Intracellular oxygen transport (Homo sapiens)

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1, 6, 10, 11, 15...2, 4, 5, 8, 12...3, 13, 25, 283, 13, 25, 287, 9, 29, 3012, 18, 229, 24, 29, 30cytosolheme heme O2 heme NGB:ferroheme b:O2CYGB dimer:O2heme NGB NGB:ferroheme bheme O2MB CYGB CYGB O2 CYGB dimerMB heme MB:ferroheme b:O2NGB MB:ferroheme bO2 14


Description

Globins are heme-containing proteins that reversibly bind molecular oxygen. Humans contain at least 5 types of globins: hemoglobins, myoglobin, cytoglobin, neuroglobin, and androglobin (reviewed in Burmester et al. 2014). Myoglobin, neuroglobin, and cytoglobin are cytosolic globins with similar affinities for oxygen (reviewed in Hankeln et al. 2005). Androglobin is a more distantly related globin of uncertain function that is expressed in testes (Hoogewijs et al. 2012). Myoglobin is predominantly expressed in muscle tissue (reviewed in Helbo et al. 2013), neuroglobin is expressed in neurons, and cytoglobin is expressed in connective tissue fibroblasts and smooth muscle cells (reviewed in Pesce et al. 2002, Hankeln et al. 2004, Ascenzi et al. 2016). Whereas myoglobin contains pentacoordinated heme iron, neuroglobin and cytoglobin contain hexacoordinated heme iron: the iron atom is bound by 4 nitrogen atoms of heme and 2 histidine residues of the globin. Binding by one of the histidines is reversible, which allows the iron atom to bind various ligands such as molecular oxygen, carbon monoxide, and nitric oxide (reviewed in Kakar et al. 2010). Neuroglobin may function in oxygen homeostasis, however the importance of its oxygen-binding activity is unclear (reviewed in Pesce et al. 2002, Hankeln et al. 2005). Cytoglobin may function in nitric oxide metabolism (Thuy et al. 2016, Liu et al. 2017). Globins can also regulate oxygen homeostasis via reactions with nitric oxide (NO), a vasodilator. Oxygenated globins scavenge NO by oxidation while deoxygenated globins can act as a nitrite reductase to produce NO (reviewed in Hendgen-Cotta et al. 2014, Tejero and Gladwin 2014). View original pathway at:Reactome.

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Pathway is converted from Reactome ID: 8981607
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Reactome version: 66
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Reactome Author: May, Bruce

