Cytoglobin

From Wikipedia, the free encyclopedia

Cytoglobin

PDB rendering based on 1umo.

Available structures: 1umo, 1urv, 1ury, 1ut0, 1ux9, 1v5h, 2dc3

Identifiers

Symbol(s)

CYGB; HGB; STAP

External IDs

OMIM: 608759 MGI: 2149481 HomoloGene: 12706

Gene ontology
Molecular Function:	• peroxidase activity • oxygen transporter activity • iron ion binding • oxygen binding • heme binding • metal ion binding
Cellular Component:	• neuron projection • cell soma
Biological Process:	• transport • response to oxidative stress • oxygen transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_134268 (mRNA)
NP_599030 (protein)

XM_992680 (mRNA)
XP_997774 (protein)

Location

Chr 17: 72.04 - 72.05 Mb

Chr 11: 116.46 - 116.47 Mb

Pubmed search

[1]

[2]

Cytoglobin is the protein product of CYGB, a human and mammalian gene.^[1]

Cytoglobin is a globin molecule located in the brain and most notably utilised in marine mammals. It is thought to be a method of protection under conditions of hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.^[2]

Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or other reactive oxygen species, or serve a protective function during oxidative stress (Trent and Hargrove, 2002).[supplied by OMIM]^[1]

[edit] References

[edit] Further reading

Kawada N, Kristensen DB, Asahina K, et al. (2001). "Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells.". J. Biol. Chem. 276 (27): 25318–23. doi:10.1074/jbc.M102630200. PMID 11320098.
Trent JT, Hargrove MS (2002). "A ubiquitously expressed human hexacoordinate hemoglobin.". J. Biol. Chem. 277 (22): 19538–45. doi:10.1074/jbc.M201934200. PMID 11893755.
Burmester T, Ebner B, Weich B, Hankeln T (2002). "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues.". Mol. Biol. Evol. 19 (4): 416–21. PMID 11919282.
Asahina K, Kawada N, Kristensen DB, et al. (2002). "Characterization of human stellate cell activation-associated protein and its expression in human liver.". Biochim. Biophys. Acta 1577 (3): 471–5. PMID 12359339.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Sawai H, Kawada N, Yoshizato K, et al. (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, et al. (2003). "A globin in the nucleus!". J. Biol. Chem. 278 (33): 30417–20. doi:10.1074/jbc.C300203200. PMID 12796507.
Hamdane D, Kiger L, Dewilde S, et al. (2004). "The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.". J. Biol. Chem. 278 (51): 51713–21. doi:10.1074/jbc.M309396200. PMID 14530264.
Schmidt M, Gerlach F, Avivi A, et al. (2004). "Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia.". J. Biol. Chem. 279 (9): 8063–9. doi:10.1074/jbc.M310540200. PMID 14660570.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Hünermund G, Schirmacher A, Ringelstein B, et al. (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, et al. (2004). "Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination.". J. Mol. Biol. 336 (4): 917–27. PMID 15095869.
Sugimoto H, Makino M, Sawai H, et al. (2004). "Structural basis of human cytoglobin for ligand binding.". J. Mol. Biol. 339 (4): 873–85. doi:10.1016/j.jmb.2004.04.024. PMID 15165856.
Fago A, Hundahl C, Dewilde S, et al. (2004). "Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance.". J. Biol. Chem. 279 (43): 44417–26. doi:10.1074/jbc.M407126200. PMID 15299006.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Hamdane D, Kiger L, Dewilde S, et al. (2005). "Hyperthermal stability of neuroglobin and cytoglobin.". FEBS J. 272 (8): 2076–84. doi:10.1111/j.1742-4658.2005.04635.x. PMID 15819897.
Sawai H, Makino M, Mizutani Y, et al. (2006). "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, et al. (2006). "Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing.". Br. J. Cancer 94 (4): 561–8. doi:10.1038/sj.bjc.6602972. PMID 16449996.
McRonald FE, Liloglou T, Xinarianos G, et al. (2006). "Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression.". Hum. Mol. Genet. 15 (8): 1271–7. doi:10.1093/hmg/ddl042. PMID 16510494.
Xinarianos G, McRonald FE, Risk JM, et al. (2006). "Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer.". Hum. Mol. Genet. 15 (13): 2038–44. doi:10.1093/hmg/ddl128. PMID 16698880.