KEGG   PATHWAY: ko05208
Entry
ko05208                     Pathway                                
Name
Chemical carcinogenesis - reactive oxygen species
Description
It is well established that cancer is a multi-step process which involves initiation, promotion and progression. Chemical carcinogens can alter any of these processes to induce their carcinogenic effects. In the majority of instances, chemical carcinogens, directly or after xenobiotic metabolism, induce DNA damage and act in a 'genotoxic' manner. There is, however, a group of carcinogens that induce cancer via nongenotoxic mechanisms. The biochemical modes of action for nongenotoxic carcinogens are diverse, one example of which is induction of oxidative stress. Trace metals and organic xenobiotics are typical classes of environmental pollutants with prooxidant effects. Trace metals generate reactive oxygen species (ROS) depending on their ability to lose electrons and catalyze Haber Weiss and Fenton reactions. ROS are also generated due to induction of various cytochrome P450 isoenzymes during detoxification of chemical carcinogens. Increased ROS generation often has been linked to DNA damage that can lead to mutations and may, therefore, play an important role in the initiation and progression of multistage carcinogenesis. Besides causing DNA damage, ROS further induce multiple intracellular signaling pathways, notably NF-kappa B, JNK/SAPK/p38, as well as Erk/MAPK. These signaling routes can lead to transcriptional induction of target genes that could promote proliferation or confer apoptosis resistance to exposed cells.
Class
Human Diseases; Cancer: overview
Pathway map
ko05208  Chemical carcinogenesis - reactive oxygen species
ko05208

Orthology
K07755  arsenite methyltransferase [EC:2.1.1.137]
K00799  glutathione S-transferase [EC:2.5.1.18]
K03878  NADH-ubiquinone oxidoreductase chain 1 [EC:7.1.1.2]
K03879  NADH-ubiquinone oxidoreductase chain 2 [EC:7.1.1.2]
K03880  NADH-ubiquinone oxidoreductase chain 3 [EC:7.1.1.2]
K03881  NADH-ubiquinone oxidoreductase chain 4 [EC:7.1.1.2]
K03882  NADH-ubiquinone oxidoreductase chain 4L [EC:7.1.1.2]
K03883  NADH-ubiquinone oxidoreductase chain 5 [EC:7.1.1.2]
K03884  NADH-ubiquinone oxidoreductase chain 6 [EC:7.1.1.2]
K03942  NADH dehydrogenase (ubiquinone) flavoprotein 1 [EC:7.1.1.2]
K03943  NADH dehydrogenase (ubiquinone) flavoprotein 2 [EC:7.1.1.2]
K03944  NADH dehydrogenase (ubiquinone) flavoprotein 3
K03945  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 1
K03946  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 2
K03947  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 3
K03948  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 4
K03949  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 5
K03950  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 6
K03951  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 7
K03952  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 8
K03953  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 9
K03954  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 10
K03955  NADH dehydrogenase (ubiquinone) 1 alpha/beta subcomplex 1, acyl-carrier protein
K03956  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 11
K11352  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 12
