biomarkers and therapeutic targets involved in human atrial fibrillation based on bioinformatics analysis. Kardiol. Pol. 2020, 78, 694–702. [Google Scholar] [CrossRef] [PubMed]
- Li, S.; Jiang, Z.; Chao, X.; Jiang, C.; Zhong, G. Identification of key immune-related genes and immune infiltration in atrial fibrillation with valvular heart disease based on bioinformatics analysis. J. Thorac. Dis. 2021, 13, 1785–1798. [Google Scholar] [CrossRef] [PubMed]
- Liao, C.H.; Akazawa, H.; Tamagawa, M.; Ito, K.; Yasuda, N.; Kudo, Y.; Yamamoto, R.; Ozasa, Y.; Fujimoto, M.; Wang, P.; et al. Cardiac mast cells cause atrial fibrillation through PDGF-A-mediated fibrosis in pressure-overloaded mouse hearts. J. Clin. Investig. 2010, 120, 242–253. [Google Scholar] [CrossRef] [PubMed]
- Smorodinova, N.; Bláha, M.; Melenovský, V.; Rozsívalová, K.; Přidal, J.; Ďurišová, M.; Pirk, J.; Kautzner, J.; Kučera, T. Analysis of immune cell populations in atrial myocardium of patients with atrial fibrillation or sinus rhythm. PLoS ONE 2017, 12, e0172691. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Keeley, E.C.; Moorman, J.R.; Liu, L.; Gimple, L.W.; Lipson, L.C.; Ragosta, M.; Taylor, A.M.; Lake, D.E.; Burdick, M.D.; Mehrad, B.; et al. Plasma chemokine levels are associated with the presence and extent of angiographic coronary collaterals in chronic ischemic heart disease. PLoS ONE 2011, 6, e21174. [Google Scholar] [CrossRef]
- Chang, S.L.; Hsiao, Y.W.; Tsai, Y.N.; Lin, S.F.; Liu, S.H.; Lin, Y.J.; Lo, L.W.; Chung, F.P.; Chao, T.F.; Hu, Y.F.; et al. Interleukin-17 enhances cardiac ventricular remodeling via activating MAPK pathway in ischemic heart failure. J. Mol. Cell. Cardiol. 2018, 122, 69–79. [Google Scholar] [CrossRef]
- Kocher, A.A.; Schuster, M.D.; Bonaros, N.; Lietz, K.; Xiang, G.; Martens, T.P.; Kurlansky, P.A.; Sondermeijer, H.; Witkowski, P.; Boyle, A.; et al. Myocardial homing and neovascularization by human bone marrow angioblasts is regulated by IL-8/Gro CXC chemokines. J. Mol. Cell. Cardiol. 2006, 40, 455–464. [Google Scholar] [CrossRef]
- Tarzami, S.T.; Miao, W.; Mani, K.; Lopez, L.; Factor, S.M.; Berman, J.W.; Kitsis, R.N. Opposing effects mediated by the chemokine receptor CXCR2 on myocardial ischemia-reperfusion injury: Recruitment of potentially damaging neutrophils and direct myocardial protection. Circulation 2003, 108, 2387–2392. [Google Scholar] [CrossRef] [Green Version]
- Pordel, S.; Sajedi Khanian, M.; Karimi, M.H.; Nikoo, H.; Doroudchi, M. Plasma CXCL1 levels and TRAF3IP2 variants in patients with myocardial infarction. J. Clin. Lab. Anal. 2018, 32, e22402. [Google Scholar] [CrossRef] [Green Version]
- Wang, L.; Zhang, Y.L.; Lin, Q.Y.; Liu, Y.; Guan, X.M.; Ma, X.L.; Cao, H.J.; Liu, Y.; Bai, J.; Xia, Y.L.; et al. CXCL1-CXCR2 axis mediates angiotensin II-induced cardiac hypertrophy and remodelling through regulation of monocyte infiltration. Eur. Heart. J. 2018, 39, 1818–1831. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Damås, J.K.; Eiken, H.G.; Oie, E.; Bjerkeli, V.; Yndestad, A.; Ueland, T.; Tonnessen, T.; Geiran, O.R.; Aass, H.; Simonsen, S.; et al. Myocardial expression of CC- and CXC-chemokines and their receptors in human end-stage heart failure. Cardiovasc. Res. 2000, 47, 778–787. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Zhang, Y.L.; Geng, C.; Yang, J.; Fang, J.; Yan, X.; Li, P.B.; Zou, L.X.; Chen, C.; Guo, S.B.; Li, H.H.; et al. Chronic inhibition of chemokine receptor CXCR2 attenuates cardiac remodeling and dysfunction in spontaneously hypertensive rats. Biochim. Biophys. Acta Mol. Basis. Dis. 2019, 1865, 165551. [Google Scholar] [CrossRef] [PubMed]
- Zhang, Y.L.; Teng, F.; Han, X.; Li, P.B.; Yan, X.; Guo, S.B.; Li, H.H. Selective blocking of CXCR2 prevents and reverses atrial fibrillation in spontaneously hypertensive rats. J. Cell. Mol. Med. 2020, 24, 11272–11282. [Google Scholar] [CrossRef]
- Falkenham, A.; de Antueno, R.; Rosin, N.; Betsch, D.; Lee, T.D.; Duncan, R.; Légaré, J.F. Nonclassical resident macrophages are important determinants in the development of myocardial fibrosis. Am. J. Pathol. 2015, 185, 927–942. [Google Scholar] [CrossRef]
- Heymans, S.; Corsten, M.F.; Verhesen, W.; Carai, P.; van Leeuwen, R.E.; Custers, K.; Peters, T.; Hazebroek, M.; Stöger, L.; Wijnands, E.; et al. Macrophage microRNA-155 promotes cardiac hypertrophy and failure. Circulation 2013, 128, 1420–1432. [Google Scholar] [CrossRef] [Green Version]
- Zhang, Y.; Bauersachs, J.; Langer, H.F. Immune mechanisms in heart failure. Eur. J. Heart Fail. 2017, 19, 1379–1389. [Google Scholar] [CrossRef] [Green Version]
- González, A.; Schelbert, E.B.; Díez, J.; Butler, J. Myocardial Interstitial Fibrosis in Heart Failure: Biological and Translational Perspectives. J. Am. Coll. Cardiol. 2018, 71, 1696–1706. [Google Scholar] [CrossRef]
- Wang, S.; Bai, J.; Zhang, Y.L.; Lin, Q.Y.; Han, X.; Qu, W.K.; Zhang, P.F.; Ge, Y.S.; Zhao, Q.; Li, H.H. CXCL1-CXCR2 signalling mediates hypertensive retinopathy by inducing macrophage infiltration. Redox Biol. 2022, 56, 102438. [Google Scholar] [CrossRef]
- Wang, L.; Zhao, X.C.; Cui, W.; Ma, Y.Q.; Ren, H.L.; Zhou, X.; Fassett, J.; Yang, Y.Z.; Chen, Y.; Xia, Y.L.; et al. Genetic and Pharmacologic Inhibition of the Chemokine Receptor CXCR2 Prevents Experimental Hypertension and Vascular Dysfunction. Circulation 2016, 134, 1353–1368. [Google Scholar] [CrossRef]
- Wenzel, P.; Knorr, M.; Kossmann, S.; Stratmann, J.; Hausding, M.; Schuhmacher, S.; Karbach, S.H.; Schwenk, M.; Yogev, N.; Schulz, E.; et al. Lysozyme M-positive monocytes mediate angiotensin II-induced arterial hypertension and vascular dysfunction. Circulation 2011, 124, 1370–1381. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chan, C.T.; Sobey, C.G.; Lieu, M.; Ferens, D.; Kett, M.M.; Diep, H.; Kim, H.A.; Krishnan, S.M.; Lewis, C.V.; Salimova, E.; et al. Obligatory Role for B Cells in the Development of Angiotensin II-Dependent Hypertension. Hypertension 2015, 66, 1023–1033. [Google Scholar] [CrossRef] [PubMed]
