Glucose 6-phosphate dehydrogenase knockdown enhances IL-8 expression in HepG2 cells via oxidative stress and NF-κB signaling pathway
Tóm tắt
Từ khóa
Tài liệu tham khảo
Arese P, Gallo V, Pantaleo A, Turrini F. Life and Death of Glucose-6-Phosphate Dehydrogenase (G6PD) Deficient Erythrocytes - Role of Redox Stress and Band 3 Modifications. Transfus Med Hemother. 2012;39:328–34.
Ho HY, Cheng ML, Chiu DT. Glucose-6-phosphate dehydrogenase - beyond the realm of red cell biology. Free Radic Res. 2014;48:1028–48.
Scott MD, Zuo L, Lubin BH, Chiu DT. NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. Blood. 1991;77:2059–64.
Beutler E. Glucose-6-phosphate dehydrogenase deficiency: a historical perspective. Blood. 2008;111:16–24.
Lin HR, Wu CC, Wu YH, Hsu CW, Cheng ML, Chiu DT. Proteome-wide dysregulation by glucose-6-phosphate dehydrogenase (G6PD) reveals a novel protective role for G6PD in aflatoxin B(1)-mediated cytotoxicity. J Proteome Res. 2013;12:3434–48.
Lin CJ, Ho HY, Cheng ML, You TH, Yu JS, Chiu DT. Impaired dephosphorylation renders G6PD-knockdown HepG2 cells more susceptible to H(2)O(2)-induced apoptosis. Free Radic Biol Med. 2010;49:361–73.
Gao LP, Cheng ML, Chou HJ, Yang YH, Ho HY, Chiu DT. Ineffective GSH regeneration enhances G6PD-knockdown Hep G2 cell sensitivity to diamide-induced oxidative damage. Free Radic Biol Med. 2009;47:529–35.
Cheng ML, Ho HY, Liang CM, Chou YH, Stern A, Lu FJ, et al. Cellular glucose-6-phosphate dehydrogenase (G6PD) status modulates the effects of nitric oxide (NO) on human foreskin fibroblasts. FEBS Lett. 2000;475:257–62.
Cheng ML, Ho HY, Lin HY, Lai YC, Chiu DT. Effective NET formation in neutrophils from individuals with G6PD Taiwan-Hakka is associated with enhanced NADP(+) biosynthesis. Free Radic Res. 2013;47:699–709.
Cheng ML, Ho HY, Wu YH, Chiu DT. Glucose-6-phosphate dehydrogenase-deficient cells show an increased propensity for oxidant-induced senescence. Free Radic Biol Med. 2004;36:580–91.
Ho HY, Cheng ML, Shiao MS, Chiu DT. Characterization of global metabolic responses of glucose-6-phosphate dehydrogenase-deficient hepatoma cells to diamide-induced oxidative stress. Free Radic Biol Med. 2013;54:71–84.
Gostner JM, Becker K, Fuchs D, Sucher R. Redox regulation of the immune response. Redox Rep. 2013;18:88–94.
Padgett LE, Broniowska KA, Hansen PA, Corbett JA, Tse HM. The role of reactive oxygen species and proinflammatory cytokines in type 1 diabetes pathogenesis. Ann N Y Acad Sci. 2013;1281:16–35.
Rolo AP, Teodoro JS, Palmeira CM. Role of oxidative stress in the pathogenesis of nonalcoholic steatohepatitis. Free Radic Biol Med. 2012;52:59–69.
Russo RC, Garcia CC, Teixeira MM, Amaral FA. The CXCL8/IL-8 chemokine family and its receptors in inflammatory diseases. Expert Rev Clin Immunol. 2014;10:593–619.
He W, Qu T, Yu Q, Wang Z, Lv H, Zhang J, et al. LPS induces IL-8 expression through TLR4, MyD88, NF-kappaB and MAPK pathways in human dental pulp stem cells. Int Endod J. 2013;46:128–36.
Liebler JM, Kunkel SL, Burdick MD, Standiford TJ, Rolfe MW, Strieter RM. Production of IL-8 and monocyte chemotactic peptide-1 by peripheral blood monocytes. Disparate responses to phytohemagglutinin and lipopolysaccharide. J Immunol. 1994;152:241–9.
Xiao S, Xu C, Jarvis JN. C1q-bearing immune complexes induce IL-8 secretion in human umbilical vein endothelial cells (HUVEC) through protein tyrosine kinase- and mitogen-activated protein kinase-dependent mechanisms: evidence that the 126 kD phagocytic C1q receptor mediates immune complex activation of HUVEC. Clin Exp Immunol. 2001;125:360–7.