K11353  NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 13
K03957  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 1
K03958  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 2
K03959  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 3
K03960  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 4
K03961  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 5
K03962  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 6
K03963  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 7
K03964  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 8
K03965  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9
K03966  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 10
K11351  NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 11
K03934  NADH dehydrogenase (ubiquinone) Fe-S protein 1 [EC:7.1.1.2]
K03935  NADH dehydrogenase (ubiquinone) Fe-S protein 2 [EC:7.1.1.2]
K03936  NADH dehydrogenase (ubiquinone) Fe-S protein 3 [EC:7.1.1.2]
K03937  NADH dehydrogenase (ubiquinone) Fe-S protein 4
K03938  NADH dehydrogenase (ubiquinone) Fe-S protein 5
K03939  NADH dehydrogenase (ubiquinone) Fe-S protein 6
K03940  NADH dehydrogenase (ubiquinone) Fe-S protein 7 [EC:7.1.1.2]
K03941  NADH dehydrogenase (ubiquinone) Fe-S protein 8 [EC:7.1.1.2]
K03967  NADH dehydrogenase (ubiquinone) 1 subunit C1
K03968  NADH dehydrogenase (ubiquinone) 1 subunit C2
K00234  succinate dehydrogenase (ubiquinone) flavoprotein subunit [EC:1.3.5.1]
K00235  succinate dehydrogenase (ubiquinone) iron-sulfur subunit [EC:1.3.5.1]
K00236  succinate dehydrogenase (ubiquinone) cytochrome b560 subunit
K00237  succinate dehydrogenase (ubiquinone) membrane anchor subunit
K00411  ubiquinol-cytochrome c reductase iron-sulfur subunit [EC:7.1.1.8]
K00412  ubiquinol-cytochrome c reductase cytochrome b subunit
K00413  ubiquinol-cytochrome c reductase cytochrome c1 subunit
K00414  ubiquinol-cytochrome c reductase core subunit 1
K00415  ubiquinol-cytochrome c reductase core subunit 2
K00416  ubiquinol-cytochrome c reductase subunit 6
K00417  ubiquinol-cytochrome c reductase subunit 7
K00418  ubiquinol-cytochrome c reductase subunit 8
K00419  ubiquinol-cytochrome c reductase subunit 9
K00420  ubiquinol-cytochrome c reductase subunit 10
K02262  cytochrome c oxidase subunit 3
K02256  cytochrome c oxidase subunit 1 [EC:7.1.1.9]
K02261  cytochrome c oxidase subunit 2
K02263  cytochrome c oxidase subunit 4
K02264  cytochrome c oxidase subunit 5a
K02265  cytochrome c oxidase subunit 5b
K02266  cytochrome c oxidase subunit 6a
K02267  cytochrome c oxidase subunit 6b
K02268  cytochrome c oxidase subunit 6c
K02270  cytochrome c oxidase subunit 7a
K02271  cytochrome c oxidase subunit 7b
K02272  cytochrome c oxidase subunit 7c
K02273  cytochrome c oxidase subunit 8
K02132  F-type H+-transporting ATPase subunit alpha
K02133  F-type H+-transporting ATPase subunit beta [EC:7.1.2.2]
K02136  F-type H+-transporting ATPase subunit gamma
K02134  F-type H+-transporting ATPase subunit delta
K02135  F-type H+-transporting ATPase subunit epsilon
K02126  F-type H+-transporting ATPase subunit a
K02127  F-type H+-transporting ATPase subunit b
K02128  F-type H+-transporting ATPase subunit c
K02138  F-type H+-transporting ATPase subunit d
K02137  F-type H+-transporting ATPase subunit O
K02131  F-type H+-transporting ATPase subunit 6
