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Laboratory Study

Microarray Analysis of Altered Gene Expression and the Role of ATF3 in HK-2 Cells Treated with Hemin

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Pages 624-632 | Received 19 Dec 2012, Accepted 22 Feb 2013, Published online: 08 Apr 2013

REFERENCES

  • Paoli M, Marles-Wright J, Smith A. Structure-function relationships in heme-proteins. DNA Cell Biol. 2002;21(4):271–280.
  • Abraham NG, Drummond GS, Lutton JD, Kappas A. The biological significance and physiological role of heme oxygenase. Cell Physiol Biochem. 1996;6:129–168.
  • Nienhaus K, Zosel F, Nienhaus GU. Ligand binding to heme proteins: a comparison of cytochrome C variants with globins. J Phys Chem B. 2012;116(40):12180–12188.
  • Immenschuh S, Baumgart-Vogt E, Mueller S. Heme oxygenase-1 and iron in liver inflammation: a complex alliance. Curr Drug Targets. 2010;11(12):1541–1550.
  • Soudi M, Zamocky M, Jakopitsch C, Furtmüller PG, Obinger C. Molecular evolution, structure, and function of peroxidasins. Chem Biodivers. 2012;9(9):1776–1793.
  • Zager RA, Johnson AC, Becker K. Renal cortical hemopexin accumulation in response to acute kidney injury. Am J Physiol Renal Physiol. 2012;303(10):F1460–F1472.
  • Zarjou A, Agarwal A. Heme oxygenase-1 as a target for TGF-β in kidney disease. Semin Nephrol. 2012;32(3):277–286.
  • Zhou J, Ouyang X, Schoeb TR, et al. Kidney injury accelerates cystogenesis via pathways modulated by heme oxygenase and complement. J Am Soc Nephrol. 2012;23(7):1161–1171.
  • Elmarakby AA, Faulkner J, Baban B, Saleh MA, Sullivan JC. Induction of hemeoxygenase-1 reduces glomerular injury and apoptosis in diabetic spontaneously hypertensive rats. Am J Physiol Renal Physiol. 2012;302(7):F791–F800.
  • Hill-Kapturczak N, Chang SH, Agarwal A. Heme oxygenase and the kidney. DNA Cell Biol. 2002;21:307–321.
  • Kanakiriya SK, Nath KA. Heme oxygenase and acute renal injury. In: Molitoris B and Finn WF, eds. Acute Renal Failure: A Companion to Brenner and Rector’s the Kidney. 1st ed., ch. 5. Philadelphia, PA: Saunders; 200178–88.
  • Muller-Eberhard U, Fraig M. Bioactivity of heme and its containment. Am J Hematol. 1993;42:59–62.
  • Stocker R. Induction of hem oxygenase as a defence against oxidative stress. Free Radic Res Commun. 1990;9:101–112.
  • Zager RA. Rhabdomyolysis and myohemoglobinuric acute renal failure. Kidney Int. 1996;49:314–326.
  • Agarwal A, Nick HS. Renal response to tissue injury: lessons from heme oxygenase-1 gene ablation and expression. J Am Soc Nephrol. 2000;11:965–973.
  • Jeney V, Balla J, Yachie A, et al. Pro-oxidant and cytotoxic effects of circulating heme. Blood. 2002;100:879–887.
  • Goldstein L, Teng ZP, Zeserson E, Patel M, Regan RF. Hemin induces an iron-dependent, oxidative injury to human neuron-like cells. J Neurosci Res. 2003;73:113–121.
  • Balla J, Balla G, Jeney V, Kakuk G, Jacob HS, Vercellotti GM. Ferriporphyrins and endothelium: a 2-edged sword-promotion of oxidation and induction of cytoprotectants. Blood. 2000;95(4):3442–3450.
  • Wagener FA, Eggert A, Boerman OC, et al. Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase. Blood. 2001;98:1802–1811.
  • Jeney V, Balla J, Yachie A, et al. Pro-oxidant and cytotoxic effects of circulating heme. Blood. 2002;100:879–887.
  • Dennery PA, Sridhar KJ, Lee CS, et al. Heme oxygenase-mediated resistance to oxygen toxicity in hamster fibroblasts. J Biol Chem. 1997;272:14937–14942.
  • Hebbel RP, Eaton JW. Pathobiology of heme interaction with the erythrocyte membrane. Semin Hematol. 1989;26:136–149.
  • Iwata M, Zager RA. Myoglobin inhibits proliferation of cultured human proximal tubular (HK-2) cells. Kidney Int. 1996;50:796–804.
  • Lavrovsky Y, Schwartzman ML, Levere RD, Abraham NG. Identification of binding sites for transcription factors NF-kappa B and AP-2 in the promoter region of the human heme oxygenase1 gene. Proc Natl Acad Sci USA. 1994;91:5987–5991.
  • Laird MD, Wakade C, Alleyne CH, Dhandapani KM. Hemin-induced necroptosis involves glutathione depletion in mouse astrocytes. Free Radic Biol Med. 2008;45:1103–1114.
  • Chowa JM, Huang GC, Lin HY, Shen SC, Yang LY, Chen YC. Cytotoxic effects of metal protoporphyrins in glioblastoma cells: roles of albumin, reactive oxygen species, and heme oxygenase-1. Toxicol Lett. 2008;177:97–107.