- Okamura, A.; Rakugi, H.; Ohishi, M.; Yanagitani, Y.; Takiuchi, S.; Moriguchi, K.; Fennessy, P.A.; Higaki, J.; Ogihara, T. Upregulation of renin-angiotensin system during differentiation of monocytes to macrophages. J. Hypertens. 1999, 17, 537–545. [Google Scholar] [CrossRef] [PubMed]
- Zhang, R.M.; McNerney, K.P.; Riek, A.E.; Bernal-Mizrachi, C. Immunity and Hypertension. Acta Physiol. (Oxf) 2021, 231, e13487. [Google Scholar] [CrossRef] [PubMed]
- Cecconi, M.; Evans, L.; Levy, M.; Rhodes, A. Sepsis and septic shock. Lancet 2018, 392, 75–87. [Google Scholar] [CrossRef]
- Gille-Johnson, P.; Smedman, C.; Gudmundsdotter, L.; Somell, A.; Nihlmark, K.; Paulie, S.; Andersson, J.; Gårdlund, B. Circulating monocytes are not the major source of plasma cytokines in patients with sepsis. Shock 2012, 38, 577–583. [Google Scholar] [CrossRef] [Green Version]
- Cummings, C.J.; Martin, T.R.; Frevert, C.W.; Quan, J.M.; Wong, V.A.; Mongovin, S.M.; Hagen, T.R.; Steinberg, K.P.; Goodman, R.B. Expression and function of the chemokine receptors CXCR1 and CXCR2 in sepsis. J. Immunol. 1999, 162, 2341–2346. [Google Scholar]
- Craciun, F.L.; Schuller, E.R.; Remick, D.G. Early enhanced local neutrophil recruitment in peritonitis-induced sepsis improves bacterial clearance and survival. J. Immunol. 2010, 185, 6930–6938. [Google Scholar] [CrossRef] [Green Version]
- Warford, J.; Lamport, A.C.; Kennedy, B.; Easton, A.S. Human Brain Chemokine and Cytokine Expression in Sepsis: A Report of Three Cases. Can. J. Neurol. Sci. 2017, 44, 96–104. [Google Scholar] [CrossRef]
- Wu, F.; Zhao, Y.; Jiao, T.; Shi, D.; Zhu, X.; Zhang, M.; Shi, M.; Zhou, H. CXCR2 is essential for cerebral endothelial activation and leukocyte recruitment during neuroinflammation. J. Neuroinflammation 2015, 12, 98. [Google Scholar] [CrossRef] [Green Version]
- Hasegawa-Ishii, S.; Inaba, M.; Shimada, A. Widespread time-dependent changes in tissue cytokine concentrations in brain regions during the acute phase of endotoxemia in mice. Neurotoxicology 2020, 76, 67–74. [Google Scholar] [CrossRef] [PubMed]
- Zhou, H.; Andonegui, G.; Wong, C.H.; Kubes, P. Role of endothelial TLR4 for neutrophil recruitment into central nervous system microvessels in systemic inflammation. J. Immunol. 2009, 183, 5244–5250. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wu, F.; Chen, X.; Zhai, L.; Wang, H.; Sun, M.; Song, C.; Wang, T.; Qian, Z. CXCR2 antagonist attenuates neutrophil transmigration into brain in a murine model of LPS induced neuroinflammation. Biochem. Biophys. Res. Commun. 2020, 529, 839–845. [Google Scholar] [CrossRef] [PubMed]
- Luo, C.J.; Zhang, F.J.; Zhang, L.; Geng, Y.Q.; Li, Q.G.; Hong, Q.; Fu, B.; Zhu, F.; Cui, S.Y.; Feng, Z.; et al. Mesenchymal stem cells ameliorate sepsis-associated acute kidney injury in mice. Shock 2014, 41, 123–129. [Google Scholar] [CrossRef] [PubMed]
- Luo, C.J.; Luo, F.; Zhang, L.; Xu, Y.; Cai, G.Y.; Fu, B.; Feng, Z.; Sun, X.F.; Chen, X.M. Knockout of interleukin-17A protects against sepsis-associated acute kidney injury. Ann. Intensive Care 2016, 6, 56. [Google Scholar] [CrossRef]
- Liu, B.; Ao, S.; Tan, F.; Ma, W.; Liu, H.; Liang, H.; Yang, X.; Chi, X. Transcriptomic analysis and laboratory experiments reveal potential critical genes and regulatory mechanisms in sepsis-associated acute kidney injury. Ann. Transl. Med. 2022, 10, 737. [Google Scholar] [CrossRef]
- Li, G.; Jia, J.; Ji, K.; Gong, X.; Wang, R.; Zhang, X.; Wang, H.; Zang, B. The neutrophil elastase inhibitor, sivelestat, attenuates sepsis-related kidney injury in rats. Int. J. Mol. Med. 2016, 38, 767–775. [Google Scholar] [CrossRef] [Green Version]
- Bu, X.; Zhang, L.; Chen, P.; Wu, X. Relation of neutrophil-to-lymphocyte ratio to acute kidney injury in patients with sepsis and septic shock: A retrospective study. Int. Immunopharmacol. 2019, 70, 372–377. [Google Scholar] [CrossRef]
- Larrouyet-Sarto, M.L.; Tamura, A.S.; Alves, V.S.; Santana, P.T.; Ciarlini-Magalhães, R.; Rangel, T.P.; Siebert, C.; Hartwig, J.R.; Dos Santos, T.M.; Wyse, A.T.S.; et al. P2X7 receptor deletion attenuates oxidative stress and liver damage in sepsis. Purinergic Signal. 2020, 16, 561–572. [Google Scholar] [CrossRef]
- Li, X.; Klintman, D.; Liu, Q.; Sato, T.; Jeppsson, B.; Thorlacius, H. Critical role of CXC chemokines in endotoxemic liver injury in mice. J. Leukoc. Biol. 2004, 75, 443–452. [Google Scholar] [CrossRef] [Green Version]
- Dorman, R.B.; Gujral, J.S.; Bajt, M.L.; Farhood, A.; Jaeschke, H. Generation and functional significance of CXC chemokines for neutrophil-induced liver injury during endotoxemia. Am. J. Physiol. Gastrointest. Liver Physiol. 2005, 288, G880–G886. [Google Scholar] [CrossRef] [Green Version]
- Sander, L.E.; Sackett, S.D.; Dierssen, U.; Beraza, N.; Linke, R.P.; Müller, M.; Blander, J.M.; Tacke, F.; Trautwein, C. Hepatic acute-phase proteins control innate immune responses during infection by promoting myeloid-derived suppressor cell function. J. Exp. Med. 2010, 207, 1453–1464. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Buchholz, B.M.; Shapiro, R.A.; Vodovotz, Y.; Billiar, T.R.; Sodhi, C.P.; Hackam, D.J.; Bauer, A.J. Myocyte TLR4 enhances enteric and systemic inflammation driving late murine endotoxic ileus. Am. J. Physiol. Gastrointest. Liver Physiol. 2015, 308, G852–G862. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Docsa, T.; Bhattarai, D.; Sipos, A.; Wade, C.E.; Cox, C.S., Jr.; Uray, K. CXCL1 is upregulated during the development of ileus resulting in decreased intestinal contractile activity. Neurogastroenterol. Motil. 2020, 32, e13757. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Papi, A.; Brightling, C.; Pedersen, S.E.; Reddel, H.K. Asthma. Lancet 2018, 391, 783–800. [Google Scholar] [CrossRef]
- Hosoki, K.; Ying, S.; Corrigan, C.; Qi, H.; Kurosky, A.; Jennings, K.; Sun, Q.; Boldogh, I.; Sur, S. Analysis of a Panel of 48 Cytokines in BAL Fluids Specifically Identifies IL-8 Levels as the Only Cytokine that Distinguishes Controlled Asthma from Uncontrolled Asthma, and Correlates Inversely with FEV1. PLoS ONE 2015, 10, e0126035. [Google Scholar] [CrossRef] [Green Version]
