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{{Infobox_gene}}
'''Cytoglobin''' is the protein product of '''CYGB''', a [[human]] and [[mammalian]] [[gene]].<ref name="entrez"/>


Cytoglobin is a [[globin]] molecule ubiquitously expressed in all tissues and most notably utilized in [[marine mammals]]. It was discovered in 2001<ref>{{cite journal | vauthors = Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K | title = Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 27 | pages = 25318–23 | date = Jul 2001 | pmid = 11320098 | doi = 10.1074/jbc.M102630200 }}</ref> and named cytoglobin in 2002.<ref>{{cite journal | vauthors = Burmester T, Ebner B, Weich B, Hankeln T | title = Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues | journal = Molecular Biology and Evolution | volume = 19 | issue = 4 | pages = 416–21 | date = Apr 2002 | pmid = 11919282 | doi = 10.1093/oxfordjournals.molbev.a004096 }}</ref> It is thought to protect against [[Hypoxia (medical)|hypoxia]]. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.<ref name="sciencedaily">{{cite web | title = Why Diving Marine Mammals Resist Brain Damage from Low Oxygen| url= https://www.sciencedaily.com/releases/2007/12/071218192033.htm | work = ScienceDaily | date = 20 December 2007 }}</ref>


{{PBB_Controls
== Function ==
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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]].<ref name="entrez">{{cite web | title = Entrez Gene: CYGB cytoglobin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114757 }}</ref><ref name="Trent_2002">{{cite journal | vauthors = Trent JT, Hargrove MS | title = A ubiquitously expressed human hexacoordinate hemoglobin | journal = The Journal of Biological Chemistry | volume = 277 | issue = 22 | pages = 19538–45 | date = May 2002 | pmid = 11893755 | doi = 10.1074/jbc.M201934200 }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_CYGB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1umo.
| PDB = {{PDB2|1umo}}, {{PDB2|1urv}}, {{PDB2|1ury}}, {{PDB2|1ut0}}, {{PDB2|1ux9}}, {{PDB2|1v5h}}, {{PDB2|2dc3}}
| Name = Cytoglobin
| HGNCid = 16505
| Symbol = CYGB
| AltSymbols =; HGB; STAP
| OMIM = 608759
| ECnumber = 
| Homologene = 12706
| MGIid = 2149481
| GeneAtlas_image1 = PBB_GE_CYGB_gnf1h08384_at_tn.png
| Function = {{GNF_GO|id=GO:0004601 |text = peroxidase activity}} {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0043005 |text = neuron projection}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 114757
    | Hs_Ensembl = ENSG00000161544
    | Hs_RefseqProtein = NP_599030
    | Hs_RefseqmRNA = NM_134268
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 72035056
    | Hs_GenLoc_end = 72045561
    | Hs_Uniprot = Q8WWM9
    | Mm_EntrezGene = 114886
    | Mm_Ensembl = ENSMUSG00000020810
    | Mm_RefseqmRNA = XM_992680
    | Mm_RefseqProtein = XP_997774
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 116461685
    | Mm_GenLoc_end = 116470403
    | Mm_Uniprot = Q546K1
  }}
}}
'''Cytoglobin''', also known as '''CYGB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYGB cytoglobin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114757| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Applications ==
{{PBB_Summary
| section_title =  
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: CYGB cytoglobin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114757| accessdate = }}</ref>
}}


==References==
CYGB expression can be used as a specific marker with which [[hepatic stellate cell]]s can be distinguished from portal [[myofibroblast]]s in the damaged human liver.<ref name="pmid24296877">{{cite journal | vauthors = 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 | title = Cytoglobin is expressed in hepatic stellate cells, but not in myofibroblasts, in normal and fibrotic human liver | journal = Laboratory Investigation | volume = 94 | issue = 2 | pages = 192–207 | date = Feb 2014 | pmid = 24296877 | doi = 10.1038/labinvest.2013.135 }}</ref>
{{reflist|2}}
 