K02125  F-type H+-transporting ATPase subunit 8
K04564  superoxide dismutase, Fe-Mn family [EC:1.15.1.1]
K05862  voltage-dependent anion channel protein 1
K15040  voltage-dependent anion channel protein 2
K15041  voltage-dependent anion channel protein 3
K05863  solute carrier family 25 (mitochondrial adenine nucleotide translocator), member 4/5/6/31
K09565  peptidyl-prolyl isomerase F (cyclophilin D) [EC:5.2.1.8]
K04565  superoxide dismutase, Cu-Zn family [EC:1.15.1.1]
K03781  catalase [EC:1.11.1.6]
K14700  solute carrier family 26 (sulfate anion transporter), member 1
K14701  solute carrier family 26 (sulfate anion transporter), member 2
K14704  solute carrier family 26 (sulfate anion transporter), member 6
K14706  solute carrier family 26 (sulfate anion transporter), member 9
K07409  cytochrome P450 family 1 subfamily A2 [EC:1.14.14.1]
K07415  cytochrome P450 family 2 subfamily E1 [EC:1.14.14.-]
K07416  cytochrome P450 family 2 subfamily F [EC:1.14.14.1]
K07408  cytochrome P450 family 1 subfamily A1 [EC:1.14.14.1]
K07410  cytochrome P450 family 1 subfamily B1 [EC:1.14.14.1]
K01253  microsomal epoxide hydrolase [EC:3.3.2.9]
K08726  soluble epoxide hydrolase / lipid-phosphate phosphatase [EC:3.3.2.10 3.1.3.76]
K22368  epoxide hydrolase 3 [EC:3.3.2.10]
K22369  epoxide hydrolase 4 [EC:3.3.-.-]
K00002  alcohol dehydrogenase (NADP+) [EC:1.1.1.2]
K00212  20alpha/3alpha-hydroxysteroid dehydrogenase / dihydrodiol dehydrogenase [EC:1.1.1.149 1.1.1.357 1.3.1.20]
K00089  3alpha-hydroxysteroid 3-dehydrogenase [EC:1.1.1.213 1.1.1.357]
K04119  aldo-keto reductase family 1 member C3 [EC:1.1.1.51 1.1.1.188 1.1.1.213 1.1.1.357]
K00037  3alpha-hydroxysteroid 3-dehydrogenase / chlordecone reductase [EC:1.1.1.50 1.1.1.357 1.1.1.225]
K00355  NAD(P)H dehydrogenase (quinone) [EC:1.6.5.2]
K00079  carbonyl reductase 1 [EC:1.1.1.184 1.1.1.189 1.1.1.197]
K09093  aryl hydrocarbon receptor
K12550  lactoperoxidase [EC:1.11.1.7]
K21423  NADPH oxidase 4 [EC:1.6.3.-]
K08009  cytochrome b-245, alpha polypeptide
K08008  NADPH oxidase 1
K08011  neutrophil cytosolic factor 1
K08010  neutrophil cytosolic factor 2
K04357  epidermal growth factor
K04361  epidermal growth factor receptor [EC:2.7.10.1]
K05460  hepatocyte growth factor
K05099  proto-oncogene tyrosine-protein kinase Met [EC:2.7.10.1]
K04364  growth factor receptor-bound protein 2
K03099  son of sevenless
K02833  GTPase HRas
K07827  GTPase KRas
K07828  GTPase NRas
K08845  A-Raf proto-oncogene serine/threonine-protein kinase [EC:2.7.11.1]
K04365  B-Raf proto-oncogene serine/threonine-protein kinase [EC:2.7.11.1]
K04366  RAF proto-oncogene serine/threonine-protein kinase [EC:2.7.11.1]
K04368  mitogen-activated protein kinase kinase 1 [EC:2.7.12.2]
K04369  mitogen-activated protein kinase kinase 2 [EC:2.7.12.2]
K04371  mitogen-activated protein kinase 1/3 [EC:2.7.11.24]
K04426  mitogen-activated protein kinase kinase kinase 5 [EC:2.7.11.25]
K04430  mitogen-activated protein kinase kinase 4 [EC:2.7.12.2]
K04431  mitogen-activated protein kinase kinase 7 [EC:2.7.12.2]
K04440  mitogen-activated protein kinase 8/9/10 (c-Jun N-terminal kinase) [EC:2.7.11.24]
K04441  p38 MAP kinase [EC:2.7.11.24]
K04448  transcription factor AP-1
K04379  proto-oncogene protein c-fos
K02649  phosphoinositide-3-kinase regulatory subunit alpha/beta/delta