- Keglowich, L.; Roth, M.; Philippova, M.; Resink, T.; Tjin, G.; Oliver, B.; Lardinois, D.; Dessus-Babus, S.; Gosens, R.; Hostettler Haack, K.; et al. Bronchial smooth muscle cells of asthmatics promote angiogenesis through elevated secretion of CXC-chemokines (ENA-78, GRO-α, and IL-8). PLoS ONE 2013, 8, e81494. [Google Scholar] [CrossRef] [Green Version]
- Xu, S.; Chen, Z.; Ge, L.; Ma, C.; He, Q.; Liu, W.; Zhang, L.; Zhou, L. Identification of potential biomarkers and pathogenesis in neutrophil-predominant severe asthma: A comprehensive bioinformatics analysis. Medicine (Baltimore) 2022, 101, e30661. [Google Scholar] [CrossRef]
- Molet, S.; Hamid, Q.; Davoine, F.; Nutku, E.; Taha, R.; Pagé, N.; Olivenstein, R.; Elias, J.; Chakir, J. IL-17 is increased in asthmatic airways and induces human bronchial fibroblasts to produce cytokines. J. Allergy Clin. Immunol. 2001, 108, 430–438. [Google Scholar] [CrossRef]
- Fujie, H.; Niu, K.; Ohba, M.; Tomioka, Y.; Kitazawa, H.; Nagashima, K.; Ohrui, T.; Numasaki, M. A distinct regulatory role of Th17 cytokines IL-17A and IL-17F in chemokine secretion from lung microvascular endothelial cells. Inflammation 2012, 35, 1119–1131. [Google Scholar] [CrossRef]
- Huang, F.; Kao, C.Y.; Wachi, S.; Thai, P.; Ryu, J.; Wu, R. Requirement for both JAK-mediated PI3K signaling and ACT1/TRAF6/TAK1-dependent NF-kappaB activation by IL-17A in enhancing cytokine expression in human airway epithelial cells. J. Immunol. 2007, 179, 6504–6513. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Petering, H.; Götze, O.; Kimmig, D.; Smolarski, R.; Kapp, A.; Elsner, J. The biologic role of interleukin-8: Functional analysis and expression of CXCR1 and CXCR2 on human eosinophils. Blood 1999, 93, 694–702. [Google Scholar] [CrossRef] [PubMed]
- Al-Alwan, L.A.; Chang, Y.; Baglole, C.J.; Risse, P.A.; Halayko, A.J.; Martin, J.G.; Eidelman, D.H.; Hamid, Q. Autocrine-regulated airway smooth muscle cell migration is dependent on IL-17-induced growth-related oncogenes. J. Allergy Clin. Immunol. 2012, 130, 977–985. [Google Scholar] [CrossRef] [PubMed]
- Cao, J.; Ren, G.; Gong, Y.; Dong, S.; Yin, Y.; Zhang, L. Bronchial epithelial cells release IL-6, CXCL1 and CXCL8 upon mast cell interaction. Cytokine 2011, 56, 823–831. [Google Scholar] [CrossRef]
- Cheung, P.F.; Wong, C.K.; Lam, C.W. Molecular mechanisms of cytokine and chemokine release from eosinophils activated by IL-17A, IL-17F, and IL-23: Implication for Th17 lymphocytes-mediated allergic inflammation. J. Immunol. 2008, 180, 5625–5635. [Google Scholar] [CrossRef]
- Al-Alwan, L.A.; Chang, Y.; Rousseau, S.; Martin, J.G.; Eidelman, D.H.; Hamid, Q. CXCL1 inhibits airway smooth muscle cell migration through the decoy receptor Duffy antigen receptor for chemokines. J. Immunol. 2014, 193, 1416–1426. [Google Scholar] [CrossRef] [Green Version]
- Jones, C.P.; Pitchford, S.C.; Lloyd, C.M.; Rankin, S.M. CXCR2 mediates the recruitment of endothelial progenitor cells during allergic airways remodeling. Stem. Cells 2009, 27, 3074–3081. [Google Scholar] [CrossRef] [Green Version]
- Alkhouri, H.; Moir, L.M.; Armour, C.L.; Hughes, J.M. CXCL1 is a negative regulator of mast cell chemotaxis to airway smooth muscle cell products in vitro. Clin. Exp. Allergy 2014, 44, 381–392. [Google Scholar] [CrossRef]
- Bradding, P.; Arthur, G. Mast cells in asthma--state of the art. Clin. Exp. Allergy 2016, 46, 194–263. [Google Scholar] [CrossRef]
- Mannino, D.M.; Buist, A.S. Global burden of COPD: Risk factors, prevalence, and future trends. Lancet 2007, 370, 765–773. [Google Scholar] [CrossRef]
- Barnes, P.J. Inflammatory mechanisms in patients with chronic obstructive pulmonary disease. J. Allergy Clin. Immunol. 2016, 138, 16–27. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- López-Campos, J.L.; Tan, W.; Soriano, J.B. Global burden of COPD. Respirology 2016, 21, 14–23. [Google Scholar] [CrossRef] [PubMed]
- Traves, S.L.; Culpitt, S.V.; Russell, R.E.; Barnes, P.J.; Donnelly, L.E. Increased levels of the chemokines GROalpha and MCP-1 in sputum samples from patients with COPD. Thorax 2002, 57, 590–595. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Belitskaya-Levy, I.; Hajjou, M.; Su, W.C.; Yie, T.A.; Tchou-Wong, K.M.; Tang, M.S.; Goldberg, J.D.; Rom, W.N. Gene profiling of normal human bronchial epithelial cells in response to asbestos and benzo(a)pyrene diol epoxide (BPDE). J. Environ. Pathol. Toxicol. Oncol. 2007, 26, 281–294. [Google Scholar] [CrossRef]
- Tiwari, N.; Marudamuthu, A.S.; Tsukasaki, Y.; Ikebe, M.; Fu, J.; Shetty, S. p53- and PAI-1-mediated induction of C-X-C chemokines and CXCR2: Importance in pulmonary inflammation due to cigarette smoke exposure. Am. J. Physiol. Lung Cell Mol. Physiol. 2016, 310, L496–L506. [Google Scholar] [CrossRef]
- Inui, T.; Watanabe, M.; Nakamoto, K.; Sada, M.; Hirata, A.; Nakamura, M.; Honda, K.; Ogawa, Y.; Takata, S.; Yokoyama, T.; et al. Bronchial epithelial cells produce CXCL1 in response to LPS and TNFα: A potential role in the pathogenesis of COPD. Exp. Lung Res. 2018, 44, 323–331. [Google Scholar] [CrossRef]
- Li, P.; Peng, J.; Chen, G.; Chen, F.; Shen, Y.; Liu, L.; Chen, L. DNA Methylation Profiling in a Cigarette Smoke-Exposed Mouse Model of Airway Inflammation. Int. J. Chron. Obstruct. Pulmon. Dis. 2022, 17, 2443–2450. [Google Scholar] [CrossRef]
- Chen, W.; Xu, X.; Bai, L.; Padilla, M.T.; Gott, K.M.; Leng, S.; Tellez, C.S.; Wilder, J.A.; Belinsky, S.A.; Scott, B.R.; et al. Low-dose gamma-irradiation inhibits IL-6 secretion from human lung fibroblasts that promotes bronchial epithelial cell transformation by cigarette-smoke carcinogen. Carcinogenesis 2012, 33, 1368–1374. [Google Scholar] [CrossRef] [Green Version]
- Ovrevik, J.; Låg, M.; Holme, J.A.; Schwarze, P.E.; Refsnes, M. Cytokine and chemokine expression patterns in lung epithelial cells exposed to components characteristic of particulate air pollution. Toxicology 2009, 259, 46–53. [Google Scholar] [CrossRef]
- Watanabe, N.; Fujita, Y.; Nakayama, J.; Mori, Y.; Kadota, T.; Hayashi, Y.; Shimomura, I.; Ohtsuka, T.; Okamoto, K.; Araya, J.; et al. Anomalous Epithelial Variations and Ectopic Inflammatory Response in Chronic Obstructive Pulmonary Disease. Am. J. Respir. Cell Mol. Biol. 2022, 67, 708–719. [Google Scholar] [CrossRef]
