HMOX1: Difference between revisions

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Revision as of 00:15, 27 October 2017

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase mediates the first step of heme catabolism, it cleaves heme to form biliverdin.

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.^[1] The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.^[2]

The HMOX gene is located on the long (q) arm of chromosome 22 at position 12.3, from base pair 34,101,636 to base pair 34,114,748.

Related conditions

Heme oxygenase-1 deficiency

Anti-inflammatory effect

The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its anti-inflammatory properties by up-regulation of interleukin 10 (IL-10) and interleukin 1 receptor antagonist (IL-1RA) expression.^[3]

References

↑ Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. p. 876. ISBN 978-0-7167-7108-1.
↑ "Entrez Gene: HMOX1 heme oxygenase (decycling) 1".
↑ Piantadosi CA, Withers CM, Bartz RR, MacGarvey NC, Fu P, Sweeney TE, Welty-Wolf KE, Suliman HB (May 2011). "Heme oxygenase-1 couples activation of mitochondrial biogenesis to anti-inflammatory cytokine expression". J. Biol. Chem. 286 (18): 16374–85. doi:10.1074/jbc.M110.207738. PMC 3091243. PMID 21454555.

Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S (1999). "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency". J Clin Invest. 103 (1): 129–35. doi:10.1172/JCI4165. PMC 407858. PMID 9884342.
Zhang Z, Song Y, Zhang Z, Li D, Zhu H, Liang R, Gu Y, Pang Y, Qi J, Wu H, Wang J (2016). "Distinct role of heme oxygenase-1 in early- and late-stage intracerebral hemorrhage in 12-month-old mice". J Cereb Blood Flow Metab. doi:10.1177/0271678X16655814. PMID 27317654.
Wang J, Doré S (2007). "Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage". Brain. 130 (6): 1643–52. doi:10.1093/brain/awm095. PMC 2291147. PMID 17525142.
Soares MP, Brouard S, Smith RN, Bach FH (2002). "Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs". Immunol. Rev. 184: 275–85. doi:10.1034/j.1600-065x.2001.1840124.x. PMID 12086318.
Morse D, Choi AM (2002). "Heme oxygenase-1: the "emerging molecule" has arrived". Am. J. Respir. Cell Mol. Biol. 27 (1): 8–16. doi:10.1165/ajrcmb.27.1.4862. PMID 12091240.
Buelow R, Tullius SG, Volk HD (2002). "Protection of grafts by hemoxygenase-1 and its toxic product carbon monoxide". Am. J. Transplant. 1 (4): 313–5. doi:10.1034/j.1600-6143.2001.10404.x. PMID 12099373.
Ishikawa K (2003). "Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders". Curr. Pharm. Des. 9 (30): 2489–97. doi:10.2174/1381612033453767. PMID 14529548.
Exner M, Minar E, Wagner O, Schillinger M (2005). "The role of heme oxygenase-1 promoter polymorphisms in human disease". Free Radic. Biol. Med. 37 (8): 1097–104. doi:10.1016/j.freeradbiomed.2004.07.008. PMID 15451051.
Ozono R (2006). "New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway". Current pharmaceutical biotechnology. 7 (2): 87–93. doi:10.2174/138920106776597630. PMID 16724942.
Tracz MJ, Alam J, Nath KA (2007). "Physiology and pathophysiology of heme: implications for kidney disease". J. Am. Soc. Nephrol. 18 (2): 414–20. doi:10.1681/ASN.2006080894. PMID 17229906.
Chang CF, Cho S, Wang J (2014). "(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways". Ann Clin Transl Neurol. 1 (4): 258–271. doi:10.1002/acn3.54. PMC 3984761. PMID 24741667.
Hill-Kapturczak N, Agarwal A (2007). "Haem oxygenase-1--a culprit in vascular and renal damage?". Nephrol. Dial. Transplant. 22 (6): 1495–9. doi:10.1093/ndt/gfm093. PMID 17389623.

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[1] Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. p. 876. ISBN 978-0-7167-7108-1.

[2] "Entrez Gene: HMOX1 heme oxygenase (decycling) 1".