O’Hara AM, Bhattacharyya A, Bai J, Mifflin RC, Ernst PB, Mitra S, et al. Tumor necrosis factor (TNF)-alpha-induced IL-8 expression in gastric epithelial cells: role of reactive oxygen species and AP endonuclease-1/redox factor (Ref)-1. Cytokine. 2009;46:359–69.
Liu X, Ye F, Xiong H, Hu D, Limb GA, Xie T, et al. IL-1beta Upregulates IL-8 Production in Human Muller Cells Through Activation of the p38 MAPK and ERK1/2 Signaling Pathways. Inflammation. 2014;37:1486–95.
Joshi-Barve S, Barve SS, Amancherla K, Gobejishvili L, Hill D, Cave M, et al. Palmitic acid induces production of proinflammatory cytokine interleukin-8 from hepatocytes. Hepatology. 2007;46:823–30.
Igoillo-Esteve M, Marselli L, Cunha DA, Ladriere L, Ortis F, Grieco FA, et al. Palmitate induces a pro-inflammatory response in human pancreatic islets that mimics CCL2 expression by beta cells in type 2 diabetes. Diabetologia. 2010;53:1395–405.
Choi SE, Kim TH, Yi SA, Hwang YC, Hwang WS, Choe SJ, et al. Capsaicin attenuates palmitate-induced expression of macrophage inflammatory protein 1 and interleukin 8 by increasing palmitate oxidation and reducing c-Jun activation in THP-1 (human acute monocytic leukemia cell) cells. Nutr Res. 2011;31:468–78.
Quan J, Liu J, Gao X, Liu J, Yang H, Chen W, et al. Palmitate induces interleukin-8 expression in human aortic vascular smooth muscle cells via Toll-like receptor 4/nuclear factor-kappaB pathway (TLR4/NF-kappaB-8). J Diabetes. 2014;6:33–41.
Yasumoto K, Okamoto S, Mukaida N, Murakami S, Mai M, Matsushima K. Tumor necrosis factor alpha and interferon gamma synergistically induce interleukin 8 production in a human gastric cancer cell line through acting concurrently on AP-1 and NF-kB-like binding sites of the interleukin 8 gene. J Biol Chem. 1992;267:22506–11.
Edwards MR, Mukaida N, Johnson M, Johnston SL. IL-1beta induces IL-8 in bronchial cells via NF-kappaB and NF-IL6 transcription factors and can be suppressed by glucocorticoids. Pulm Pharmacol Ther. 2005;18:337–45.
Yang BC, Yang ZH, Pan XJ, Xiao FJ, Liu XY, Zhu MX, et al. Crotonaldehyde-exposed macrophages induce IL-8 release from airway epithelial cells through NF-kappaB and AP-1 pathways. Toxicol Lett. 2013;219:26–34.
Szabo G, Mandrekar P, Dolganiuc A. Innate immune response and hepatic inflammation. Semin Liver Dis. 2007;27:339–50.
Gomez-Lechon MJ, Donato MT, Martinez-Romero A, Jimenez N, Castell JV, O’Connor JE. A human hepatocellular in vitro model to investigate steatosis. Chem Biol Interact. 2007;165:106–16.
Ho HY, Cheng ML, Wang YH, Chiu DT. Flow cytometry for assessment of the efficacy of siRNA. Cytometry A. 2006;69:1054–61.
Ho HY, Cheng ML, Lu FJ, Chou YH, Stern A, Liang CM, et al. Enhanced oxidative stress and accelerated cellular senescence in glucose-6-phosphate dehydrogenase (G6PD)-deficient human fibroblasts. Free Radic Biol Med. 2000;29:156–69.
Yang HC, Chen TL, Wu YH, Cheng KP, Lin YH, Cheng ML, et al. Glucose 6-phosphate dehydrogenase deficiency enhances germ cell apoptosis and causes defective embryogenesis in Caenorhabditis elegans. Cell Death Dis. 2013;4, e616.
Lee JW, Choi AH, Ham M, Kim JW, Choe SS, Park J, et al. G6PD up-regulation promotes pancreatic beta-cell dysfunction. Endocrinology. 2011;152:793–803.
Park J, Choe SS, Choi AH, Kim KH, Yoon MJ, Suganami T, et al. Increase in glucose-6-phosphate dehydrogenase in adipocytes stimulates oxidative stress and inflammatory signals. Diabetes. 2006;55:2939–49.
Ho HY, Cheng ML, Chiu DT. Glucose-6-phosphate dehydrogenase–from oxidative stress to cellular functions and degenerative diseases. Redox Rep. 2007;12:109–18.
Moret I, Cerrillo E, Navarro-Puche A, Iborra M, Rausell F, Tortosa L, et al. Oxidative stress in Crohn’s disease. Gastroenterol Hepatol. 2014;37:28–34.
Crowley SD. The Cooperative Roles of Inflammation and Oxidative Stress in the Pathogenesis of Hypertension. Antioxid Redox Signal. 2014;20:102–20.