  • Yin X, Wolford CC, Chang YS, et al. ATF3, an adaptive-response gene, enhances TGF signaling and cancer-initiating cell features in breast cancer cells. J Cell Sci. 2010;123(20):3558–3565.
  • Hai T, Wolford CC, Chang YS. ATF3, a hub of the cellular adaptive-response network, in the pathogenesis of diseases: is modulation of inflammation a unifying component? Gene Expr. 2010;15(1): 1–11.
  • Hasan RN, Schafer AI. Hemin up-regulates Erg-1 expression in vascular smooth muscle cell via reactive oxygen species, ERK-1/2. Elk-1 and NF-KB. Circ Res. 2008;102:42–50.
  • Lander HM, Levine DM, Novogrodsky A. Hemin stimulation of cAMP production in human lymphocytes. FEBS Lett. 1992;303(2–3):242–246.
  • Woessmann W, Mivechi NF. Role of ERK activation in growth and erythroid differentiation of K562 cells. Exp Cell Res. 2001;264(7):193–200.
  • Nakaso K, Yano H, Fukuhara Y, Takeshima T, Wada-Isoe K, Nakashima K. PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells. FEBS Lett. 2003;546:181–184.
  • Grima J, Zhu LJ, Zong SD, Catterall JF, Bardin CW, Cheng CY. Rat testin is a newly identified component of the junctional complexes in various tissues who- se mRNA is predominantly expressed in the testis and ovary. Biol Reprod. 1995;52:340–355.
  • Shih HJ, Yang Y, Huang CJ, Chow YC. Hemin-induced HO-1 over expression after testicular torsion-detorsion involeves NRF2, NF-κB, ERK. Eur Urol Suppl. 2008;7(3):91.
  • Hai T, Hartman MG. The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis. Gene. 2001;273:1–11.
  • Liang G, Wolfgang CD, Chen BP, Chen TH, Hai T. ATF3 gene. Genomic organization, promoter, and regulation. J Biol Chem. 1996;271:1695–1701.
  • Beri R, Chandra R. Chemistry and biology of heme: effect of metal salts, organometals, and metalloporphyrins on heme synthesis and catabolism, with special reference to clinical implications and interactions with cytochrome P-450. Drug Metab Rev. 1993;25:149–152.
  • Fitch CD, Chevli R, Kanjanangglupan P, Dutta P, Chevli K, Chou AC. Intracellular ferriprotoporphyrin IX is a potent lytic agent. Blood. 1983;62:1165–1168.
  • Shaklai N, Shviro E, Rabizadeh E, Kirschner-Zibler I. Accumulation and drainage of hemin in the red cell membrane. Biochim Biophys Acta. 1985;821:355–366.
  • Balla G, Vercellotti GM, Muller-Eberhard U, Eaton J, Jacob HS. Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab Invest. 1991;64:648–655.
  • Liu SC, Zhai S, Lawler J, Palek J. Hemin-induced dissociation of erythrocyte membrane skeletal proteins. J Biol Chem. 1985;260:12234–12239.
  • Harvey JW, Beutler E. Binding of heme by glutathione Stransferase: a possible role of the erythrocyte enzyme. Blood. 1982;60: 1227–1230.
  • Zaidi A, Marden MC, Poyart C, Leclerc L. Protection by lazaroids of the erythrocyte (Ca2+, Mg2+)-ATPase against iron-induced inhibition. Eur J Pharmacol. 1995;290:133–139.
  • Sullivan SG, Baysal E, Stern A. Inhibition of hemin-induced hemolysis by desferrioxamine: binding of hemin to red cell membranes and the effects of alteration of membrane sulfhydryl groups. Biochem Biophys Acta. 1992;1104:38–44.
  • Zhang PL, Lun MY, Schworer CM, et al. Heat shock protein expression is highly sensitive to ischemia-reperfusion injury in rat kidneys. Ann Clin Lab Sci. 2008;38(1):57–64.
  • Cai Y, Zhang C, Nawa T, et al. Homocysteine responsive ATF3 gene expression in human vascular endothelial cells: activation of c-Jun NH (2) terminal kinase and promoter response element. Blood. 2000;96(6):2140–2148.
  • Zmuda EJ, Qi L, Zhu MX, Mirmira RG, Montminy MR, Hai T. The roles of ATF3, an adaptive-response gene, in high-fat-diet-induced diabetes and pancreatic β-Cell dysfunction. Mol Endocrinol. 2010;24:1423–1433.
  • Gilchrist M, Henderson WR Jr, Clark AE, et al. Activating transcription factor 3 is a negative regulator of allergic pulmonary inflammation. J Exp Med. 2008;205:2349–2357.
  • Yan CH, Jamaluddin MS, Aggarwal B, Myers J, Boyd DD. Gene expression profiling identifies activating transcription factor 3 as a novel contributor to the proapoptotic effect of curcumin. Mol Cancer Ther. 2005;4:233–241.
  • Nakagomi S, Suzuki Y, Namikawa K, Kiryu-Seo S, Kiyama H. Expression of the activating transcription factor 3 prevents c-Jun N-terminal kinase-induced neuronal death by promoting heat shock protein 27 expression and Akt activation. J Neurosci. 2003;23:5187–5196.

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