[pmid21454555-3] Piantadosi CA, Withers CM, Bartz RR, MacGarvey NC, Fu P, Sweeney TE, Welty-Wolf KE, Suliman HB (May 2011). "Heme oxygenase-1 couples activation of mitochondrial biogenesis to anti-inflammatory cytokine expression". J. Biol. Chem. 286 (18): 16374–85. doi:10.1074/jbc.M110.207738. PMC 3091243. PMID 21454555.

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[2]

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''HMOX1''' ('''heme oxygenase (decycling) 1''') is a [[human]] [[gene]] that encodes for the enzyme [[Heme oxygenase|heme oxygenase 1]] ({{EC number|1.14.99.3}}). Heme oxygenase mediates the first step of [[heme#Degradation|heme catabolism]], it cleaves [[heme]] to form [[biliverdin]].
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image = PBB_Protein_HMOX1_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n3u.
- | PDB = {{PDB2|1n3u}}, {{PDB2|1n45}}, {{PDB2|1ni6}}, {{PDB2|1oyk}}, {{PDB2|1oyl}}, {{PDB2|1oze}}, {{PDB2|1ozl}}, {{PDB2|1ozr}}, {{PDB2|1ozw}}, {{PDB2|1s13}}, {{PDB2|1s8c}}, {{PDB2|1t5p}}, {{PDB2|1twn}}, {{PDB2|1twr}}, {{PDB2|1xjz}}, {{PDB2|1xk0}}, {{PDB2|1xk1}}, {{PDB2|1xk2}}, {{PDB2|1xk3}}
- | Name = Heme oxygenase (decycling) 1
- | HGNCid = 5013
- | Symbol = HMOX1
- | AltSymbols =; HO-1; bK286B10
- | OMIM = 141250
- | ECnumber =
- | Homologene = 31075
- | MGIid = 96163
- | GeneAtlas_image1 = PBB_GE_HMOX1_203665_at_tn.png
- | Function = {{GNF_GO|id=GO:0004392 |text = heme oxygenase (decyclizing) activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
- | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}}
- | Process = {{GNF_GO|id=GO:0006788 |text = heme oxidation}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 3162
-    | Hs_Ensembl = ENSG00000100292
-    | Hs_RefseqProtein = NP_002124
-    | Hs_RefseqmRNA = NM_002133
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 22
-    | Hs_GenLoc_start = 34107057
-    | Hs_GenLoc_end = 34120172
-    | Hs_Uniprot = P09601
-    | Mm_EntrezGene = 15368
-    | Mm_Ensembl = ENSMUSG00000005413
-    | Mm_RefseqmRNA = NM_010442
-    | Mm_RefseqProtein = NP_034572
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 8
-    | Mm_GenLoc_start = 77989694
-    | Mm_GenLoc_end = 77996661
-    | Mm_Uniprot = Q3U5H8
-  }}
-}}
-'''HMOX1''' ('''heme oxygenase (decycling) 1''') is a [[human]] [[gene]] that encodes for the enzyme [[Heme oxygenase|heme oxygenase 1]] (EC 1.14.99.3). Heme oxygenase is an essential enzyme in [[heme catabolism]], it cleaves [[heme]] to form [[biliverdin]].
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.<ref>{{cite web | title = Entrez Gene: HMOX1 heme oxygenase (decycling) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3162| accessdate = }}</ref>
+| summary_text = Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, [[carbon monoxide]], and [[ferrous]] [[iron]].<ref>{{Cite book|title = Lehninger's Principles of Biochemistry, 5th Edition|publisher = W.H. Freeman and Company|year = 2008|isbn = 978-0-7167-7108-1|location = New York|pages = 876}}</ref> The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.<ref>{{cite web | title = Entrez Gene: HMOX1 heme oxygenase (decycling) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3162| accessdate = }}</ref>
 }}
-The HMOX gene is located on the long (q) arm of [[chromosome 22 (human)|chromosome 22]] at position 13.1, from base pair 34,101,636 to base pair 34,114,748.