K00922  phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha/beta/delta [EC:2.7.1.153]
K04392  Ras-related C3 botulinum toxin substrate 1
K06276  3-phosphoinositide dependent protein kinase-1 [EC:2.7.11.1]
K04456  RAC serine/threonine-protein kinase [EC:2.7.11.1]
K09408  forkhead box protein O3
K02158  Bcl-2-antagonist of cell death
K05696  tyrosine-protein phosphatase non-receptor type 1 [EC:3.1.3.48]
K01110  phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN [EC:3.1.3.16 3.1.3.48 3.1.3.67]
K04467  inhibitor of nuclear factor kappa-B kinase subunit alpha [EC:2.7.11.10]
K07209  inhibitor of nuclear factor kappa-B kinase subunit beta [EC:2.7.11.10]
K07210  inhibitor of nuclear factor kappa-B kinase subunit gamma
K04734  NF-kappa-B inhibitor alpha
K04735  transcription factor p65
K02580  nuclear factor NF-kappa-B p105 subunit
K06068  novel protein kinase C delta type [EC:2.7.11.13]
K05698  receptor-type tyrosine-protein phosphatase eta [EC:3.1.3.48]
K14394  low molecular weight phosphotyrosine protein phosphatase [EC:3.1.3.2 3.1.3.48]
K07293  tyrosine-protein phosphatase non-receptor type 11 [EC:3.1.3.48]
K05704  tyrosine-protein kinase Src [EC:2.7.10.2]
K06619  abelson tyrosine-protein kinase 1 [EC:2.7.10.2]
K08887  abelson tyrosine-protein kinase 2 [EC:2.7.10.2]
K06070  protein kinase D [EC:2.7.11.13]
K05725  focal adhesion kinase 1 [EC:2.7.10.2]
K01115  phospholipase D1/2 [EC:3.1.4.4]
K04466  mitogen-activated protein kinase kinase kinase 14 [EC:2.7.11.25]
K08268  hypoxia-inducible factor 1 alpha
K09097  aryl hydrocarbon receptor nuclear translocator
K05448  vascular endothelial growth factor A
K10456  kelch-like protein 19
K05638  nuclear factor erythroid 2-related factor 2
K00510  heme oxygenase 1 [EC:1.14.14.18]
Compound
C00001  H2O
C00003  NAD+
C00005  NADPH
C00006  NADP+
C00007  Oxygen
C00019  S-Adenosyl-L-methionine
C00021  S-Adenosyl-L-homocysteine
C00023  Iron
C00027  Hydrogen peroxide
C00051  Glutathione
C00070  Copper
C00084  Acetaldehyde
C00127  Glutathione disulfide
C00146  Phenol
C00291  Nickel
C00469  Ethanol
C00472  p-Benzoquinone
C00530  Hydroquinone
C00704  Superoxide
C00951  Estradiol-17beta
C01407  Benzene
C01413  Cadmium
C01782  Benzene oxide
C02389  p-Benzosemiquinone
C02575  Pentachlorophenol
C02814  Benzene-1,2,4-triol
C03434  Tetrachlorohydroquinone
C03622  N-Hydroxy-4-aminobiphenyl
C04623  DDT
C05301  2-Hydroxyestradiol
C05309  Semiquinone
C05981  Phosphatidylinositol-3,4,5-trisphosphate
C06268  Chromium
C06269  Arsenic
C06696  Lead
C07294  Methylarsonate
C07295  Methanearsonous acid
C07308  Cacodylate
C07535  Benzo[a]pyrene
C07557  2,3,7,8-Tetrachlorodibenzodioxin
C10998  4-Aminobiphenyl
C14209  4-Hydroxy-17beta-estradiol
C14850  Benzo[a]pyrene-7,8-oxide
C14852  Benzo[a]pyrene-7,8-dihydrodiol
C16038  2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
C16453  4-(N-Nitrosomethylamino)-1-(3-pyridyl)-1-butanone
C16844  Hydroxyl radical
C18205  2,2',4,4'-Tetrabromodiphenyl ether
C18933  Chloranil
C19171  Cobalt
C20300  Dimethylarsinous acid
C20316  4-Nitrosobiphenyl
C20319  Hydronitroxide radical
C22355  Benzo[a]pyrene-7,8-diol
C22356  Benzo[a]pyrene-7,8-dione
C22357  17beta-Estradiol-2,3-quinone
C22381  Reactive oxygen species
Reference
PMID:24281075
  Authors
Henkler F, Brinkmann J, Luch A
  Title
The role of oxidative stress in carcinogenesis induced by metals and xenobiotics.