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Bibliography

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  1. Pesce A, Bolognesi M, Bocedi A, Ascenzi P, Dewilde S, Moens L, Hankeln T, Burmester T.; ''Neuroglobin and cytoglobin. Fresh blood for the vertebrate globin family.''; PubMed Europe PMC Scholia
  2. Boulton FE, Huntsman RG.; ''Variants of human myoglobin: their oxygen dissociation curves.''; PubMed Europe PMC Scholia
  3. Hendgen-Cotta UB, Kelm M, Rassaf T.; ''Myoglobin functions in the heart.''; PubMed Europe PMC Scholia
  4. Trent JT, Watts RA, Hargrove MS.; ''Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen.''; PubMed Europe PMC Scholia
  5. Bocahut A, Bernad S, Sebban P, Sacquin-Mora S.; ''Relating the diffusion of small ligands in human neuroglobin to its structural and mechanical properties.''; PubMed Europe PMC Scholia
  6. Ascenzi P, di Masi A, Leboffe L, Fiocchetti M, Nuzzo MT, Brunori M, Marino M.; ''Neuroglobin: From structure to function in health and disease.''; PubMed Europe PMC Scholia
  7. Liu X, El-Mahdy MA, Boslett J, Varadharaj S, Hemann C, Abdelghany TM, Ismail RS, Little SC, Zhou D, Thuy LT, Kawada N, Zweier JL.; ''Cytoglobin regulates blood pressure and vascular tone through nitric oxide metabolism in the vascular wall.''; PubMed Europe PMC Scholia
  8. Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, Weber RE.; ''Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance.''; PubMed Europe PMC Scholia
  9. Wang Y, Baskin JS, Xia T, Zewail AH.; ''Human myoglobin recognition of oxygen: dynamics of the energy landscape.''; PubMed Europe PMC Scholia
  10. Hundahl CA, Kelsen J, Hay-Schmidt A.; ''Neuroglobin and cytoglobin expression in the human brain.''; PubMed Europe PMC Scholia
  11. Orlowski S, Nowak W.; ''Topology and thermodynamics of gaseous ligands diffusion paths in human neuroglobin.''; PubMed Europe PMC Scholia
  12. Burmester T, Ebner B, Weich B, Hankeln T.; ''Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues.''; PubMed Europe PMC Scholia
  13. Trent JT, Hargrove MS.; ''A ubiquitously expressed human hexacoordinate hemoglobin.''; PubMed Europe PMC Scholia
  14. Hamdane D, Kiger L, Dewilde S, Green BN, Pesce A, Uzan J, Burmester T, Hankeln T, Bolognesi M, Moens L, Marden MC.; ''The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.''; PubMed Europe PMC Scholia
  15. Hoogewijs D, Ebner B, Germani F, Hoffmann FG, Fabrizius A, Moens L, Burmester T, Dewilde S, Storz JF, Vinogradov SN, Hankeln T.; ''Androglobin: a chimeric globin in metazoans that is preferentially expressed in Mammalian testes.''; PubMed Europe PMC Scholia
  16. Helbo S, Weber RE, Fago A.; ''Expression patterns and adaptive functional diversity of vertebrate myoglobins.''; PubMed Europe PMC Scholia
  17. ROSSI-FANELLI A, ANTONINI E.; ''Studies on the oxygen and carbon monoxide equilibria of human myoglobin.''; PubMed Europe PMC Scholia
  18. Tomita A, Kreutzer U, Adachi S, Koshihara SY, Jue T.; '''It's hollow': the function of pores within myoglobin.''; PubMed Europe PMC Scholia
  19. Hankeln T, Wystub S, Laufs T, Schmidt M, Gerlach F, Saaler-Reinhardt S, Reuss S, Burmester T.; ''The cellular and subcellular localization of neuroglobin and cytoglobin -- a clue to their function?''; PubMed Europe PMC Scholia
  20. Burmester T, Hankeln T.; ''Function and evolution of vertebrate globins.''; PubMed Europe PMC Scholia
  21. Yamada T, Furuichi Y, Takakura H, Hashimoto T, Hanai Y, Jue T, Masuda K.; ''Interaction between myoglobin and mitochondria in rat skeletal muscle.''; PubMed Europe PMC Scholia
  22. Thuy le TT, Van Thuy TT, Matsumoto Y, Hai H, Ikura Y, Yoshizato K, Kawada N.; ''Absence of cytoglobin promotes multiple organ abnormalities in aged mice.''; PubMed Europe PMC Scholia
  23. Kakar S, Hoffman FG, Storz JF, Fabian M, Hargrove MS.; ''Structure and reactivity of hexacoordinate hemoglobins.''; PubMed Europe PMC Scholia
  24. Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M.; ''Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.''; PubMed Europe PMC Scholia
  25. Tejero J, Gladwin MT.; ''The globin superfamily: functions in nitric oxide formation and decay.''; PubMed Europe PMC Scholia
  26. Dewilde S, Kiger L, Burmester T, Hankeln T, Baudin-Creuza V, Aerts T, Marden MC, Caubergs R, Moens L.; ''Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.''; PubMed Europe PMC Scholia
  27. Hankeln T, Ebner B, Fuchs C, Gerlach F, Haberkamp M, Laufs TL, Roesner A, Schmidt M, Weich B, Wystub S, Saaler-Reinhardt S, Reuss S, Bolognesi M, De Sanctis D, Marden MC, Kiger L, Moens L, Dewilde S, Nevo E, Avivi A, Weber RE, Fago A, Burmester T.; ''Neuroglobin and cytoglobin in search of their role in the vertebrate globin family.''; PubMed Europe PMC Scholia
  28. Watanabe S, Takahashi N, Uchida H, Wakasugi K.; ''Human neuroglobin functions as an oxidative stress-responsive sensor for neuroprotection.''; PubMed Europe PMC Scholia
  29. Bocahut A, Derrien V, Bernad S, Sebban P, Sacquin-Mora S, Guittet E, Lescop E.; ''Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.''; PubMed Europe PMC Scholia
