Cytoglobin

CYGB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases CYGB, HGB, STAP, cytoglobin
External IDs MGI: 2149481 HomoloGene: 12706 GeneCards: CYGB
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

114757

114886

Ensembl

ENSG00000161544

ENSMUSG00000020810

UniProt

Q8WWM9

Q9CX80

RefSeq (mRNA)

NM_134268

NM_030206

RefSeq (protein)

NP_599030.1

NP_084482.1

Location (UCSC) Chr 17: 76.53 – 76.55 Mb Chr 11: 116.65 – 116.65 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Cytoglobin is the protein product of CYGB, a human and mammalian gene.[3]

Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001[4] and named cytoglobin in 2002.[5] It is thought to protect against hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.[6]

Function

Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or reactive oxygen species, or serve a protective function during oxidative stress.[3][7]

Applications

CYGB expression can be used as a specific marker with which hepatic stellate cells can be distinguished from portal myofibroblasts in the damaged human liver.[8]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. 1 2 "Entrez Gene: CYGB cytoglobin".
  4. ↑ Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K (Jul 2001). "Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells". The Journal of Biological Chemistry. 276 (27): 25318–23. doi:10.1074/jbc.M102630200. PMID 11320098.
  5. ↑ Burmester T, Ebner B, Weich B, Hankeln T (Apr 2002). "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues". Molecular Biology and Evolution. 19 (4): 416–21. doi:10.1093/oxfordjournals.molbev.a004096. PMID 11919282.
  6. ↑ "Why Diving Marine Mammals Resist Brain Damage from Low Oxygen". ScienceDaily. 20 December 2007.
  7. ↑ Trent JT, Hargrove MS (May 2002). "A ubiquitously expressed human hexacoordinate hemoglobin". The Journal of Biological Chemistry. 277 (22): 19538–45. doi:10.1074/jbc.M201934200. PMID 11893755.
  8. ↑ Motoyama H, Komiya T, Thuy le TT, Tamori A, Enomoto M, Morikawa H, Iwai S, Uchida-Kobayashi S, Fujii H, Hagihara A, Kawamura E, Murakami Y, Yoshizato K, Kawada N (Feb 2014). "Cytoglobin is expressed in hepatic stellate cells, but not in myofibroblasts, in normal and fibrotic human liver". Laboratory Investigation. 94 (2): 192–207. doi:10.1038/labinvest.2013.135. PMID 24296877.

Further reading

  • Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K (Jul 2001). "Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells". The Journal of Biological Chemistry. 276 (27): 25318–23. doi:10.1074/jbc.M102630200. PMID 11320098. 
  • Burmester T, Ebner B, Weich B, Hankeln T (Apr 2002). "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues". Molecular Biology and Evolution. 19 (4): 416–21. doi:10.1093/oxfordjournals.molbev.a004096. PMID 11919282. 
  • Asahina K, Kawada N, Kristensen DB, Nakatani K, Seki S, Shiokawa M, Tateno C, Obara M, Yoshizato K (Sep 2002). "Characterization of human stellate cell activation-associated protein and its expression in human liver". Biochimica et Biophysica Acta. 1577 (3): 471–5. doi:10.1016/s0167-4781(02)00477-3. PMID 12359339. 
  • Sawai H, Kawada N, Yoshizato K, Nakajima H, Aono S, Shiro Y (May 2003). "Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans". Biochemistry. 42 (17): 5133–42. doi:10.1021/bi027067e. PMID 12718557. 
  • Geuens E, Brouns I, Flamez D, Dewilde S, Timmermans JP, Moens L (Aug 2003). "A globin in the nucleus!". The Journal of Biological Chemistry. 278 (33): 30417–20. doi:10.1074/jbc.C300203200. PMID 12796507. 
  • Hamdane D, Kiger L, Dewilde S, Green BN, Pesce A, Uzan J, Burmester T, Hankeln T, Bolognesi M, Moens L, Marden MC (Dec 2003). "The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin". The Journal of Biological Chemistry. 278 (51): 51713–21. doi:10.1074/jbc.M309396200. PMID 14530264. 
  • Schmidt M, Gerlach F, Avivi A, Laufs T, Wystub S, Simpson JC, Nevo E, Saaler-Reinhardt S, Reuss S, Hankeln T, Burmester T (Feb 2004). "Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia". The Journal of Biological Chemistry. 279 (9): 8063–9. doi:10.1074/jbc.M310540200. PMID 14660570. 
  • Hünermund G, Schirmacher A, Ringelstein B, Young P, Watts GD, Meuleman J, Nelis E, Chance PF, Timmerman V, Stögbauer F, Kuhlenbäumer G (Apr 2004). "Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy". Muscle & Nerve. 29 (4): 601–4. doi:10.1002/mus.20009. PMID 15052627. 
  • de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M (Feb 2004). "Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination". Journal of Molecular Biology. 336 (4): 917–27. doi:10.1016/j.jmb.2003.12.063. PMID 15095869. 
  • Sugimoto H, Makino M, Sawai H, Kawada N, Yoshizato K, Shiro Y (Jun 2004). "Structural basis of human cytoglobin for ligand binding". Journal of Molecular Biology. 339 (4): 873–85. doi:10.1016/j.jmb.2004.04.024. PMID 15165856. 
  • Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, Weber RE (Oct 2004). "Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance". The Journal of Biological Chemistry. 279 (43): 44417–26. doi:10.1074/jbc.M407126200. PMID 15299006. 
  • Hamdane D, Kiger L, Dewilde S, Uzan J, Burmester T, Hankeln T, Moens L, Marden MC (Apr 2005). "Hyperthermal stability of neuroglobin and cytoglobin". The FEBS Journal. 272 (8): 2076–84. doi:10.1111/j.1742-4658.2005.04635.x. PMID 15819897. 
  • Sawai H, Makino M, Mizutani Y, Ohta T, Sugimoto H, Uno T, Kawada N, Yoshizato K, Kitagawa T, Shiro Y (Oct 2005). "Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin". Biochemistry. 44 (40): 13257–65. doi:10.1021/bi050997o. PMID 16201751. 
  • Shaw RJ, Liloglou T, Rogers SN, Brown JS, Vaughan ED, Lowe D, Field JK, Risk JM (Feb 2006). "Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing". British Journal of Cancer. 94 (4): 561–8. doi:10.1038/sj.bjc.6602972. PMC 2361183Freely accessible. PMID 16449996. 
  • McRonald FE, Liloglou T, Xinarianos G, Hill L, Rowbottom L, Langan JE, Ellis A, Shaw JM, Field JK, Risk JM (Apr 2006). "Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression". Human Molecular Genetics. 15 (8): 1271–7. doi:10.1093/hmg/ddl042. PMID 16510494. 
  • Xinarianos G, McRonald FE, Risk JM, Bowers NL, Nikolaidis G, Field JK, Liloglou T (Jul 2006). "Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer". Human Molecular Genetics. 15 (13): 2038–44. doi:10.1093/hmg/ddl128. PMID 16698880. 

External links


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