  Journal
Cancers (Basel) 2:376-96 (2010)
DOI:10.3390/cancers2020376
Reference
PMID:22705365
  Authors
Lee JC, Son YO, Pratheeshkumar P, Shi X
  Title
Oxidative stress and metal carcinogenesis.
  Journal
Free Radic Biol Med 53:742-57 (2012)
DOI:10.1016/j.freeradbiomed.2012.06.002
Reference
PMID:32033297
  Authors
Hu Y, Li J, Lou B, Wu R, Wang G, Lu C, Wang H, Pi J, Xu Y
  Title
The Role of Reactive Oxygen Species in Arsenic Toxicity.
  Journal
Biomolecules 10:E240 (2020)
DOI:10.3390/biom10020240
Reference
PMID:33864199
  Authors
Ozturk M, Metin M, Altay V, Bhat RA, Ejaz M, Gul A, Unal BT, Hasanuzzaman M, Nibir L, Nahar K, Bukhari A, Dervash MA, Kawano T
  Title
Arsenic and Human Health: Genotoxicity, Epigenomic Effects, and Cancer Signaling.
  Journal
Biol Trace Elem Res 10.1007/s12011-021-02719-w (2021)
DOI:10.1007/s12011-021-02719-w
Reference
PMID:23510327
  Authors
Hubaux R, Becker-Santos DD, Enfield KS, Rowbotham D, Lam S, Lam WL, Martinez VD
  Title
Molecular features in arsenic-induced lung tumors.
  Journal
Mol Cancer 12:20 (2013)
DOI:10.1186/1476-4598-12-20
Reference
PMID:21648415
  Authors
Naranmandura H, Xu S, Sawata T, Hao WH, Liu H, Bu N, Ogra Y, Lou YJ, Suzuki N
  Title
Mitochondria are the main target organelle for trivalent monomethylarsonous acid (MMA(III))-induced cytotoxicity.
  Journal
Chem Res Toxicol 24:1094-103 (2011)
DOI:10.1021/tx200156k
Reference
PMID:23583964
  Authors
Faita F, Cori L, Bianchi F, Andreassi MG
  Title
Arsenic-induced genotoxicity and genetic susceptibility to arsenic-related pathologies.
  Journal
Int J Environ Res Public Health 10:1527-46 (2013)
DOI:10.3390/ijerph10041527
Reference
PMID:28179585
  Authors
Sage AP, Minatel BC, Ng KW, Stewart GL, Dummer TJB, Lam WL, Martinez VD
  Title
Oncogenomic disruptions in arsenic-induced carcinogenesis.
  Journal
Oncotarget 8:25736-25755 (2017)
DOI:10.18632/oncotarget.15106
Reference
PMID:21414382
  Authors
Jomova K, Valko M
  Title
Advances in metal-induced oxidative stress and human disease.
  Journal
Toxicology 283:65-87 (2011)
DOI:10.1016/j.tox.2011.03.001
Reference
PMID:16430879
  Authors
Valko M, Rhodes CJ, Moncol J, Izakovic M, Mazur M
  Title
Free radicals, metals and antioxidants in oxidative stress-induced cancer.
  Journal
Chem Biol Interact 160:1-40 (2006)
DOI:10.1016/j.cbi.2005.12.009
Reference
PMID:32731582
  Authors
Tumolo M, Ancona V, De Paola D, Losacco D, Campanale C, Massarelli C, Uricchio VF
  Title
Chromium Pollution in European Water, Sources, Health Risk, and Remediation Strategies: An Overview.