- Chen, L.; Ge, Q.; Tjin, G.; Alkhouri, H.; Deng, L.; Brandsma, C.A.; Adcock, I.; Timens, W.; Postma, D.; Burgess, J.K.; et al. Effects of cigarette smoke extract on human airway smooth muscle cells in COPD. Eur. Respir. J. 2014, 44, 634–646. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kent, L.; Smyth, L.; Clayton, C.; Scott, L.; Cook, T.; Stephens, R.; Fox, S.; Hext, P.; Farrow, S.; Singh, D. Cigarette smoke extract induced cytokine and chemokine gene expression changes in COPD macrophages. Cytokine 2008, 42, 205–216. [Google Scholar] [CrossRef] [PubMed]
- Shaykhiev, R.; Krause, A.; Salit, J.; Strulovici-Barel, Y.; Harvey, B.G.; O’Connor, T.P.; Crystal, R.G. Smoking-dependent reprogramming of alveolar macrophage polarization: Implication for pathogenesis of chronic obstructive pulmonary disease. J. Immunol. 2009, 183, 2867–2883. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- da Silva, C.O.; Gicquel, T.; Daniel, Y.; Bártholo, T.; Vène, E.; Loyer, P.; Pôrto, L.C.; Lagente, V.; Victoni, T. Alteration of immunophenotype of human macrophages and monocytes after exposure to cigarette smoke. Sci. Rep. 2020, 10, 12796. [Google Scholar] [CrossRef] [PubMed]
- Traves, S.L.; Smith, S.J.; Barnes, P.J.; Donnelly, L.E. Specific CXC but not CC chemokines cause elevated monocyte migration in COPD: A role for CXCR2. J. Leukoc. Biol. 2004, 76, 441–450. [Google Scholar] [CrossRef] [PubMed]
- Sedaghat, A.R. Chronic Rhinosinusitis. Am. Fam. Physician 2017, 96, 500–506. [Google Scholar]
- Wang, H.; Pan, L.; Liu, Z. Neutrophils as a Protagonist and Target in Chronic Rhinosinusitis. Clin. Exp. Otorhinolaryngol. 2019, 12, 337–347. [Google Scholar] [CrossRef] [Green Version]
- Wang, H.; Li, Z.Y.; Jiang, W.X.; Liao, B.; Zhai, G.T.; Wang, N.; Zhen, Z.; Ruan, J.W.; Long, X.B.; Wang, H.; et al. The activation and function of IL-36γ in neutrophilic inflammation in chronic rhinosinusitis. J. Allergy Clin. Immunol. 2018, 141, 1646–1658. [Google Scholar] [CrossRef] [Green Version]
- Tsai, Y.J.; Hao, S.P.; Chen, C.L.; Wu, W.B. Thromboxane A2 Regulates CXCL1 and CXCL8 Chemokine Expression in the Nasal Mucosa-Derived Fibroblasts of Chronic Rhinosinusitis Patients. PLoS ONE 2016, 11, e0158438. [Google Scholar] [CrossRef] [Green Version]
- Rudack, C.; Steinhoff, M.; Mooren, F.; Buddenkotte, J.; Becker, K.; von Eiff, C.; Sachse, F. PAR-2 activation regulates IL-8 and GRO-alpha synthesis by NF-kappaB, but not RANTES, IL-6, eotaxin or TARC expression in nasal epithelium. Clin. Exp. Allergy 2007, 37, 1009–1022. [Google Scholar] [CrossRef]
- Sachse, F.; von Eiff, C.; Becker, K.; Steinhoff, M.; Rudack, C. Proinflammatory impact of Staphylococcus epidermidis on the nasal epithelium quantified by IL-8 and GRO-alpha responses in primary human nasal epithelial cells. Int. Arch. Allergy Immunol. 2008, 145, 24–32. [Google Scholar] [CrossRef] [PubMed]
- Huang, D.; Su, L.; He, C.; Chen, L.; Huang, D.; Peng, J.; Yang, F.; Cao, Y.; Luo, X. Pristimerin alleviates cigarette smoke-induced inflammation in chronic obstructive pulmonary disease via inhibiting NF-κB pathway. Biochem. Cell Biol. 2022, 100, 223–235. [Google Scholar] [CrossRef] [PubMed]
- Rostami, A.; Sepidarkish, M.; Leeflang, M.M.G.; Riahi, S.M.; Nourollahpour Shiadeh, M.; Esfandyari, S.; Mokdad, A.H.; Hotez, P.J.; Gasser, R.B. SARS-CoV-2 seroprevalence worldwide: A systematic review and meta-analysis. Clin. Microbiol. Infect. 2021, 27, 331–340. [Google Scholar] [CrossRef] [PubMed]
- Lin, X.; Fu, B.; Yin, S.; Li, Z.; Liu, H.; Zhang, H.; Xing, N.; Wang, Y.; Xue, W.; Xiong, Y.; et al. ORF8 contributes to cytokine storm during SARS-CoV-2 infection by activating IL-17 pathway. iScience 2021, 24, 102293. [Google Scholar] [CrossRef]
- Khan, S.; Shafiei, M.S.; Longoria, C.; Schoggins, J.W.; Savani, R.C.; Zaki, H. SARS-CoV-2 spike protein induces inflammation via TLR2-dependent activation of the NF-κB pathway. Elife 2021, 10, e68563. [Google Scholar] [CrossRef]
- Hasan, M.Z.; Islam, S.; Matsumoto, K.; Kawai, T. SARS-CoV-2 infection initiates interleukin-17-enriched transcriptional response in different cells from multiple organs. Sci. Rep. 2021, 11, 16814. [Google Scholar] [CrossRef]
- Chua, R.L.; Lukassen, S.; Trump, S.; Hennig, B.P.; Wendisch, D.; Pott, F.; Debnath, O.; Thürmann, L.; Kurth, F.; Völker, M.T.; et al. COVID-19 severity correlates with airway epithelium-immune cell interactions identified by single-cell analysis. Nat. Biotechnol. 2020, 38, 970–979. [Google Scholar] [CrossRef]
- Zaid, Y.; Doré, É.; Dubuc, I.; Archambault, A.S.; Flamand, O.; Laviolette, M.; Flamand, N.; Boilard, É.; Flamand, L. Chemokines and eicosanoids fuel the hyperinflammation within the lungs of patients with severe COVID-19. J. Allergy Clin. Immunol. 2021, 148, 368–380. [Google Scholar] [CrossRef]
- Korobova, Z.R.; Arsentieva, N.A.; Liubimova, N.E.; Dedkov, V.G.; Gladkikh, A.S.; Sharova, A.A.; Chernykh, E.I.; Kashchenko, V.A.; Ratnikov, V.A.; Gorelov, V.P.; et al. A Comparative Study of the Plasma Chemokine Profile in COVID-19 Patients Infected with Different SARS-CoV-2 Variants. Int. J. Mol. Sci. 2022, 23, 9058. [Google Scholar] [CrossRef]
- Martin, C.; Burdon, P.C.; Bridger, G.; Gutierrez-Ramos, J.C.; Williams, T.J.; Rankin, S.M. Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence. Immunity 2003, 19, 583–593. [Google Scholar] [CrossRef] [Green Version]
- Sun, S.; Cai, X.; Wang, H.; He, G.; Lin, Y.; Lu, B.; Chen, C.; Pan, Y.; Hu, X. Abnormalities of peripheral blood system in patients with COVID-19 in Wenzhou, China. Clin. Chim. Acta 2020, 507, 174–180. [Google Scholar] [CrossRef] [PubMed]
- Borges, L.; Pithon-Curi, T.C.; Curi, R.; Hatanaka, E. COVID-19 and Neutrophils: The Relationship between Hyperinflammation and Neutrophil Extracellular Traps. Mediators Inflamm. 2020, 2020, 8829674. [Google Scholar] [CrossRef] [PubMed]
- Veras, F.P.; Pontelli, M.C.; Silva, C.M.; Toller-Kawahisa, J.E.; de Lima, M.; Nascimento, D.C.; Schneider, A.H.; Caetité, D.; Tavares, L.A.; Paiva, I.M.; et al. SARS-CoV-2-triggered neutrophil extracellular traps mediate COVID-19 pathology. J. Exp. Med. 2020, 217, e20201129. [Google Scholar] [CrossRef] [PubMed]