Spolarics Z, Stein DS, Garcia ZC. Endotoxin stimulates hydrogen peroxide detoxifying activity in rat hepatic endothelial cells. Hepatology. 1996;24:691–6.
Spolarics Z. Endotoxemia, pentose cycle, and the oxidant/antioxidant balance in the hepatic sinusoid. J Leukoc Biol. 1998;63:534–41.
Shimada T, Watanabe N, Hiraishi H, Terano A. Redox regulation of interleukin-8 expression in MKN28 cells. Dig Dis Sci. 1999;44:266–73.
DeForge LE, Preston AM, Takeuchi E, Kenney J, Boxer LA, Remick DG. Regulation of interleukin 8 gene expression by oxidant stress. J Biol Chem. 1993;268:25568–76.
Sies H. Role of metabolic H2O2 generation: redox signaling and oxidative stress. J Biol Chem. 2014;289:8735–41.
Li YJ, Shimizu T, Hirata Y, Inagaki H, Takizawa H, Azuma A, et al. EM, EM703 inhibit NF-kB activation induced by oxidative stress from diesel exhaust particle in human bronchial epithelial cells: importance in IL-8 transcription. Pulm Pharmacol Ther. 2013;26:318–24.
Amore A, Formica M, Giacchino F, Gigliola G, Bonello F, Conti G, et al. N-Acetylcysteine in hemodialysis diabetic patients resets the activation of NF-kB in lymphomonocytes to normal values. J Nephrol. 2013;26:778–86.
Li DY, Xue MY, Geng ZR, Chen PY. The suppressive effects of Bursopentine (BP5) on oxidative stress and NF-kB activation in lipopolysaccharide-activated murine peritoneal macrophages. Cell Physiol Biochem. 2012;29:9–20.
Wilkins R, Tucci M, Benghuzzi H. Role of plant-derived antioxidants on NF-kb expression in LPS-stimulated macrophages - biomed 2011. Biomed Sci Instrum. 2011;47:222–7.
Halliwell B. Cell culture, oxidative stress, and antioxidants: avoiding pitfalls. Biomed J. 2014;37:99–105.
Chainani-Wu N. Safety and anti-inflammatory activity of curcumin: a component of tumeric (Curcuma longa). J Altern Complement Med. 2003;9:161–8.
Trujillo J, Chirino YI, Molina-Jijon E, Anderica-Romero AC, Tapia E, Pedraza-Chaverri J. Renoprotective effect of the antioxidant curcumin: Recent findings. Redox Biol. 2013;1:448–56.
Derochette S, Franck T, Mouithys-Mickalad A, Deby-Dupont G, Neven P, Serteyn D. Intra- and extracellular antioxidant capacities of the new water-soluble form of curcumin (NDS27) on stimulated neutrophils and HL-60 cells. Chem Biol Interact. 2013;201:49–57.
Xiao X, Yang M, Sun D, Sun S. Curcumin protects against sepsis-induced acute lung injury in rats. J Surg Res. 2012;176:e31–9.
Vaughan RA, Garcia-Smith R, Dorsey J, Griffith JK, Bisoffi M, Trujillo KA. Tumor necrosis factor alpha induces Warburg-like metabolism and is reversed by anti-inflammatory curcumin in breast epithelial cells. Int J Cancer. 2013;133:2504–10.
Kloesch B, Becker T, Dietersdorfer E, Kiener H, Steiner G. Anti-inflammatory and apoptotic effects of the polyphenol curcumin on human fibroblast-like synoviocytes. Int Immunopharmacol. 2013;15:400–5.
Klawitter M, Quero L, Klasen J, Gloess AN, Klopprogge B, Hausmann O, et al. Curcuma DMSO extracts and curcumin exhibit an anti-inflammatory and anti-catabolic effect on human intervertebral disc cells, possibly by influencing TLR2 expression and JNK activity. J Inflamm (Lond). 2012;9:29.
Henrotin Y, Clutterbuck AL, Allaway D, Lodwig EM, Harris P, Mathy-Hartert M, et al. Biological actions of curcumin on articular chondrocytes. Osteoarthritis Cartilage. 2010;18:141–9.
Shanmugam MK, Rane G, Kanchi MM, Arfuso F, Chinnathambi A, Zayed ME, et al. The Multifaceted Role of Curcumin in Cancer Prevention and Treatment. Molecules. 2015;20:2728–69.
Shakibaei M, Mobasheri A, Lueders C, Busch F, Shayan P, Goel A. Curcumin enhances the effect of chemotherapy against colorectal cancer cells by inhibition of NF-kappaB and Src protein kinase signaling pathways. PLoS One. 2013;8, e57218.