  Journal
Int J Environ Res Public Health 17:E5438 (2020)
DOI:10.3390/ijerph17155438
Reference
PMID:28860815
  Authors
Wang Y, Su H, Gu Y, Song X, Zhao J
  Title
Carcinogenicity of chromium and chemoprevention: a brief update.
  Journal
Onco Targets Ther 10:4065-4079 (2017)
DOI:10.2147/OTT.S139262
Reference
PMID:24820114
  Authors
Jin X, Chen M, Song L, Li H, Li Z
  Title
The evaluation of p,p'-DDT exposure on cell adhesion of hepatocellular carcinoma.
  Journal
Toxicology 322:99-108 (2014)
DOI:10.1016/j.tox.2014.05.002
Reference
PMID:20370557
  Authors
Liou GY, Storz P
  Title
Reactive oxygen species in cancer.
  Journal
Free Radic Res 44:479-96 (2010)
DOI:10.3109/10715761003667554
Reference
PMID:11275476
  Authors
Murata M, Tamura A, Tada M, Kawanishi S
  Title
Mechanism of oxidative DNA damage induced by carcinogenic 4-aminobiphenyl.
  Journal
Free Radic Biol Med 30:765-73 (2001)
DOI:10.1016/S0891-5849(01)00463-4
Reference
PMID:31283132
  Authors
  Title
  Journal
Pentachlorophenol and Some Related Compounds (2019)
Reference
PMID:19408893
  Authors
Zhu BZ, Shan GQ
  Title
Potential mechanism for pentachlorophenol-induced carcinogenicity: a novel mechanism for metal-independent production of hydroxyl radicals.
  Journal
Chem Res Toxicol 22:969-77 (2009)
DOI:10.1021/tx900030v
Reference
PMID:22166497
  Authors
McHale CM, Zhang L, Smith MT
  Title
Current understanding of the mechanism of benzene-induced leukemia in humans: implications for risk assessment.
  Journal
Carcinogenesis 33:240-52 (2012)
DOI:10.1093/carcin/bgr297
Reference
PMID:32977499
  Authors
Scharf P, Broering MF, Oliveira da Rocha GH, Farsky SHP
  Title
Cellular and Molecular Mechanisms of Environmental Pollutants on Hematopoiesis.
  Journal
Int J Mol Sci 21:E6996 (2020)
DOI:10.3390/ijms21196996
Reference
PMID:23066403
  Authors
Snyder R
  Title
Leukemia and benzene.
  Journal
Int J Environ Res Public Health 9:2875-93 (2012)
DOI:10.3390/ijerph9082875
Reference
PMID:9118888
  Authors
Snyder R, Hedli CC
  Title
An overview of benzene metabolism.
  Journal
Environ Health Perspect 104 Suppl 6:1165-71 (1996)
DOI:10.1289/ehp.961041165
Reference
PMID:11978484
  Authors
Kawanishi S, Hiraku Y, Murata M, Oikawa S
  Title
The role of metals in site-specific DNA damage with reference to carcinogenesis.
  Journal
Free Radic Biol Med 32:822-32 (2002)
DOI:10.1016/S0891-5849(02)00779-7
Reference
PMID:27919191
  Authors
Das DN, Panda PK, Naik PP, Mukhopadhyay S, Sinha N, Bhutia SK
  Title
Phytotherapeutic approach: a new hope for polycyclic aromatic hydrocarbons induced cellular disorders, autophagic and apoptotic cell death.
  Journal
Toxicol Mech Methods 27:1-17 (2017)
DOI:10.1080/15376516.2016.1268228
Reference
PMID:21910479
  Authors
Shultz CA, Quinn AM, Park JH, Harvey RG, Bolton JL, Maser E, Penning TM.
  Title
Specificity of human aldo-keto reductases, NAD(P)H:quinone oxidoreductase, and carbonyl reductases to redox-cycle polycyclic aromatic hydrocarbon diones and 4-hydroxyequilenin-o-quinone.
