KEGG   PATHWAY: oga04216
Entry
oga04216                    Pathway                                
Name
Ferroptosis - Otolemur garnettii (small-eared galago)
Description
Ferroptosis is a regulated form of cell death and characterized by a production of reactive oxygen species (ROS) from accumulated iron and lipid peroxidation. It can be induced by experimental compounds (e.g.,erastin, RSL3) or clinical drugs(e.g., sulfasalazine, sorafenib) in cancer cell and certain normal cells. It is involved in multiple physiological and pathological processes, such as cancer cell death, neurodegenerative disease, tissue damage and acute renal failure.
Class
Cellular Processes; Cell growth and death
Pathway map
oga04216  Ferroptosis
oga04216

Other DBs
GO: 0097707
Organism
Otolemur garnettii (small-eared galago) [GN:oga]
Gene
100942646  SLC3A2; 4F2 cell-surface antigen heavy chain [KO:K06519]
100962725  SLC7A11; cystine/glutamate transporter [KO:K13869]
100963622  TP53; cellular tumor antigen p53 [KO:K04451]
100959223  GCLC; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
100946049  GCLM; glutamate--cysteine ligase regulatory subunit [KO:K11205]
100960047  GSS; glutathione synthetase isoform X1 [KO:K21456] [EC:6.3.2.3]
100963823  GPX4; phospholipid hydroperoxide glutathione peroxidase, mitochondrial isoform X1 [KO:K05361] [EC:1.11.1.12]
100944923  ACSL5; long-chain-fatty-acid--CoA ligase 5 [KO:K01897] [EC:6.2.1.3]
100962839  ACSL3; long-chain-fatty-acid--CoA ligase 3 [KO:K01897] [EC:6.2.1.3]
100947291  ACSL4; long-chain-fatty-acid--CoA ligase 4 isoform X2 [KO:K01897] [EC:6.2.1.3]
100958751  ACSL6; long-chain-fatty-acid--CoA ligase 6 isoform X2 [KO:K01897] [EC:6.2.1.3]
100960693  ACSL1; long-chain-fatty-acid--CoA ligase 1 isoform X2 [KO:K01897] [EC:6.2.1.3]
100946424  LPCAT3; lysophospholipid acyltransferase 5 [KO:K13515] [EC:2.3.1.23 2.3.1.-]
100953458  ALOX15; arachidonate 15-lipoxygenase [KO:K00460] [EC:1.13.11.33]
100942303  SAT1; diamine acetyltransferase 1 [KO:K00657] [EC:2.3.1.57]
100966045  SAT2; diamine acetyltransferase 2 [KO:K00657] [EC:2.3.1.57]
100967087  inhibitor of carbonic anhydrase isoform X1 [KO:K14736]
100941133  serotransferrin [KO:K14736]
100965409  TFRC; transferrin receptor protein 1 [KO:K06503]
100945790  STEAP3; metalloreductase STEAP3 isoform X3 [KO:K10142] [EC:1.16.1.-]
100948411  SLC11A2; natural resistance-associated macrophage protein 2 isoform X3 [KO:K21398]
100950746  SLC39A8; zinc transporter ZIP8 [KO:K14714]
100941581  SLC39A14; zinc transporter ZIP14 isoform X2 [KO:K14720]
100953673  poly(rC)-binding protein 2-like [KO:K13162]
100940398  LOW QUALITY PROTEIN: poly(rC)-binding protein 2-like [KO:K13162]
100958231  SLC40A1; solute carrier family 40 member 1 [KO:K14685]
100959117  LOW QUALITY PROTEIN: ceruloplasmin-like [KO:K13624] [EC:1.16.3.1]
100956170  CP; ceruloplasmin [KO:K13624] [EC:1.16.3.1]
100960795  PCBP1; poly(rC)-binding protein 1 [KO:K12889]
100947386  FTH1; ferritin heavy chain [KO:K00522] [EC:1.16.3.1]
100946473  FTL; ferritin light chain [KO:K13625]
100963656  MAP1LC3C; microtubule-associated proteins 1A/1B light chain 3C [KO:K10435]
100956121  MAP1LC3B; microtubule-associated proteins 1A/1B light chain 3B [KO:K10435]
100957512  MAP1LC3A; microtubule-associated proteins 1A/1B light chain 3A [KO:K10435]
100944238  ATG5; autophagy protein 5 isoform X1 [KO:K08339]
100958520  ATG7; ubiquitin-like modifier-activating enzyme ATG7 [KO:K08337]
100947212  NCOA4; nuclear receptor coactivator 4 isoform X2 [KO:K09289]
100959325  PRNP; major prion protein [KO:K05634]
100965040  HMOX1; heme oxygenase 1 [KO:K00510] [EC:1.14.14.18]
100962937  VDAC2; voltage-dependent anion-selective channel protein 2 isoform X1 [KO:K15040]
100945532  VDAC3; voltage-dependent anion-selective channel protein 3 [KO:K15041]
100951499  cytochrome b-245 heavy chain [KO:K21421] [EC:1.-.-.-]
100956862  FTMT; ferritin, mitochondrial [KO:K18495] [EC:1.16.3.1]
Compound
C00010  CoA
C00024  Acetyl-CoA
C00025  L-Glutamate
C00027  Hydrogen peroxide
C00032  Heme
C00051  Glutathione
C00097  L-Cysteine
C00127  Glutathione disulfide
C00129  Isopentenyl diphosphate
C00219  Arachidonate
C00356  (S)-3-Hydroxy-3-methylglutaryl-CoA
C00418  (R)-Mevalonate
C00491  L-Cystine
C00669  gamma-L-Glutamyl-L-cysteine
C02249  Arachidonyl-CoA
C02477  alpha-Tocopherol
C11378  Ubiquinone-10
C14818  Fe2+
C14819  Fe3+
C16170  (7Z,10Z,13Z,16Z)-Docosatetraenoyl-CoA
C16527  Adrenic acid
C16844  Hydroxyl radical
C21478  Erastin
C21479  RSL3
C21480  1-Octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine
C21481  1-Octadecanoyl-2-(7Z,10Z,13Z,16Z-docosatetraenoyl)-sn-glycero-3-phosphoethanolamine
C21482  1-Octadecanoyl-2-(15S-hydroxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine
C21483  1-Octadecanoyl-2-(15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine
C21484  1-Octadecanoyl-sn-glycero-3-phosphoethanolamine
D00448  Sulfasalazine (USP/INN)
D08524  Sorafenib (USAN/INN)
Reference
  Authors
Conrad M, Angeli JP, Vandenabeele P, Stockwell BR
  Title
Regulated necrosis: disease relevance and therapeutic opportunities.