- Liu, J.; Liu, Y.; Xiang, P.; Pu, L.; Xiong, H.; Li, C.; Zhang, M.; Tan, J.; Xu, Y.; Song, R.; et al. Neutrophil-to-lymphocyte ratio predicts critical illness patients with 2019 coronavirus disease in the early stage. J. Transl. Med. 2020, 18, 206. [Google Scholar] [CrossRef] [PubMed]
- Yang, Y.; Wang, S.; Xie, X.; Li, J.; Zhang, R. Change of gene expression profiles in human cardiomyocytes and macrophages infected with SARS-CoV-2 and its significance. Zhong Nan Da Xue Xue Bao Yi Xue Ban 2021, 46, 1203–1211. [Google Scholar]
- Javanian, M.; Barary, M.; Ghebrehewet, S.; Koppolu, V.; Vasigala, V.; Ebrahimpour, S. A brief review of influenza virus infection. J. Med. Virol. 2021, 93, 4638–4646. [Google Scholar] [CrossRef]
- Pleschka, S. Overview of influenza viruses. Curr. Top Microbiol. Immunol. 2013, 370, 1–20. [Google Scholar]
- Collin, E.A.; Sheng, Z.; Lang, Y.; Ma, W.; Hause, B.M.; Li, F. Cocirculation of two distinct genetic and antigenic lineages of proposed influenza D virus in cattle. J. Virol. 2015, 89, 1036–1042. [Google Scholar] [CrossRef]
- Sederdahl, B.K.; Williams, J.V. Epidemiology and Clinical Characteristics of Influenza C Virus. Viruses 2020, 12, 89. [Google Scholar] [CrossRef] [Green Version]
- Kulkarni, U.; Zemans, R.L.; Smith, C.A.; Wood, S.C.; Deng, J.C.; Goldstein, D.R. Excessive neutrophil levels in the lung underlie the age-associated increase in influenza mortality. Mucosal. Immunol. 2019, 12, 545–554. [Google Scholar] [CrossRef] [Green Version]
- Mai, E.; Percopo, C.M.; Limkar, A.R.; Sek, A.C.; Ma, M.; Rosenberg, H.F. Respiratory Epithelial Cells Respond to Lactobacillus plantarum but Provide No Cross-Protection against Virus-Induced Inflammation. Viruses 2020, 13, 2. [Google Scholar] [CrossRef] [PubMed]
- Hornick, E.E.; Banoth, B.; Miller, A.M.; Zacharias, Z.R.; Jain, N.; Wilson, M.E.; Gibson-Corley, K.N.; Legge, K.L.; Bishop, G.A.; Sutterwala, F.S.; et al. Nlrp12 Mediates Adverse Neutrophil Recruitment during Influenza Virus Infection. J. Immunol. 2018, 200, 1188–1197. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tavares, L.P.; Garcia, C.C.; Machado, M.G.; Queiroz-Junior, C.M.; Barthelemy, A.; Trottein, F.; Siqueira, M.M.; Brandolini, L.; Allegretti, M.; Machado, A.M.; et al. CXCR1/2 Antagonism Is Protective during Influenza and Post-Influenza Pneumococcal Infection. Front. Immunol. 2017, 8, 1799. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Robinson, D.P.; Hall, O.J.; Nilles, T.L.; Bream, J.H.; Klein, S.L. 17β-estradiol protects females against influenza by recruiting neutrophils and increasing virus-specific CD8 T cell responses in the lungs. J. Virol. 2014, 88, 4711–4720. [Google Scholar] [CrossRef] [Green Version]
- Turianová, L.; Lachová, V.; Beňová, K.; Kostrábová, A.; Betáková, T. Influenza A virus lacking the effector and C terminal domains of NS1 protein induces cytokines associated with high pathogenicity in mice. Acta Virol. 2020, 64, 78–87. [Google Scholar] [CrossRef]
- Tobin, J.M.; Nickolich, K.L.; Ramanan, K.; Pilewski, M.J.; Lamens, K.D.; Alcorn, J.F.; Robinson, K.M. Influenza Suppresses Neutrophil Recruitment to the Lung and Exacerbates Secondary Invasive Pulmonary Aspergillosis. J. Immunol. 2020, 205, 480–488. [Google Scholar] [CrossRef]
- Sharma, A.K.; Mulloy, D.P.; Le, L.T.; Laubach, V.E. NADPH oxidase mediates synergistic effects of IL-17 and TNF-α on CXCL1 expression by epithelial cells after lung ischemia-reperfusion. Am. J. Physiol. Lung Cell Mol. Physiol. 2014, 306, L69–L79. [Google Scholar] [CrossRef]
- Belperio, J.A.; Keane, M.P.; Burdick, M.D.; Gomperts, B.N.; Xue, Y.Y.; Hong, K.; Mestas, J.; Zisman, D.; Ardehali, A.; Saggar, R.; et al. CXCR2/CXCR2 ligand biology during lung transplant ischemia-reperfusion injury. J. Immunol. 2005, 175, 6931–6939. [Google Scholar] [CrossRef]
- Lee, A.C.H.; Edobor, A.; Wigakumar, T.; Lysandrou, M.; Johnston, L.K.; McMullen, P.; Mirle, V.; Diaz, A.; Piech, R.; Rose, R.; et al. Donor leukocyte trafficking during human ex vivo lung perfusion. Clin. Transplant. 2022, 36, e14670. [Google Scholar] [CrossRef]
- Dheda, K.; Barry, C.E., 3rd; Maartens, G. Tuberculosis. Lancet 2016, 387, 1211–1226. [Google Scholar] [CrossRef]
- Kumar, N.P.; Moideen, K.; Nancy, A.; Viswanathan, V.; Shruthi, B.S.; Sivakumar, S.; Natarajan, M.; Kornfeld, H.; Babu, S. Plasma chemokines are biomarkers of disease severity, higher bacterial burden and delayed sputum culture conversion in pulmonary tuberculosis. Sci. Rep. 2019, 9, 18217. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Koyuncu, D.; Niazi, M.K.K.; Tavolara, T.; Abeijon, C.; Ginese, M.L.; Liao, Y.; Mark, C.; Specht, A.; Gower, A.C.; Restrepo, B.I.; et al. CXCL1: A new diagnostic biomarker for human tuberculosis discovered using Diversity Outbred mice. PLoS Pathog. 2021, 17, e1009773. [Google Scholar] [CrossRef] [PubMed]
- Kumar, N.P.; Hissar, S.; Thiruvengadam, K.; Banurekha, V.V.; Balaji, S.; Elilarasi, S.; Gomathi, N.S.; Ganesh, J.; Aravind, M.A.; Baskaran, D.; et al. Plasma chemokines as immune biomarkers for diagnosis of pediatric tuberculosis. BMC Infect. Dis. 2021, 21, 1055. [Google Scholar] [CrossRef] [PubMed]
- Kumar, N.P.; Moideen, K.; Nancy, A.; Viswanathan, V.; Thiruvengadam, K.; Nair, D.; Banurekha, V.V.; Sivakumar, S.; Hissar, S.; Kornfeld, H.; et al. Plasma Chemokines Are Baseline Predictors of Unfavorable Treatment Outcomes in Pulmonary Tuberculosis. Clin. Infect. Dis. 2021, 73, e3419–e3427. [Google Scholar] [CrossRef] [PubMed]
- Abu El-Asrar, A.M.; Struyf, S.; Kangave, D.; Al-Obeidan, S.A.; Opdenakker, G.; Geboes, K.; Van Damme, J. Cytokine and CXC chemokine expression patterns in aqueous humor of patients with presumed tuberculous uveitis. Cytokine 2012, 59, 377–381. [Google Scholar] [CrossRef] [PubMed]
- Dorhoi, A.; Yeremeev, V.; Nouailles, G.; Weiner, J., 3rd; Jörg, S.; Heinemann, E.; Oberbeck-Müller, D.; Knaul, J.K.; Vogelzang, A.; Reece, S.T.; et al. Type I IFN signaling triggers immunopathology in tuberculosis-susceptible mice by modulating lung phagocyte dynamics. Eur. J. Immunol. 2014, 44, 2380–2393. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lombard, R.; Doz, E.; Carreras, F.; Epardaud, M.; Le Vern, Y.; Buzoni-Gatel, D.; Winter, N. IL-17RA in Non-Hematopoietic Cells Controls CXCL-1 and 5 Critical to Recruit Neutrophils to the Lung of Mycobacteria-Infected Mice during the Adaptive Immune Response. PLoS ONE 2016, 11, e0149455. [Google Scholar] [CrossRef] [Green Version]