  Journal
Chem Res Toxicol 24:2153-66 (2011)
DOI:10.1021/tx200294c
Reference
PMID:25279998
  Authors
Penning TM
  Title
Human aldo-keto reductases and the metabolic activation of polycyclic aromatic hydrocarbons.
  Journal
Chem Res Toxicol 27:1901-17 (2014)
DOI:10.1021/tx500298n
Reference
PMID:10706104
  Authors
Burczynski ME, Penning TM
  Title
Genotoxic polycyclic aromatic hydrocarbon ortho-quinones generated by aldo-keto reductases induce CYP1A1 via nuclear translocation of the aryl hydrocarbon receptor.
  Journal
Cancer Res 60:908-15 (2000)
Reference
PMID:15963346
  Authors
Xue W, Warshawsky D
  Title
Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review.
  Journal
Toxicol Appl Pharmacol 206:73-93 (2005)
DOI:10.1016/j.taap.2004.11.006
Reference
PMID:15142886
  Authors
Chen ZH, Hurh YJ, Na HK, Kim JH, Chun YJ, Kim DH, Kang KS, Cho MH, Surh YJ
  Title
Resveratrol inhibits TCDD-induced expression of CYP1A1 and CYP1B1 and catechol estrogen-mediated oxidative DNA damage in cultured human mammary epithelial cells.
  Journal
Carcinogenesis 25:2005-13 (2004)
DOI:10.1093/carcin/bgh183
Reference
PMID:16684662
  Authors
Rifkind AB
  Title
CYP1A in TCDD toxicity and in physiology-with particular reference to CYP dependent arachidonic acid metabolism and other endogenous substrates.
  Journal
Drug Metab Rev 38:291-335 (2006)
DOI:10.1080/03602530600570107
Reference
PMID:9380738
  Authors
Cavalieri EL, Stack DE, Devanesan PD, Todorovic R, Dwivedy I, Higginbotham S, Johansson SL, Patil KD, Gross ML, Gooden JK, Ramanathan R, Cerny RL, Rogan EG
  Title
Molecular origin of cancer: catechol estrogen-3,4-quinones as endogenous tumor initiators.
  Journal
Proc Natl Acad Sci U S A 94:10937-42 (1997)
DOI:10.1073/pnas.94.20.10937
Reference
PMID:9472688
  Authors
Zhu BT, Conney AH
  Title
Functional role of estrogen metabolism in target cells: review and perspectives.
  Journal
Carcinogenesis 19:1-27 (1998)
DOI:10.1093/carcin/19.1.1
Reference
PMID:19387921
  Authors
McKillop IH, Schrum LW
  Title
Role of alcohol in liver carcinogenesis.
  Journal
Semin Liver Dis 29:222-32 (2009)
DOI:10.1055/s-0029-1214377
Reference
PMID:15603755
  Authors
Gonzalez FJ
  Title
Role of cytochromes P450 in chemical toxicity and oxidative stress: studies with CYP2E1.
  Journal
Mutat Res 569:101-10 (2005)
DOI:10.1016/j.mrfmmm.2004.04.021
Reference
PMID:31864052
  Authors
Montalbano AM, Albano GD, Anzalone G, Moscato M, Gagliardo R, Di Sano C, Bonanno A, Ruggieri S, Cibella F, Profita M
  Title
Cytotoxic and genotoxic effects of the flame retardants (PBDE-47, PBDE-99 and PBDE-209) in human bronchial epithelial cells.
  Journal
Chemosphere 245:125600 (2020)
DOI:10.1016/j.chemosphere.2019.125600
Reference
PMID:33907575
  Authors
Sun HN, Ren CX, Gong YX, Xie DP, Kwon T
  Title
Regulatory function of peroxiredoxin I on 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-induced lung cancer development.
  Journal
Oncol Lett 21:465 (2021)
DOI:10.3892/ol.2021.12726
Reference
PMID:25372613
  Authors
Pluchino LA, Wang HC
  Title
Chronic exposure to combined carcinogens enhances breast cell carcinogenesis with mesenchymal and stem-like cell properties.
