Effects of UVB-induced oxidative stress on protein expression and specific protein oxidation in normal human epithelial keratinocytes: a proteomic approach
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Attar M, Lloyd JR, Bickers DR, Mukhtar H: Malignant conversion of UV radiation and chemically induced mouse skin benign tumors by free-radical-generating compounds. Carcinogenesis 1989, 10: 1841–1845. 10.1093/carcin/10.10.1841
Paz ML, González Maglio DH, Weill FS, Bustamante J, Leoni J: Mitochondrial dysfunction and cellular stress progression after ultraviolet B irradiation in human keratinocytes. Photodermatol Photoimmunol Photomed 2008, 24: 115–122. 10.1111/j.1600-0781.2008.00348.x
Kovacs D, Raffa S, Flori E, Aspite N, Briganti S, Cardinali G, Torrisi MR, Picardo M: Keratinocyte growth factor down-regulates intracellular ROS production induced by UVB. J Dermatol Sci 2009, 54: 106–113. 10.1016/j.jdermsci.2009.01.005
D'Autréaux B, Toledano MB: ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007, 8: 813–824. 10.1038/nrm2256
Kamata H, Hirata H: Redox regulation of cellular signalling. Cell Signal 1999, 11: 1–14. 10.1016/S0898-6568(98)00037-0
Thannickal VJ, Fanburg BL: Reactive oxygen species in cell signaling. Am J Physiol Lung Cell Mol Physiol 2000, 279: L1005–1028.
Toyokuni S, Okamoto K, Yodoi J, Hiai H: Persistent oxidative stress in cancer. FEBS Lett 1995, 358: 1–3. 10.1016/0014-5793(94)01368-B
Punnonen K, Puntala A, Jansén CT, Ahotupa M: UVB irradiation induces lipid peroxidation and reduces antioxidant enzyme activities in human keratinocytes in vitro. Acta Derm Venereol 1991, 71: 239–242.
Stadtman ER, Berlett BS: Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab Rev 1998, 30: 225–243. 10.3109/03602539808996310
Esterbauer H, Schaur RJ, Zollner H: Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991, 11: 81–128. 10.1016/0891-5849(91)90192-6
LeBlanc WG, Vidal L, Kirsner RS, Lee DJ, Caban-Martinez AJ, McCollister KE, Arheart KL, Chung-Bridges K, Christ S, Clark J, Lewis JE, Davila EP, Rouhani P, Fleming LE: Reported skin cancer screening of US adult workers. J Am Acad Dermatol 2008, 59: 55–63. 10.1016/j.jaad.2008.03.013
Perluigi M, Giorgi A, Blarzino C, De Marco F, Foppoli C, Di Domenico F, Butterfield DA, Schininà ME, Cini C, Coccia R: Proteomics analysis of protein expression and specific protein oxidation in human papillomavirus transformed keratinocytes upon UVB irradiation. J Cell Mol Med 2009, 13: 1809–1822. 10.1111/j.1582-4934.2008.00465.x
Jung T, Grune T: The proteasome and its role in the degradation of oxidized proteins. IUBMB Life 2008, 60: 743–752. 10.1002/iub.114
Dahlmann B: Role of proteasomes in disease. BMC Biochem 2007,8(Suppl 1):S3. 10.1186/1471-2091-8-S1-S3
Keller JN, Hanni KB, Markesbery WR: Impaired proteasome function in Alzheimer's disease. J Neurochem 2000, 75: 436–9. 10.1046/j.1471-4159.2000.0750436.x
Petropoulos I, Conconi M, Wang X, Hoenel B, Brégégère F, Milner Y, Friguet B: Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol A Biol Sci Med Sci 2000, 55: B220–227.
Timperio AM, Egidi MG, Zolla L: Proteomics applied on plant abiotic stresses: Role of heat shock proteins (HSP). J Proteomics 2008, 71: 391–411. 10.1016/j.jprot.2008.07.005
Arrigo AP, Virot S, Chaufour S, Firdaus W, Kretz-Remy C, Diaz-Latoud C: Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. Antioxid Redox Signal 2005, 7: 414–422. 10.1089/ars.2005.7.414
McClung JK, King RL, Walker LS, Danner DB, Nuell MJ, Stewart CA, Dell'Orco RT: Expression of prohibitin, an antiproliferative protein. Exp Gerontol 1992, 27: 413–418. 10.1016/0531-5565(92)90074-A
Nuell MJ, Stewart DA, Walker L, Friedman V, Wood CM, Owens GA, Smith JR, Schneider EL, Dell' Orco R, Lumpkin CK, Danner DB, Mc-Clung JK: Prohibitin, an evolutionarily conserved intracellular protein that blocks DNA synthesis in normal fibroblasts and HeLa cells. Mol Cell Biol 1991, 11: 1372–1381.
