KEGG   PATHWAY: gfr04216
Entry
gfr04216                    Pathway                                
Name
Ferroptosis - Geospiza fortis (medium ground-finch)
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
gfr04216  Ferroptosis
gfr04216

Other DBs
GO: 0097707
Organism
Geospiza fortis (medium ground-finch) [GN:gfr]
Gene
102034129  cystine/glutamate transporter-like [KO:K13869]
102042265  SLC7A11; solute carrier family 7 member 11 [KO:K13869]
102035643  GCLC; glutamate-cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
102038019  GSS; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
102045367  GPX4; glutathione peroxidase 4 [KO:K05361] [EC:1.11.1.12]
102033249  ACSL5; acyl-CoA synthetase long-chain family member 5 [KO:K01897] [EC:6.2.1.3]
102035319  ACSL1; acyl-CoA synthetase long-chain family member 1 [KO:K01897] [EC:6.2.1.3]
102041385  ACSL4; acyl-CoA synthetase long-chain family member 4 [KO:K01897] [EC:6.2.1.3]
102037766  ACSL6; acyl-CoA synthetase long-chain family member 6 [KO:K01897] [EC:6.2.1.3]
102037784  ACSL3; acyl-CoA synthetase long-chain family member 3 [KO:K01897] [EC:6.2.1.3]
102041216  LPCAT3; lysophosphatidylcholine acyltransferase 3 [KO:K13515] [EC:2.3.1.23 2.3.1.-]
102034901  SAT1; spermidine/spermine N1-acetyltransferase 1 [KO:K00657] [EC:2.3.1.57]
102033474  diamine acetyltransferase 1-like [KO:K00657] [EC:2.3.1.57]
102034411  TF; transferrin [KO:K14736]
102041725  TFRC; transferrin receptor [KO:K06503]
102043446  STEAP3; STEAP3 metalloreductase [KO:K10142] [EC:1.16.1.-]
102034086  natural resistance-associated macrophage protein 2-like [KO:K21398]
102036794  SLC39A8; solute carrier family 39 member 8 [KO:K14714]
102039907  SLC39A14; solute carrier family 39 member 14 [KO:K14720]
102045110  PCBP2; poly(rC) binding protein 2 [KO:K13162]
102036400  SLC40A1; solute carrier family 40 member 1 [KO:K14685]
102036461  CP; ceruloplasmin [KO:K13624] [EC:1.16.3.1]
102040223  FTH1; ferritin heavy chain 1 [KO:K00522] [EC:1.16.3.1]
102037259  MAP1LC3C; microtubule associated protein 1 light chain 3 gamma [KO:K10435]
102034522  MAP1LC3B; microtubule associated protein 1 light chain 3 beta [KO:K10435]
102044371  MAP1LC3A; microtubule-associated proteins 1A/1B light chain 3A [KO:K10435]
102040398  ATG5; autophagy related 5 [KO:K08339]
102035766  ATG7; autophagy related 7 [KO:K08337]
102045382  NCOA4; nuclear receptor coactivator 4 [KO:K09289]
102043181  HMOX1; heme oxygenase 1 [KO:K00510] [EC:1.14.14.18]
102038775  VDAC2; voltage dependent anion channel 2 [KO:K15040]
102034080  VDAC3; voltage dependent anion channel 3 [KO:K15041]
102043904  cytochrome b-245 heavy chain [KO:K21421] [EC: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
gfr00480  Glutathione metabolism
gfr00900  Terpenoid backbone biosynthesis
KO pathway
ko04216   
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