CYGB dioxygenates NO

Stable Identifier
R-HSA-5340226
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
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CYGB dioxygenates NO
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Vertebrates possess multiple respiratory globins that differ in structure, function, and tissue distribution. Three different globins have been described so far: haemoglobin 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) (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. As well as oxygen binding capability, CYGB possesses nitric oxide dioxygenase activity (Halligan et al. 2009), a common feature amongst the globin family (Smagghe et al. 2008). CYGB consumes NO through the dioxygenase pathway, which regulates cell respiration and proliferation (Smagghe et al. 2008). O2 binds to the ferric form of CYGB (CYGB-Fe2+:O2). During NO dioxygenation, CYGB is reduced to the ferrous form (CYGB-Fe3+) (Gardner 2005).

Literature References
PubMed ID Title Journal Year
14530264 The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin

Hamdane, D, Kiger, L, Dewilde, S, Green, BN, Pesce, A, Uzan, J, Burmester, T, Hankeln, T, Bolognesi, M, Moens, L, Marden, MC

J. Biol. Chem. 2003
19147491 Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation

Halligan, KE, Jourd'heuil, FL, Jourd'heuil, D

J. Biol. Chem. 2009
11893755 A ubiquitously expressed human hexacoordinate hemoglobin

Trent, JT, Hargrove, MS

J. Biol. Chem. 2002
18446211 NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo

Smagghe, BJ, Trent JT, 3rd, Hargrove, MS

PLoS One 2008
15598505 Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases

Gardner, PR

J. Inorg. Biochem. 2005
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Catalyst Activity
Catalyst Activity
Title
nitric oxide dioxygenase activity of CYGB dimer:O2 [cytosol]
Physical Entity
CYGB dimer:O2 [cytosol]
Activity
nitric oxide dioxygenase activity (0008941)
Orthologous Events
CYGB dioxygenates NO (Bos taurus)
CYGB dioxygenates NO (Caenorhabditis elegans)
CYGB dioxygenates NO (Canis familiaris)
CYGB dioxygenates NO (Danio rerio)
CYGB dioxygenates NO (Gallus gallus)
CYGB dioxygenates NO (Mus musculus)
CYGB dioxygenates NO (Rattus norvegicus)
CYGB dioxygenates NO (Sus scrofa)
CYGB dioxygenates NO (Xenopus tropicalis)
Authored
Jassal, B  (2014-03-12)
Reviewed
D'Eustachio, P  (2015-02-11)
Created
Jassal, B  (2014-03-12)