+The HMOX gene is located on the long (q) arm of [[chromosome 22 (human)|chromosome 22]] at position 12.3, from base pair 34,101,636 to base pair 34,114,748.
+== Related conditions ==
+* [[Heme oxygenase-1 deficiency]]
-==Related conditions==
+== Anti-inflammatory effect ==
-[[Heme oxygenase-1 deficiency]]
+The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its anti-inflammatory properties by  up-regulation of [[interleukin 10]] (IL-10) and [[interleukin 1 receptor antagonist]] (IL-1RA) expression.<ref name="pmid21454555">{{cite journal |vauthors=Piantadosi CA, Withers CM, Bartz RR, MacGarvey NC, Fu P, Sweeney TE, Welty-Wolf KE, Suliman HB | title = Heme oxygenase-1 couples activation of mitochondrial biogenesis to anti-inflammatory cytokine expression | journal = J. Biol. Chem. | volume = 286 | issue = 18 | pages = 16374–85 |date=May 2011 | pmid = 21454555 | pmc = 3091243 | doi = 10.1074/jbc.M110.207738 }}</ref>
-==See also==
+== See also ==
 * [[HMOX2]]
+* [[Focal segmental glomerulosclerosis]]
 ==References==
-{{reflist|2}}
+{{reflist}}
-==Further reading==
+== Further reading ==
 {{refbegin | 2}}
-* {{cite journal | author=Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S | title=Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency | journal=J Clin Invest | year=1999 | pages=129-35 | volume=103 | issue=1  | id=PMID 9884342}}
+* {{cite journal |vauthors=Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S | title=Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency | journal=J Clin Invest | year=1999 | pages=129–35 | volume=103 | issue=1  | pmid=9884342 | doi=10.1172/JCI4165 | pmc=407858}}
-{{PBB_Further_reading
+* {{cite journal |vauthors=Zhang Z, Song Y, Zhang Z, Li D, Zhu H, Liang R, Gu Y, Pang Y, Qi J, Wu H, Wang J | title=Distinct role of heme oxygenase-1 in early- and late-stage intracerebral hemorrhage in 12-month-old mice | journal=J Cereb Blood Flow Metab| year=2016 | pmid=27317654 | doi=10.1177/0271678X16655814 }}
-| citations =
+*{{cite journal |vauthors=Wang J, Doré S | title=Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage.| journal=Brain | year=2007 | pages=1643–52 | volume=130 | issue=6  | pmid=17525142| doi=10.1093/brain/awm095 | pmc=2291147}}
-*{{cite journal  | author=Soares MP, Brouard S, Smith RN, Bach FH |title=Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs. |journal=Immunol. Rev. |volume=184 |issue=  |pages= 275-85 |year= 2002 |pmid= 12086318 |doi=  }}
+*{{cite journal  |vauthors=Soares MP, Brouard S, Smith RN, Bach FH |title=Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs |journal=Immunol. Rev. |volume=184 |issue=  |pages= 275–85 |year= 2002 |pmid= 12086318 |doi=10.1034/j.1600-065x.2001.1840124.x  }}
-*{{cite journal  | author=Morse D, Choi AM |title=Heme oxygenase-1: the "emerging molecule" has arrived. |journal=Am. J. Respir. Cell Mol. Biol. |volume=27 |issue= 1 |pages= 8-16 |year= 2002 |pmid= 12091240 |doi=  }}
+*{{cite journal  |vauthors=Morse D, Choi AM |title=Heme oxygenase-1: the "emerging molecule" has arrived |journal=Am. J. Respir. Cell Mol. Biol. |volume=27 |issue= 1 |pages= 8–16 |year= 2002 |pmid= 12091240 |doi=  10.1165/ajrcmb.27.1.4862}}
-*{{cite journal  | author=Buelow R, Tullius SG, Volk HD |title=Protection of grafts by hemoxygenase-1 and its toxic product carbon monoxide. |journal=Am. J. Transplant. |volume=1 |issue= 4 |pages= 313-5 |year= 2002 |pmid= 12099373 |doi=  }}