  30. Burmester T, Weich B, Reinhardt S, Hankeln T.; ''A vertebrate globin expressed in the brain.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114864view16:37, 25 January 2021ReactomeTeamReactome version 75
113310view11:38, 2 November 2020ReactomeTeamReactome version 74
112521view15:48, 9 October 2020ReactomeTeamReactome version 73
101433view11:30, 1 November 2018ReactomeTeamreactome version 66
100971view21:08, 31 October 2018ReactomeTeamreactome version 65
100508view19:42, 31 October 2018ReactomeTeamreactome version 64
100054view16:25, 31 October 2018ReactomeTeamreactome version 63
99606view14:59, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93368view11:21, 9 August 2017ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
CYGB ProteinQ8WWM9 (Uniprot-TrEMBL)
CYGB dimer:O2ComplexR-HSA-5340212 (Reactome)
CYGB dimerComplexR-HSA-5340240 (Reactome)
MB ProteinP02144 (Uniprot-TrEMBL)
MB:ferroheme b:O2ComplexR-HSA-8981605 (Reactome)
MB:ferroheme bComplexR-HSA-8981612 (Reactome)
NGB ProteinQ9NPG2 (Uniprot-TrEMBL)
NGB:ferroheme b:O2ComplexR-HSA-8981609 (Reactome)
NGB:ferroheme bComplexR-HSA-8981620 (Reactome)
O2 MetaboliteCHEBI:15379 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
heme MetaboliteCHEBI:17627 (ChEBI)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
CYGB dimer:O2ArrowR-HSA-5340214 (Reactome)
CYGB dimer:O2R-HSA-8982617 (Reactome)
CYGB dimerArrowR-HSA-8982617 (Reactome)
CYGB dimerR-HSA-5340214 (Reactome)
MB:ferroheme b:O2ArrowR-HSA-8981606 (Reactome)
MB:ferroheme b:O2R-HSA-8981622 (Reactome)
MB:ferroheme bArrowR-HSA-8981622 (Reactome)
MB:ferroheme bR-HSA-8981606 (Reactome)
NGB:ferroheme b:O2ArrowR-HSA-8981610 (Reactome)
NGB:ferroheme b:O2R-HSA-8981621 (Reactome)
NGB:ferroheme bArrowR-HSA-8981621 (Reactome)
NGB:ferroheme bR-HSA-8981610 (Reactome)
O2ArrowR-HSA-8981621 (Reactome)
O2ArrowR-HSA-8981622 (Reactome)
O2ArrowR-HSA-8982617 (Reactome)
O2R-HSA-5340214 (Reactome)
O2R-HSA-8981606 (Reactome)
O2R-HSA-8981610 (Reactome)
R-HSA-5340214 (Reactome) Vertebrates possess multiple respiratory globins that differ in structure, function, and tissue distribution. Three different globins have been described so far: hemoglobin facilitates oxygen transport in blood, myoglobin mediates oxygen transport and storage in the muscle and neuroglobin has a yet unidentified function in nerve cells. A fourth globin has been identified in mouse, human and zebrafish. It is ubiquitously expressed in human tissue and therefore called cytoglobin (CYGB) (Burmester et al. 2002, Trent & Hargrove 2002). Unlike the specific expression patterns of Hb and Mb, CYGB is found in vascular smooth muscle, fibroblasts and cardiomyocytes. CYGB functions as a homodimer (Hamdane et al. 2003) and is localised to the cytosol of these cells where its O2 loading and unloading ability within a narrow O2 tension range makes it an ideal protein for O2 storage, especially during hypoxia (Fago et al. 2004).
R-HSA-8981606 (Reactome) Myoglobin binds molecular oxygen (O2) in the cells of muscle tissue (Rossi-Fanelli and Antonini 1958, Boulton and Huntsman 1972, Wang et al. 2004). The dissociation constant of Myoglobin-oxygen is about 1 micromole per liter. The myoglobin:oxygen complex stores oxygen and also transports oxygen from the sarcolemma to the mitochondria. Myoglobin binds other small molecules such as nitric oxide and carbon monoxide. The ligands of myoglobin appear to migrate from the surface of the protein through pores (pockets) in the protein structure to reach the embedded heme group (reviewed in Tomita et al. 2010).
R-HSA-8981610 (Reactome) Neuroglobin binds molecular oxygen (O2) in neurons of the central nervous system and peripheral nervous system (Burmester et al. 2000, Dewilde et al. 2001, Trent et al. 2001, Orlowski and Nowak 2008, Bocahut et al. 2009, Watanabe et al. 2012, Hundahl et al. 2013). An elongated cavity in the protein may facilitate the diffusion of oxygen to the heme (Pesce et al. 2003).
R-HSA-8981621 (Reactome) When the concentration of oxygen is low, neuroglobin:oxygen dissociates to yield free oxygen (Burmester et al. 2000, Dewilde et al. 2001, Trent et al. 2001).
R-HSA-8981622 (Reactome) When the concentration of oxygen is low myoglobin:oxygen dissociates to yield free oxygen (Rossi-Fanelli and Antonini 1958, Boulton and Huntsman 1972, Wang et al. 2004). The dissociation constant is about 1 micromole per liter. Myoglobin:oxygen may also transfer oxygen directly to cytochrome oxidase of mitochondria (inferred from rat homologs in Yamada et al. 2013).
R-HSA-8982617 (Reactome) At low oxygen concentrations cytoglobin:oxygen dissociates to yield free oxygen (O2) (Burmester et al. 2002, Trent and Hargrove 2002, Hamdane et al. 2003, Fago et al. 2004). The affinity of cytoglobin for oxygen is similar to the affinity of myoglobin for oxygen therefore cytoglobin is postulated to act similarly to myoglobin in transporting oxygen from regions of high concentration to regions of low concentration.
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