Carter WG, Wayner EA, Bouchard TS, Kaur P: The role of integrins α2 β1 and α3 β1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 1990, 110: 1387–1404. 10.1083/jcb.110.4.1387
Manohar A, Shome SG, Lamar J, Stirling L, Iyer V, Pumiglia K, DiPersio CM: Alpha 3 beta 1 integrin promotes keratinocyte cell survival through activation of a MEK [?]/ERK [?] signaling pathway. J Cell Sci 2004, 117: 4043–4054. 10.1242/jcs.01277
Pignatelli M, Hanby AM, Stamp GW: Low expression of β1, α2 and α3 subunits of VLA integrins in malignant mammary tumours. J Pathol 1991, 165: 25–32. 10.1002/path.1711650106
Moll R, Franke WW, Schiller DL, Geiger B, Krepler R: The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell 1982, 3: 11–24. 10.1016/0092-8674(82)90400-7
Rao KS, Babu KK, Gupta PD: Keratins and skin disorders. Cell Biol Int 1996, 20: 261–74. 10.1006/cbir.1996.0029
Aplin AE, Howe A, Alahari SK, Juliano RL: Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev 1998, 50: 197–263.
De Marco F, Perluigi M, Foppoli C, Blarzino C, Cini C, Coccia R, Venuti A: UVB irradiation down-regulates HPV-16 RNA expression: implications for malignant progression of transformed cells. Virus Res 2007, 130: 249–259. 10.1016/j.virusres.2007.06.018
Mann M, Jensen ON: Proteomic analysis of post-translational modifications. Nat Biotechnol 2003, 21: 255–261. 10.1038/nbt0303-255
Elliott JG, Oliver JD, High S: The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J Biol Chem 1997, 272: 13849–13855. 10.1074/jbc.272.21.13849
Antoniou AN, Ford S, Alphey M, Osborne A, Elliott T, Powis SJ: The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J 2002, 21: 2655–2663. 10.1093/emboj/21.11.2655
Kang SJ, Cresswell P: Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules. EMBO J 2002, 21: 1650–1660. 10.1093/emboj/21.7.1650
Lahav J, Wijnen EM, Hess O, Hamaia SW, Griffiths D, Makris M, Knight CG, Essex DW, Farndale RW: Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin a2h1. Blood 2003, 102: 2085–2092. 10.1182/blood-2002-06-1646
Uebara T, Nakamura T, Yao D, Shi ZQ, Gu Z, Ma Y, Masliah E, Nomura Y, Lipton SA: S-nitrosylated protein disulphide isomerase links protein misfolding to neurodegeneration. Nature 2006, 441: 513–517. 10.1038/nature04782
Falahatpisheh H, Nanez A, Montoya-Durango D, Qian Y, Tiffany-Castiglioni E, Ramos KS: Activation profiles of HSPA5 during the glomerular mesangial cell stress response to chemical injury. Cell Stress Chaperones 2007, 12: 209–218. 10.1379/CSC-259.1
Millard TH, Sharp SJ, Machesky LM: Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex. Biochem J 2004, 380: 1–17. 10.1042/BJ20040176
Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY: The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 2000, 10: 815–827. 10.1093/glycob/10.8.815
Waisman DM: Annexin II tetramer: structure and function. Mol Cell Biochem 1995, 149–150: 301–322. 10.1007/BF01076592
Tanaka T, Akatsuka S, Ozeki M, Shirase TH, Toyokuni S: Redox regulation of Annexin 2 and its implications for oxidative stress-induced renal carcinogenesis and metastasis. Oncogene 2004, 23: 3980–3989. 10.1038/sj.onc.1207555
Haley B, Paunesku T, Protić M, Woloschak GE: Response of heterogeneous ribonuclear proteins (hnRNP) to ionising radiation and their involvement in DNA damage repair. Int J Radiat Biol 2009, 85: 643–655. 10.1080/09553000903009548
Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA: Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 2002, 82: 1524–1532. 10.1046/j.1471-4159.2002.01103.x
Tamarit J, Cabiscol E, Ros J: Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem 1998, 273: 3027–3032. 10.1074/jbc.273.5.3027
Levine RL, Stadtman ER: Oxidative modification of proteins during aging. Exp Gerontol 2001, 36: 1495–1502. 10.1016/S0531-5565(01)00135-8
Pirisi L, Yasumoto S, Feller M, Doniger J, Di Paolo JA: Transformation of human fibroblasts and keratinocytes with human papillomavirus type 16 DNA. J Virol 1987, 61: 1061–1066.
Conrad CC, Talent JM, Malakowsky CA, Gracy RW: Post-Electrophoretic Identification of Oxidized Proteins. Biol Proced Online 2000, 2: 39–45. 10.1251/bpo17
Maurer HH, Peters FT: Toward high-throughput drug screening using mass spectrometry. Ther Drug Monit 2005, 27: 686–688. 10.1097/01.ftd.0000180224.19384.f0
Mignogna G, Giorgi A, Stefanelli P, Neri A, Colotti G, Maras B, Schininà ME: Inventory of the proteins in Neisseria meningitidis serogroup B strain MC58. J Proteome 2005, 4: 1361–1370. 10.1021/pr0500511
Pappin DJ: Peptide mass fingerprinting using MALDI-TOF mass spectrometry. Methods Mol Biol 2003, 211: 211–219.
Lauderback CM, Hackett JM, Huang FF, Keller JN, Szweda LI, Markesbery WR, Butterfield DA: The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Abeta1–42. J Neurochem 2001, 78: 413–416. 10.1046/j.1471-4159.2001.00451.x
Jessop CE, Bulleid NJ: Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J Biol Chem 2004, 279: 55341–55347. 10.1074/jbc.M411409200