  Journal
Nat Rev Drug Discov 15:348-66 (2016)
DOI:10.1038/nrd.2015.6
Reference
  Authors
Yang WS, Stockwell BR
  Title
Ferroptosis: Death by Lipid Peroxidation.
  Journal
Trends Cell Biol 26:165-76 (2016)
DOI:10.1016/j.tcb.2015.10.014
Reference
  Authors
Kagan VE, Mao G, Qu F, Angeli JP, Doll S, Croix CS, Dar HH, Liu B, Tyurin VA, Ritov VB, Kapralov AA, Amoscato AA, Jiang J, Anthonymuthu T, Mohammadyani D, Yang Q, Proneth B, Klein-Seetharaman J, Watkins S, Bahar I, Greenberger J, Mallampalli RK, Stockwell BR, Tyurina YY, Conrad M, Bayir H
  Title
Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis.
  Journal
Nat Chem Biol 13:81-90 (2017)
DOI:10.1038/nchembio.2238
Reference
  Authors
D'Herde K, Krysko DV
  Title
Ferroptosis: Oxidized PEs trigger death.
  Journal
Nat Chem Biol 13:4-5 (2017)
DOI:10.1038/nchembio.2261
Reference
  Authors
Guiney SJ, Adlard PA, Bush AI, Finkelstein DI, Ayton S
  Title
Ferroptosis and cell death mechanisms in Parkinson's disease.
  Journal
Neurochem Int 104:34-48 (2017)
DOI:10.1016/j.neuint.2017.01.004
Reference
  Authors
Bogdan AR, Miyazawa M, Hashimoto K, Tsuji Y
  Title
Regulators of Iron Homeostasis: New Players in Metabolism, Cell Death, and Disease.
  Journal
Trends Biochem Sci 41:274-86 (2016)
DOI:10.1016/j.tibs.2015.11.012
Reference
  Authors
Xie Y, Hou W, Song X, Yu Y, Huang J, Sun X, Kang R, Tang D
  Title
Ferroptosis: process and function.
  Journal
Cell Death Differ 23:369-79 (2016)
DOI:10.1038/cdd.2015.158
Reference
  Authors
Murphy ME
  Title
Ironing out how p53 regulates ferroptosis.
  Journal
Proc Natl Acad Sci U S A 113:12350-12352 (2016)
DOI:10.1073/pnas.1615159113
Reference
  Authors
Muckenthaler MU, Rivella S, Hentze MW, Galy B
  Title
A Red Carpet for Iron Metabolism.
  Journal
Cell 168:344-361 (2017)
DOI:10.1016/j.cell.2016.12.034
Reference
  Authors
Yu H, Guo P, Xie X, Wang Y, Chen G
  Title
Ferroptosis, a new form of cell death, and its relationships with tumourous diseases.
  Journal
J Cell Mol Med 21:648-657 (2017)
DOI:10.1111/jcmm.13008
Reference
  Authors
Wang SJ, Ou Y, Jiang L, Gu W
  Title
Ferroptosis: A missing puzzle piece in the p53 blueprint?
  Journal
Mol Cell Oncol 3:e1046581 (2016)
DOI:10.1080/23723556.2015.1046581
Reference
  Authors
Cao JY, Dixon SJ
  Title
Mechanisms of ferroptosis.
  Journal
Cell Mol Life Sci 73:2195-209 (2016)
DOI:10.1007/s00018-016-2194-1
Reference
  Authors
Mancias JD, Pontano Vaites L, Nissim S, Biancur DE, Kim AJ, Wang X, Liu Y, Goessling W, Kimmelman AC, Harper JW
  Title
Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis.
  Journal
Elife 4:e10308 (2015)
DOI:10.7554/eLife.10308
Reference
  Authors
Wang YQ, Chang SY, Wu Q, Gou YJ, Jia L, Cui YM, Yu P, Shi ZH, Wu WS, Gao G, Chang YZ
  Title
The Protective Role of Mitochondrial Ferritin on Erastin-Induced Ferroptosis.
  Journal
Front Aging Neurosci 8:308 (2016)
DOI:10.3389/fnagi.2016.00308
Reference
  Authors
Kwon MY, Park E, Lee SJ, Chung SW
  Title
Heme oxygenase-1 accelerates erastin-induced ferroptotic cell death.
  Journal
Oncotarget 6:24393-403 (2015)
DOI:10.18632/oncotarget.5162
Reference
  Authors
Reed JC, Pellecchia M
  Title
Ironing out cell death mechanisms.
  Journal
Cell 149:963-5 (2012)
DOI:10.1016/j.cell.2012.05.009
Related
pathway
oga00480  Glutathione metabolism
oga00900  Terpenoid backbone biosynthesis
KO pathway
ko04216   
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