Um MY, Hwang KH, Ahn J, Ha TY. Curcumin attenuates diet-induced hepatic steatosis by activating AMP-activated protein kinase. Basic Clin Pharmacol Toxicol. 2013;113:152–7.
Mei X, Xu D, Xu S, Zheng Y, Xu S. Novel role of Zn(II)-curcumin in enhancing cell proliferation and adjusting proinflammatory cytokine-mediated oxidative damage of ethanol-induced acute gastric ulcers. Chem Biol Interact. 2012;197:31–9.
Kanitkar M, Gokhale K, Galande S, Bhonde RR. Novel role of curcumin in the prevention of cytokine-induced islet death in vitro and diabetogenesis in vivo. Br J Pharmacol. 2008;155:702–13.
Jain SK, Rains J, Croad J, Larson B, Jones K. Curcumin supplementation lowers TNF-alpha, IL-6, IL-8, and MCP-1 secretion in high glucose-treated cultured monocytes and blood levels of TNF-alpha, IL-6, MCP-1, glucose, and glycosylated hemoglobin in diabetic rats. Antioxid Redox Signal. 2009;11:241–9.
Cao J, Liu Y, Jia L, Zhou HM, Kong Y, Yang G, et al. Curcumin induces apoptosis through mitochondrial hyperpolarization and mtDNA damage in human hepatoma G2 cells. Free Radic Biol Med. 2007;43:968–75.
Becatti M, Prignano F, Fiorillo C, Pescitelli L, Nassi P, Lotti T, et al. The involvement of Smac/DIABLO, p53, NF-kB, and MAPK pathways in apoptosis of keratinocytes from perilesional vitiligo skin: Protective effects of curcumin and capsaicin. Antioxid Redox Signal. 2010;13:1309–21.
Kim YS, Ahn Y, Hong MH, Joo SY, Kim KH, Sohn IS, et al. Curcumin attenuates inflammatory responses of TNF-alpha-stimulated human endothelial cells. J Cardiovasc Pharmacol. 2007;50:41–9.
Bharti AC, Donato N, Singh S, Aggarwal BB. Curcumin (diferuloylmethane) down-regulates the constitutive activation of nuclear factor-kappa B and IkappaBalpha kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Blood. 2003;101:1053–62.
Jobin C, Bradham CA, Russo MP, Juma B, Narula AS, Brenner DA, et al. Curcumin blocks cytokine-mediated NF-kappa B activation and proinflammatory gene expression by inhibiting inhibitory factor I-kappa B kinase activity. J Immunol. 1999;163:3474–83.
Wilmanski J, Siddiqi M, Deitch EA, Spolarics Z. Augmented IL-10 production and redox-dependent signaling pathways in glucose-6-phosphate dehydrogenase-deficient mouse peritoneal macrophages. J Leukoc Biol. 2005;78:85–94.
Wilmanski J, Villanueva E, Deitch EA, Spolarics Z. Glucose-6-phosphate dehydrogenase deficiency and the inflammatory response to endotoxin and polymicrobial sepsis. Crit Care Med. 2007;35:510–18.
Spolarics Z, Siddiqi M, Siegel JH, Garcia ZC, Stein DS, Ong H, et al. Increased incidence of sepsis and altered monocyte functions in severely injured type A- glucose-6-phosphate dehydrogenase-deficient African American trauma patients. Crit Care Med. 2001;29:728–36.
Abu-Osba YK, Mallouh AA, Hann RW. Incidence and causes of sepsis in glucose-6-phosphate dehydrogenase-deficient newborn infants. J Pediatr. 1989;114:748–52.
Upperman JS, Pillage G, Siddiqi MQ, Zeevi A, Kelly N, Ford HR, et al. Dominance of high-producing interleukin 6 and low-producing interleukin 10 and interferon gamma alleles in glucose-6-phosphate dehydrogenase-deficient trauma patients. Shock. 2005;23:197–201.
Liese AM, Siddiqi MQ, Siegel JH, Deitch EA, Spolarics Z. Attenuated monocyte IL-10 production in glucose-6-phosphate dehydrogenase-deficient trauma patients. Shock. 2002;18:18–23.
Liao SL, Lai SH, Tsai MH, Weng YH. Cytokine Responses of TNF-alpha, IL-6, and IL-10 in G6PD-Deficient Infants. Pediatr Hematol Oncol. 2014;31:87–94.
Timens W, Boes A, Rozeboom-Uiterwijk T, Poppema S. Immaturity of the human splenic marginal zone in infancy. Possible contribution to the deficient infant immune response. J Immunol. 1989;143:3200–6.
Saito F, Kuwata H, Oiki E, Koike M, Uchiyama Y, Honda K, et al. Inefficient phagosome maturation in infant macrophages. Biochem Biophys Res Commun. 2008;375:113–18.