  Journal
PLoS One 9:e108698 (2014)
DOI:10.1371/journal.pone.0108698
Reference
PMID:25535943
  Authors
Pluchino LA, Liu AK, Wang HC
  Title
Reactive oxygen species-mediated breast cell carcinogenesis enhanced by multiple carcinogens and intervened by dietary ergosterol and mimosine.
  Journal
Free Radic Biol Med 80:12-26 (2015)
DOI:10.1016/j.freeradbiomed.2014.12.015
Reference
PMID:30327380
  Authors
Moldogazieva NT, Lutsenko SV, Terentiev AA
  Title
Reactive Oxygen and Nitrogen Species-Induced Protein Modifications: Implication in Carcinogenesis and Anticancer Therapy.
  Journal
Cancer Res 78:6040-6047 (2018)
DOI:10.1158/0008-5472.CAN-18-0980
Reference
PMID:32358622
  Authors
Kirtonia A, Sethi G, Garg M
  Title
The multifaceted role of reactive oxygen species in tumorigenesis.
  Journal
Cell Mol Life Sci 77:4459-4483 (2020)
DOI:10.1007/s00018-020-03536-5
Reference
PMID:29449774
  Authors
Kumari S, Badana AK, G MM, G S, Malla R
  Title
Reactive Oxygen Species: A Key Constituent in Cancer Survival.
  Journal
Biomark Insights 13:1177271918755391 (2018)
DOI:10.1177/1177271918755391
Reference
PMID:28881698
  Authors
Gao X, Schottker B
  Title
Reduction-oxidation pathways involved in cancer development: a systematic review of literature reviews.
  Journal
Oncotarget 8:51888-51906 (2017)
DOI:10.18632/oncotarget.17128
Reference
PMID:15769673
  Authors
Storz P
  Title
Reactive oxygen species in tumor progression.
  Journal
Front Biosci 10:1881-96 (2005)
DOI:10.2741/1667
Reference
PMID:28835450
  Authors
Assi M
  Title
The differential role of reactive oxygen species in early and late stages of cancer.
  Journal
Am J Physiol Regul Integr Comp Physiol 313:R646-R653 (2017)
DOI:10.1152/ajpregu.00247.2017
Reference
PMID:15024053
  Authors
Storz P, Doppler H, Toker A
  Title
Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling.
  Journal
Mol Cell Biol 24:2614-26 (2004)
DOI:10.1128/MCB.24.7.2614-2626.2004
Reference
PMID:24998536
  Authors
Nourazarian AR, Kangari P, Salmaninejad A
  Title
Roles of oxidative stress in the development and progression of breast cancer.
  Journal
Asian Pac J Cancer Prev 15:4745-51 (2014)
DOI:10.7314/apjcp.2014.15.12.4745
Reference
PMID:32336668
  Authors
Zheng F, Goncalves FM, Abiko Y, Li H, Kumagai Y, Aschner M
  Title
Redox toxicology of environmental chemicals causing oxidative stress.
  Journal
Redox Biol 34:101475 (2020)
DOI:10.1016/j.redox.2020.101475
Related
pathway
ko00190  Oxidative phosphorylation
ko00980  Metabolism of xenobiotics by cytochrome P450
ko04010  MAPK signaling pathway
ko04064  NF-kappa B signaling pathway
ko04066  HIF-1 signaling pathway
ko04151  PI3K-Akt signaling pathway
ko04370  VEGF signaling pathway
ko05207  Chemical carcinogenesis - receptor activation
ko05211  Renal cell carcinoma
ko05215  Prostate cancer
ko05219  Bladder cancer
ko05221  Acute myeloid leukemia
ko05222  Small cell lung cancer
ko05223  Non-small cell lung cancer
ko05224  Breast cancer
ko05225  Hepatocellular carcinoma
LinkDB

DBGET integrated database retrieval system