- Niazi, M.K.; Dhulekar, N.; Schmidt, D.; Major, S.; Cooper, R.; Abeijon, C.; Gatti, D.M.; Kramnik, I.; Yener, B.; Gurcan, M.; et al. Lung necrosis and neutrophils reflect common pathways of susceptibility to Mycobacterium tuberculosis in genetically diverse, immune-competent mice. Dis. Model Mech. 2015, 8, 1141–1153. [Google Scholar] [CrossRef]
- Seiler, P.; Aichele, P.; Bandermann, S.; Hauser, A.E.; Lu, B.; Gerard, N.P.; Gerard, C.; Ehlers, S.; Mollenkopf, H.J.; Kaufmann, S.H. Early granuloma formation after aerosol Mycobacterium tuberculosis infection is regulated by neutrophils via CXCR3-signaling chemokines. Eur. J. Immunol. 2003, 33, 2676–2686. [Google Scholar] [CrossRef]
- Ramakrishnan, L. Revisiting the role of the granuloma in tuberculosis. Nat. Rev. Immunol. 2012, 12, 352–366. [Google Scholar] [CrossRef]
- Wolf, A.J.; Linas, B.; Trevejo-Nuñez, G.J.; Kincaid, E.; Tamura, T.; Takatsu, K.; Ernst, J.D. Mycobacterium tuberculosis infects dendritic cells with high frequency and impairs their function in vivo. J. Immunol. 2007, 179, 2509–2519. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Doz, E.; Lombard, R.; Carreras, F.; Buzoni-Gatel, D.; Winter, N. Mycobacteria-infected dendritic cells attract neutrophils that produce IL-10 and specifically shut down Th17 CD4 T cells through their IL-10 receptor. J. Immunol. 2013, 191, 3818–3826. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Boro, M.; Singh, V.; Balaji, K.N. Mycobacterium tuberculosis-triggered Hippo pathway orchestrates CXCL1/2 expression to modulate host immune responses. Sci. Rep. 2016, 6, 37695. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Boro, M.; Balaji, K.N. CXCL1 and CXCL2 Regulate NLRP3 Inflammasome Activation via G-Protein-Coupled Receptor CXCR2. J. Immunol. 2017, 199, 1660–1671. [Google Scholar] [CrossRef]
- Rennekampff, H.O.; Hansbrough, J.F.; Woods, V., Jr.; Doré, C.; Kiessig, V.; Schröder, J.M. Role of melanoma growth stimulatory activity (MGSA/gro) on keratinocyte function in wound healing. Arch. Dermatol. Res. 1997, 289, 204–212. [Google Scholar] [CrossRef]
- Kroeze, K.L.; Boink, M.A.; Sampat-Sardjoepersad, S.C.; Waaijman, T.; Scheper, R.J.; Gibbs, S. Autocrine regulation of re-epithelialization after wounding by chemokine receptors CCR1, CCR10, CXCR1, CXCR2, and CXCR3. J. Investig. Dermatol. 2012, 132, 216–225. [Google Scholar] [CrossRef] [Green Version]
- Li, J.; Thornhill, M.H. Growth-regulated peptide-alpha (GRO-alpha) production by oral keratinocytes: A comparison with skin keratinocytes. Cytokine 2000, 12, 1409–1413. [Google Scholar] [CrossRef]
- Hasegawa, M.; Higashi, K.; Matsushita, T.; Hamaguchi, Y.; Saito, K.; Fujimoto, M.; Takehara, K. Dermokine inhibits ELR(+)CXC chemokine expression and delays early skin wound healing. J. Dermatol. Sci. 2013, 70, 34–41. [Google Scholar] [CrossRef]
- Griffiths, C.E.M.; Armstrong, A.W.; Gudjonsson, J.E.; Barker, J.N.W.N. Psoriasis. Lancet 2021, 397, 1301–1315. [Google Scholar] [CrossRef]
- Parisi, R.; Iskandar, I.Y.K.; Kontopantelis, E.; Augustin, M.; Griffiths, C.E.M.; Ashcroft, D.M. Global Psoriasis Atlas. National, regional, and worldwide epidemiology of psoriasis: Systematic analysis and modelling study. BMJ 2020, 369, m1590. [Google Scholar] [CrossRef]
- Zou, A.; Jian, Q. CXCL10 and its related key genes as potential biomarkers for psoriasis: Evidence from bioinformatics and real-time quantitative polymerase chain reaction. Medicine (Baltimore) 2021, 100, e27365. [Google Scholar] [CrossRef] [PubMed]
- Kojima, T.; Cromie, M.A.; Fisher, G.J.; Voorhees, J.J.; Elder, J.T. GRO-alpha mRNA is selectively overexpressed in psoriatic epidermis and is reduced by cyclosporin A in vivo, but not in cultured keratinocytes. J. Investig. Dermatol. 1993, 101, 767–772. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gillitzer, R.; Ritter, U.; Spandau, U.; Goebeler, M.; Bröcker, E.B. Differential expression of GRO-alpha and IL-8 mRNA in psoriasis: A model for neutrophil migration and accumulation in vivo. J. Investig. Dermatol. 1996, 107, 778–782. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kulke, R.; Tödt-Pingel, I.; Rademacher, D.; Röwert, J.; Schröder, J.M.; Christophers, E. Co-localized overexpression of GRO-alpha and IL-8 mRNA is restricted to the suprapapillary layers of psoriatic lesions. J. Investig. Dermatol. 1996, 106, 526–530. [Google Scholar] [CrossRef] [Green Version]
- Pohl, D.; Andrýs, C.; Borská, L.; Fiala, Z.; Hamáková, K.; Ettler, K.; Krejsek, J. CC and CXC chemokines patterns in psoriasis determined by protein array method were influenced by Goeckerman’s therapy. Acta Medica (Hradec Kralove) 2009, 52, 9–13. [Google Scholar] [CrossRef] [Green Version]
- Kato, Y.; Yamamoto, T. Increased serum levels of growth-related oncogene-alpha in patients with generalized pustular psoriasis. Dermatology 2010, 220, 46–48. [Google Scholar] [CrossRef]
- Yamamoto, M.; Imai, Y.; Sakaguchi, Y.; Haneda, T.; Yamanishi, K. Serum cytokines correlated with the disease severity of generalized pustular psoriasis. Dis. Markers 2013, 34, 153–161. [Google Scholar] [CrossRef]
- Choudhary, S.; Anand, R.; Pradhan, D.; Bastia, B.; Kumar, S.N.; Singh, H.; Puri, P.; Thomas, G.; Jain, A.K. Transcriptomic landscaping of core genes and pathways of mild and severe psoriasis vulgaris. Int. J. Mol. Med. 2021, 47, 219–231. [Google Scholar] [CrossRef]
- Albanesi, C.; Scarponi, C.; Cavani, A.; Federici, M.; Nasorri, F.; Girolomoni, G. Interleukin-17 is produced by both Th1 and Th2 lymphocytes, and modulates interferon-gamma- and interleukin-4-induced activation of human keratinocytes. J. Investig. Dermatol. 2000, 115, 81–87. [Google Scholar] [CrossRef]
- Nograles, K.E.; Zaba, L.C.; Guttman-Yassky, E.; Fuentes-Duculan, J.; Suárez-Fariñas, M.; Cardinale, I.; Khatcherian, A.; Gonzalez, J.; Pierson, K.C.; White, T.R.; et al. Th17 cytokines interleukin (IL)-17 and IL-22 modulate distinct inflammatory and keratinocyte-response pathways. Br. J. Dermatol. 2008, 159, 1092–1102. [Google Scholar] [CrossRef] [Green Version]
