KEGG   PATHWAY: umr04216
Entry
umr04216                    Pathway                                
Name
Ferroptosis - Ursus maritimus (polar bear)
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
umr04216  Ferroptosis
umr04216

Other DBs
GO: 0097707
Organism
Ursus maritimus (polar bear) [GN:umr]
Gene
103678209  SLC3A2; 4F2 cell-surface antigen heavy chain [KO:K06519]
103657957  SLC7A11; cystine/glutamate transporter isoform X1 [KO:K13869]
103660368  TP53; cellular tumor antigen p53 isoform X1 [KO:K04451]
103664124  GCLC; glutamate--cysteine ligase catalytic subunit isoform X1 [KO:K11204] [EC:6.3.2.2]
103669404  GCLM; glutamate--cysteine ligase regulatory subunit [KO:K11205]
103669812  GSS; glutathione synthetase isoform X1 [KO:K21456] [EC:6.3.2.3]
103681777  GPX4; phospholipid hydroperoxide glutathione peroxidase [KO:K05361] [EC:1.11.1.12]
103662726  ACSL3; long-chain-fatty-acid--CoA ligase 3 isoform X1 [KO:K01897] [EC:6.2.1.3]
103681011  ACSL1; long-chain-fatty-acid--CoA ligase 1 [KO:K01897] [EC:6.2.1.3]
103679743  ACSL4; long-chain-fatty-acid--CoA ligase 4 isoform X1 [KO:K01897] [EC:6.2.1.3]
103657137  ACSL5; long-chain-fatty-acid--CoA ligase 5 [KO:K01897] [EC:6.2.1.3]
103670507  ACSL6; long-chain-fatty-acid--CoA ligase 6 isoform X2 [KO:K01897] [EC:6.2.1.3]
103656177  LPCAT3; lysophospholipid acyltransferase 5 [KO:K13515] [EC:2.3.1.23 2.3.1.-]
103660453  ALOX15; polyunsaturated fatty acid lipoxygenase ALOX15 [KO:K00460] [EC:1.13.11.33]
103660477  SAT2; thialysine N-epsilon-acetyltransferase [KO:K00657] [EC:2.3.1.57]
103668270  SAT1; diamine acetyltransferase 1 [KO:K00657] [EC:2.3.1.57]
103678998  inhibitor of carbonic anhydrase isoform X1 [KO:K14736]
103679015  LOW QUALITY PROTEIN: serotransferrin-like [KO:K14736]
103678941  TFRC; transferrin receptor protein 1 isoform X1 [KO:K06503]
103658631  STEAP3; metalloreductase STEAP3 [KO:K10142] [EC:1.16.1.-]
103675484  SLC11A2; natural resistance-associated macrophage protein 2 isoform X1 [KO:K21398]
103677987  SLC39A8; metal cation symporter ZIP8 [KO:K14714]
103673319  SLC39A14; metal cation symporter ZIP14 [KO:K14720]
103675535  PCBP2; poly(rC)-binding protein 2 isoform X1 [KO:K13162]
103659667  SLC40A1; solute carrier family 40 member 1 [KO:K14685]
103678034  ceruloplasmin-like [KO:K13624] [EC:1.16.3.1]
103678054  ceruloplasmin isoform X1 [KO:K13624] [EC:1.16.3.1]
103671366  PCBP1; poly(rC)-binding protein 1 [KO:K12889]
103678175  FTH1; ferritin heavy chain [KO:K00522] [EC:1.16.3.1]
103668210  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103668217  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103668221  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103668222  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103668227  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103668313  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103675682  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
121103384  ferritin heavy chain-like [KO:K00522] [EC:1.16.3.1]
103657109  FTL; ferritin light chain [KO:K13625]
103668234  ferritin light chain-like [KO:K13625]
103661033  ferritin light chain-like [KO:K13625]
103661469  LOW QUALITY PROTEIN: ferritin light chain-like [KO:K13625]
103666643  MAP1LC3C; microtubule-associated proteins 1A/1B light chain 3C [KO:K10435]
103673943  MAP1LC3B; microtubule-associated proteins 1A/1B light chain 3B [KO:K10435]
103669916  MAP1LC3A; microtubule-associated proteins 1A/1B light chain 3A [KO:K10435]
103675849  ATG5; autophagy protein 5 isoform X2 [KO:K08339]
103669551  ATG7; ubiquitin-like modifier-activating enzyme ATG7 isoform X1 [KO:K08337]
103667907  NCOA4; nuclear receptor coactivator 4 isoform X1 [KO:K09289]
103674536  major prion protein [KO:K05634]
103676557  HMOX1; heme oxygenase 1 isoform X1 [KO:K00510] [EC:1.14.14.18]
103667846  VDAC2; voltage-dependent anion-selective channel protein 2 [KO:K15040]
103677056  VDAC3; voltage-dependent anion-selective channel protein 3 [KO:K15041]
103668228  cytochrome b-245 heavy chain [KO:K21421] [EC:1.-.-.-]
103670582  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
PMID:26775689
  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
PMID:26653790
  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
PMID:27842066
  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
PMID:27842067
  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
PMID:28082232
  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
PMID:26725301
  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
PMID:26794443
  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
PMID:27791175
  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
PMID:28129536
  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
PMID:27860262
  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
PMID:27314071
  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
PMID:27048822
  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
PMID:26436293
  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
PMID:28066232
  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
PMID:26405158
  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
PMID:22632964
  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
umr00480  Glutathione metabolism
umr00900  Terpenoid backbone biosynthesis
KO pathway
ko04216   
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