+*{{cite journal  |vauthors=Buelow R, Tullius SG, Volk HD |title=Protection of grafts by hemoxygenase-1 and its toxic product carbon monoxide |journal=Am. J. Transplant. |volume=1 |issue= 4 |pages= 313–5 |year= 2002 |pmid= 12099373 |doi=10.1034/j.1600-6143.2001.10404.x  }}
-*{{cite journal  | author=Ishikawa K |title=Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders. |journal=Curr. Pharm. Des. |volume=9 |issue= 30 |pages= 2489-97 |year= 2003 |pmid= 14529548 |doi=  }}
+*{{cite journal  | author=Ishikawa K |title=Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders |journal=Curr. Pharm. Des. |volume=9 |issue= 30 |pages= 2489–97 |year= 2003 |pmid= 14529548 |doi=10.2174/1381612033453767  }}
-*{{cite journal  | author=Exner M, Minar E, Wagner O, Schillinger M |title=The role of heme oxygenase-1 promoter polymorphisms in human disease. |journal=Free Radic. Biol. Med. |volume=37 |issue= 8 |pages= 1097-104 |year= 2005 |pmid= 15451051 |doi= 10.1016/j.freeradbiomed.2004.07.008 }}
+*{{cite journal  |vauthors=Exner M, Minar E, Wagner O, Schillinger M |title=The role of heme oxygenase-1 promoter polymorphisms in human disease |journal=Free Radic. Biol. Med. |volume=37 |issue= 8 |pages= 1097–104 |year= 2005 |pmid= 15451051 |doi= 10.1016/j.freeradbiomed.2004.07.008 }}
-*{{cite journal  | author=Ozono R |title=New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway. |journal=Current pharmaceutical biotechnology |volume=7 |issue= 2 |pages= 87-93 |year= 2006 |pmid= 16724942 |doi=  }}
+*{{cite journal  | author=Ozono R |title=New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway |journal=Current pharmaceutical biotechnology |volume=7 |issue= 2 |pages= 87–93 |year= 2006 |pmid= 16724942 |doi=10.2174/138920106776597630  }}
-*{{cite journal  | author=Tracz MJ, Alam J, Nath KA |title=Physiology and pathophysiology of heme: implications for kidney disease. |journal=J. Am. Soc. Nephrol. |volume=18 |issue= 2 |pages= 414-20 |year= 2007 |pmid= 17229906 |doi= 10.1681/ASN.2006080894 }}
+*{{cite journal  |vauthors=Tracz MJ, Alam J, Nath KA |title=Physiology and pathophysiology of heme: implications for kidney disease |journal=J. Am. Soc. Nephrol. |volume=18 |issue= 2 |pages= 414–20 |year= 2007 |pmid= 17229906 |doi= 10.1681/ASN.2006080894 }}
-*{{cite journal  | author=Hill-Kapturczak N, Agarwal A |title=Haem oxygenase-1--a culprit in vascular and renal damage? |journal=Nephrol. Dial. Transplant. |volume=22 |issue= 6 |pages= 1495-9 |year= 2007 |pmid= 17389623 |doi= 10.1093/ndt/gfm093 }}
+*{{cite journal  |vauthors=Chang CF, Cho S, Wang J |title=(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways |journal=Ann Clin Transl Neurol. |volume=1 |issue= 4 |pages= 258–271 |year= 2014 |pmid= 24741667 |doi= 10.1002/acn3.54 |pmc=3984761}}
-}}
+*{{cite journal  |vauthors=Hill-Kapturczak N, Agarwal A |title=Haem oxygenase-1--a culprit in vascular and renal damage? |journal=Nephrol. Dial. Transplant. |volume=22 |issue= 6 |pages= 1495–9 |year= 2007 |pmid= 17389623 |doi= 10.1093/ndt/gfm093 }}
 {{refend}}
+{{PDB Gallery|geneid=3162}}
+{{Dioxygenases}}
+{{Enzymes}}
+{{Portal bar|Molecular and Cellular Biology|border=no}}
+[[Category:Human genes]]
+[[Category:EC 1.14.99]]
 {{genetics-stub}}
-{{Dioxygenases}}
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-{{WikiDoc Sources}}

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

HMOX1: Difference between revisions

Revision as of 00:15, 27 October 2017

Contents

Related conditions

Anti-inflammatory effect

See also

References

Further reading

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