- Takei-Taniguchi, R.; Imai, Y.; Ishikawa, C.; Sakaguchi, Y.; Nakagawa, N.; Tsuda, T.; Hollenberg, M.D.; Yamanishi, K. Interleukin-17- and protease-activated receptor 2-mediated production of CXCL1 and CXCL8 modulated by cyclosporine A, vitamin D3 and glucocorticoids in human keratinocytes. J. Dermatol. 2012, 39, 625–631. [Google Scholar] [CrossRef] [PubMed]
- Wang, C.Q.F.; Akalu, Y.T.; Suarez-Farinas, M.; Gonzalez, J.; Mitsui, H.; Lowes, M.A.; Orlow, S.J.; Manga, P.; Krueger, J.G. IL-17 and TNF synergistically modulate cytokine expression while suppressing melanogenesis: Potential relevance to psoriasis. J. Investig. Dermatol. 2013, 133, 2741–2752. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Reich, K.; Papp, K.A.; Matheson, R.T.; Tu, J.H.; Bissonnette, R.; Bourcier, M.; Gratton, D.; Kunynetz, R.A.; Poulin, Y.; Rosoph, L.A.; et al. Evidence that a neutrophil-keratinocyte crosstalk is an early target of IL-17A inhibition in psoriasis. Exp. Dermatol. 2015, 24, 529–535. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, N.; Yamasaki, K.; Saito, R.; Fukushi-Takahashi, S.; Shimada-Omori, R.; Asano, M.; Aiba, S. Alarmin function of cathelicidin antimicrobial peptide LL37 through IL-36γ induction in human epidermal keratinocytes. J. Immunol. 2014, 193, 5140–5148. [Google Scholar] [CrossRef] [Green Version]
- Guo, J.; Tu, J.; Hu, Y.; Song, G.; Yin, Z. Cathepsin G cleaves and activates IL-36γ and promotes the inflammation of psoriasis. Drug Des. Devel. Ther. 2019, 13, 581–588. [Google Scholar] [CrossRef] [Green Version]
- Xu, N.; Meisgen, F.; Butler, L.M.; Han, G.; Wang, X.J.; Söderberg-Nauclér, C.; Ståhle, M.; Pivarcsi, A.; Sonkoly, E. MicroRNA-31 is overexpressed in psoriasis and modulates inflammatory cytokine and chemokine production in keratinocytes via targeting serine/threonine kinase 40. J. Immunol. 2013, 190, 678–688. [Google Scholar] [CrossRef] [Green Version]
- Bordoni, R.; Fine, R.; Murray, D.; Richmond, A. Characterization of the role of melanoma growth stimulatory activity (MGSA) in the growth of normal melanocytes, nevocytes, and malignant melanocytes. J. Cell Biochem. 1990, 44, 207–219. [Google Scholar] [CrossRef]
- Mockenhaupt, M.; Peters, F.; Schwenk-Davoine, I.; Herouy, Y.; Schraufstätter, I.; Elsner, P.; Norgauer, J. Evidence of involvement of CXC-chemokines in proliferation of cultivated human melanocytes. Int. J. Mol. Med. 2003, 12, 597–601. [Google Scholar] [CrossRef]
- Zhang, Y.; Zeng, H.; Hu, Y.; Jiang, L.; Fu, C.; Zhang, L.; Zhang, F.; Zhang, X.; Zhu, L.; Huang, J.; et al. Establishment and validation of evaluation models for post-inflammatory pigmentation abnormalities. Front. Immunol. 2022, 13, 991594. [Google Scholar] [CrossRef] [PubMed]
- Chiang, C.C.; Cheng, W.J.; Korinek, M.; Lin, C.Y.; Hwang, T.L. Neutrophils in Psoriasis. Front. Immunol. 2019, 10, 2376. [Google Scholar] [CrossRef]
- Schopf, R.E.; Altmeyer, P.; Lemmel, E.M. Increased respiratory burst activity of monocytes and polymorphonuclear leukocytes in psoriasis. Br. J. Dermatol. 1982, 107, 505–510. [Google Scholar] [CrossRef] [PubMed]
- Dilek, N.; Dilek, A.R.; Taşkın, Y.; Erkinüresin, T.; Yalçın, Ö.; Saral, Y. Contribution of myeloperoxidase and inducible nitric oxide synthase to pathogenesis of psoriasis. Postepy Dermatol. Alergol. 2016, 33, 435–439. [Google Scholar] [CrossRef] [Green Version]
- Res, P.C.; Piskin, G.; de Boer, O.J.; van der Loos, C.M.; Teeling, P.; Bos, J.D.; Teunissen, M.B. Overrepresentation of IL-17A and IL-22 producing CD8 T cells in lesional skin suggests their involvement in the pathogenesis of psoriasis. PLoS ONE 2010, 5, e14108. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lin, A.M.; Rubin, C.J.; Khandpur, R.; Wang, J.; Riblett, M.; Yalavarthi, S.; Villanueva, E.C.; Shah, P.; Kaplan, M.J.; Bruce, A.T. Mast cells and neutrophils release IL-17 through extracellular trap formation in psoriasis. J. Immunol. 2011, 187, 490–500. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Liu, X.T.; Shi, Z.R.; Lu, S.Y.; Hong, D.; Qiu, X.N.; Tan, G.Z.; Xiong, H.; Guo, Q.; Wang, L. Enhanced Migratory Ability of Neutrophils Toward Epidermis Contributes to the Development of Psoriasis via Crosstalk With Keratinocytes by Releasing IL-17A. Front. Immunol. 2022, 13, 817040. [Google Scholar] [CrossRef] [PubMed]
- Lambert, S.; Hambro, C.A.; Johnston, A.; Stuart, P.E.; Tsoi, L.C.; Nair, R.P.; Elder, J.T. Neutrophil Extracellular Traps Induce Human Th17 Cells: Effect of Psoriasis-Associated TRAF3IP2 Genotype. J. Investig. Dermatol. 2019, 139, 1245–1253. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Shao, S.; Fang, H.; Dang, E.; Xue, K.; Zhang, J.; Li, B.; Qiao, H.; Cao, T.; Zhuang, Y.; Shen, S.; et al. Neutrophil Extracellular Traps Promote Inflammatory Responses in Psoriasis via Activating Epidermal TLR4/IL-36R Crosstalk. Front. Immunol. 2019, 10, 746. [Google Scholar] [CrossRef] [Green Version]
- Herster, F.; Bittner, Z.; Archer, N.K.; Dickhöfer, S.; Eisel, D.; Eigenbrod, T.; Knorpp, T.; Schneiderhan-Marra, N.; Löffler, M.W.; Kalbacher, H.; et al. Neutrophil extracellular trap-associated RNA and LL37 enable self-amplifying inflammation in psoriasis. Nat. Commun. 2020, 11, 105. [Google Scholar] [CrossRef]
- Dürr, U.H.; Sudheendra, U.S.; Ramamoorthy, A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta 2006, 1758, 1408–1425. [Google Scholar] [CrossRef] [Green Version]
- Kim, J.E.; Kim, B.J.; Jeong, M.S.; Seo, S.J.; Kim, M.N.; Hong, C.K.; Ro, B.I. Expression and modulation of LL-37 in normal human keratinocytes, HaCaT cells, and inflammatory skin diseases. J. Korean Med. Sci. 2005, 20, 649–654. [Google Scholar] [CrossRef] [Green Version]
- Meyer-Hoffert, U.; Wingertszahn, J.; Wiedow, O. Human leukocyte elastase induces keratinocyte proliferation by epidermal growth factor receptor activation. J. Investig. Dermatol. 2004, 123, 338–345. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- D’Erme, A.M.; Wilsmann-Theis, D.; Wagenpfeil, J.; Hölzel, M.; Ferring-Schmitt, S.; Sternberg, S.; Wittmann, M.; Peters, B.; Bosio, A.; Bieber, T.; et al. IL-36γ (IL-1F9) is a biomarker for psoriasis skin lesions. J. Investig. Dermatol. 2015, 135, 1025–1032. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wang, W.; Yu, X.; Wu, C.; Jin, H. IL-36γ inhibits differentiation and induces inflammation of keratinocyte via Wnt signaling pathway in psoriasis. Int. J. Med. Sci. 2017, 14, 1002–1007. [Google Scholar] [CrossRef] [Green Version]
- Nguyen, C.T.; Furuya, H.; Das, D.; Marusina, A.I.; Merleev, A.A.; Ravindran, R.; Jalali, Z.; Khan, I.H.; Maverakis, E.; Adamopoulos, I.E. Peripheral γδ T Cells Regulate Neutrophil Expansion and Recruitment in Experimental Psoriatic Arthritis. Arthritis Rheumatol. 2022, 74, 1524–1534. [Google Scholar] [CrossRef]
- Kennedy Crispin, M.; Fuentes-Duculan, J.; Gulati, N.; Johnson-Huang, L.M.; Lentini, T.; Sullivan-Whalen, M.; Gilleaudeau, P.; Cueto, I.; Suárez-Fariñas, M.; Lowes, M.A.; et al. Gene profiling of narrowband UVB-induced skin injury defines cellular and molecular innate immune responses. J. Investig. Dermatol. 2013, 133, 692–701. [Google Scholar] [CrossRef] [Green Version]
- Oka, M.; Edamatsu, H.; Kunisada, M.; Hu, L.; Takenaka, N.; Sakaguchi, M.; Kataoka, T.; Nishigori, C. Phospholipase Cε has a crucial role in ultraviolet B-induced neutrophil-associated skin inflammation by regulating the expression of CXCL1/KC. Lab. Investig. 2011, 91, 711–718. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Black, J.O. Xeroderma Pigmentosum. Head Neck Pathol. 2016, 10, 139–144. [Google Scholar] [CrossRef] [Green Version]
- Kunisada, M.; Hosaka, C.; Takemori, C.; Nakano, E.; Nishigori, C. CXCL1 Inhibition Regulates UVB-Induced Skin Inflammation and Tumorigenesis in Xpa-Deficient Mice. J. Investig. Dermatol. 2017, 137, 1975–1983. [Google Scholar] [CrossRef]
- Deftu, A.F.; Filippi, A.; Shibsaki, K.; Gheorghe, R.O.; Chiritoiu, M.; Ristoiu, V. Chemokine (C-X-C motif) ligand 1 (CXCL1) and chemokine (C-X-C motif) ligand 2 (CXCL2) modulate the activity of TRPV1+/IB4+ cultured rat dorsal root ganglia neurons upon short-term and acute application. J. Physiol. Pharmacol. 2017, 68, 385–395. [Google Scholar]
- Deftu, A.F.; Filippi, A.; Gheorghe, R.O.; Ristoiu, V. CXCL1 activates TRPV1 via Gi/o protein and actin filaments. Life Sci. 2018, 193, 282–291. [Google Scholar] [CrossRef]
- Zenobia, C.; Luo, X.L.; Hashim, A.; Abe, T.; Jin, L.; Chang, Y.; Jin, Z.C.; Sun, J.X.; Hajishengallis, G.; Curtis, M.A.; et al. Commensal bacteria-dependent select expression of CXCL2 contributes to periodontal tissue homeostasis. Cell Microbiol. 2013, 15, 1419–1426. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rath-Deschner, B.; Memmert, S.; Damanaki, A.; Nokhbehsaim, M.; Eick, S.; Cirelli, J.A.; Götz, W.; Deschner, J.; Jäger, A.; Nogueira, A.V.B. CXCL1, CCL2, and CCL5 modulation by microbial and biomechanical signals in periodontal cells and tissues-in vitro and in vivo studies. Clin. Oral. Investig. 2020, 24, 3661–3670. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Miyake, M.; Furuya, H.; Onishi, S.; Hokutan, K.; Anai, S.; Chan, O.; Shi, S.; Fujimoto, K.; Goodison, S.; Cai, W.; et al. Monoclonal Antibody against CXCL1 (HL2401) as a Novel Agent in Suppressing IL6 Expression and Tumoral Growth. Theranostics 2019, 9, 853–867. [Google Scholar] [CrossRef] [PubMed]
- Furuya, M.; Suyama, T.; Usui, H.; Kasuya, Y.; Nishiyama, M.; Tanaka, N.; Ishiwata, I.; Nagai, Y.; Shozu, M.; Kimura, S. Up-regulation of CXC chemokines and their receptors: Implications for proinflammatory microenvironments of ovarian carcinomas and endometriosis. Hum. Pathol. 2007, 38, 1676–1687. [Google Scholar] [CrossRef]
- Greene, S.; Robbins, Y.; Mydlarz, W.K.; Huynh, A.P.; Schmitt, N.C.; Friedman, J.; Horn, L.A.; Palena, C.; Schlom, J.; Maeda, D.Y.; et al. Inhibition of MDSC Trafficking with SX-682, a CXCR1/2 Inhibitor, Enhances NK-Cell Immunotherapy in Head and Neck Cancer Models. Clin. Cancer Res. 2020, 26, 1420–1431. [Google Scholar] [CrossRef] [Green Version]
- Kim, J.H.; Lee, S.J.; Kang, K.W.; Lee, B.H.; Park, Y.; Kim, B.S. CXCR2, a novel target to overcome tyrosine kinase inhibitor resistance in chronic myelogenous leukemia cells. Biochem. Pharmacol. 2021, 190, 114658. [Google Scholar] [CrossRef]
- Zhu, F.; He, H.; Fan, L.; Ma, C.; Xu, Z.; Xue, Y.; Wang, Y.; Zhang, C.; Zhou, G. Blockade of CXCR2 suppresses proinflammatory activities of neutrophils in ulcerative colitis. Am. J. Transl. Res. 2020, 12, 5237–5251. [Google Scholar]
- Castelli, V.; Brandolini, L.; d’Angelo, M.; Giorgio, C.; Alfonsetti, M.; Cocchiaro, P.; Lombardi, F.; Cimini, A.; Allegretti, M. CXCR1/2 Inhibitor Ladarixin Ameliorates the Insulin Resistance of 3T3-L1 Adipocytes by Inhibiting Inflammation and Improving Insulin Signaling. Cells 2021, 10, 2324. [Google Scholar] [CrossRef]
- Kostic, M.; Dzopalic, T.; Zivanovic, S.; Zivkovic, N.; Cvetanovic, A.; Stojanovic, I.; Vojinovic, S.; Marjanovic, G.; Savic, V.; Colic, M. IL-17 and glutamate excitotoxicity in the pathogenesis of multiple sclerosis. Scand. J. Immunol. 2014, 79, 181–186. [Google Scholar] [CrossRef]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. |
© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Korbecki, J.; Maruszewska, A.; Bosiacki, M.; Chlubek, D.; Baranowska-Bosiacka, I. The Potential Importance of CXCL1 in the Physiological State and in Noncancer Diseases of the Cardiovascular System, Respiratory System and Skin. Int. J. Mol. Sci. 2023, 24, 205. https://doi.org/10.3390/ijms24010205
Korbecki J, Maruszewska A, Bosiacki M, Chlubek D, Baranowska-Bosiacka I. The Potential Importance of CXCL1 in the Physiological State and in Noncancer Diseases of the Cardiovascular System, Respiratory System and Skin. International Journal of Molecular Sciences. 2023; 24(1):205. https://doi.org/10.3390/ijms24010205
Chicago/Turabian StyleKorbecki, Jan, Agnieszka Maruszewska, Mateusz Bosiacki, Dariusz Chlubek, and Irena Baranowska-Bosiacka. 2023. "The Potential Importance of CXCL1 in the Physiological State and in Noncancer Diseases of the Cardiovascular System, Respiratory System and Skin" International Journal of Molecular Sciences 24, no. 1: 205. https://doi.org/10.3390/ijms24010205