==Further reading==
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K | title = Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 27 | pages = 25318–23 | date = Jul 2001 | pmid = 11320098 | doi = 10.1074/jbc.M102630200 }}
| citations =
* {{cite journal | vauthors = Burmester T, Ebner B, Weich B, Hankeln T | title = Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues | journal = Molecular Biology and Evolution | volume = 19 | issue = 4 | pages = 416–21 | date = Apr 2002 | pmid = 11919282 | doi = 10.1093/oxfordjournals.molbev.a004096 }}
*{{cite journal | author=Kawada N, Kristensen DB, Asahina K, ''et al.'' |title=Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25318-23 |year= 2001 |pmid= 11320098 |doi= 10.1074/jbc.M102630200 }}
* {{cite journal | vauthors = Asahina K, Kawada N, Kristensen DB, Nakatani K, Seki S, Shiokawa M, Tateno C, Obara M, Yoshizato K | title = Characterization of human stellate cell activation-associated protein and its expression in human liver | journal = Biochimica et Biophysica Acta | volume = 1577 | issue = 3 | pages = 471–5 | date = Sep 2002 | pmid = 12359339 | doi = 10.1016/s0167-4781(02)00477-3 }}
*{{cite journal | author=Trent JT, Hargrove MS |title=A ubiquitously expressed human hexacoordinate hemoglobin. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19538-45 |year= 2002 |pmid= 11893755 |doi= 10.1074/jbc.M201934200 }}
* {{cite journal | vauthors = Sawai H, Kawada N, Yoshizato K, Nakajima H, Aono S, Shiro Y | title = Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans | journal = Biochemistry | volume = 42 | issue = 17 | pages = 5133–42 | date = May 2003 | pmid = 12718557 | doi = 10.1021/bi027067e }}
*{{cite journal  | author=Burmester T, Ebner B, Weich B, Hankeln T |title=Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. |journal=Mol. Biol. Evol. |volume=19 |issue= 4 |pages= 416-21 |year= 2002 |pmid= 11919282 |doi= }}
* {{cite journal | vauthors = Geuens E, Brouns I, Flamez D, Dewilde S, Timmermans JP, Moens L | title = A globin in the nucleus! | journal = The Journal of Biological Chemistry | volume = 278 | issue = 33 | pages = 30417–20 | date = Aug 2003 | pmid = 12796507 | doi = 10.1074/jbc.C300203200 }}
*{{cite journal | author=Asahina K, Kawada N, Kristensen DB, ''et al.'' |title=Characterization of human stellate cell activation-associated protein and its expression in human liver. |journal=Biochim. Biophys. Acta |volume=1577 |issue= 3 |pages= 471-5 |year= 2002 |pmid= 12359339 |doi= }}
* {{cite journal | vauthors = Hamdane D, Kiger L, Dewilde S, Green BN, Pesce A, Uzan J, Burmester T, Hankeln T, Bolognesi M, Moens L, Marden MC | title = The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 51 | pages = 51713–21 | date = Dec 2003 | pmid = 14530264 | doi = 10.1074/jbc.M309396200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Schmidt M, Gerlach F, Avivi A, Laufs T, Wystub S, Simpson JC, Nevo E, Saaler-Reinhardt S, Reuss S, Hankeln T, Burmester T | title = Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia | journal = The Journal of Biological Chemistry | volume = 279 | issue = 9 | pages = 8063–9 | date = Feb 2004 | pmid = 14660570 | doi = 10.1074/jbc.M310540200 }}
*{{cite journal | author=Sawai H, Kawada N, Yoshizato K, ''et al.'' |title=Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. |journal=Biochemistry |volume=42 |issue= 17 |pages= 5133-42 |year= 2003 |pmid= 12718557 |doi= 10.1021/bi027067e }}
* {{cite journal | vauthors = Hünermund G, Schirmacher A, Ringelstein B, Young P, Watts GD, Meuleman J, Nelis E, Chance PF, Timmerman V, Stögbauer F, Kuhlenbäumer G | title = Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy | journal = Muscle & Nerve | volume = 29 | issue = 4 | pages = 601–4 | date = Apr 2004 | pmid = 15052627 | doi = 10.1002/mus.20009 }}
*{{cite journal | author=Geuens E, Brouns I, Flamez D, ''et al.'' |title=A globin in the nucleus! |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30417-20 |year= 2003 |pmid= 12796507 |doi= 10.1074/jbc.C300203200 }}
* {{cite journal | vauthors = de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M | title = Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination | journal = Journal of Molecular Biology | volume = 336 | issue = 4 | pages = 917–27 | date = Feb 2004 | pmid = 15095869 | doi = 10.1016/j.jmb.2003.12.063 }}
*{{cite journal | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51713-21 |year= 2004 |pmid= 14530264 |doi= 10.1074/jbc.M309396200 }}
* {{cite journal | vauthors = Sugimoto H, Makino M, Sawai H, Kawada N, Yoshizato K, Shiro Y | title = Structural basis of human cytoglobin for ligand binding | journal = Journal of Molecular Biology | volume = 339 | issue = 4 | pages = 873–85 | date = Jun 2004 | pmid = 15165856 | doi = 10.1016/j.jmb.2004.04.024 }}
*{{cite journal | author=Schmidt M, Gerlach F, Avivi A, ''et al.'' |title=Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 8063-9 |year= 2004 |pmid= 14660570 |doi= 10.1074/jbc.M310540200 }}
* {{cite journal | vauthors = Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, Weber RE | title = Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance | journal = The Journal of Biological Chemistry | volume = 279 | issue = 43 | pages = 44417–26 | date = Oct 2004 | pmid = 15299006 | doi = 10.1074/jbc.M407126200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Hamdane D, Kiger L, Dewilde S, Uzan J, Burmester T, Hankeln T, Moens L, Marden MC | title = Hyperthermal stability of neuroglobin and cytoglobin | journal = The FEBS Journal | volume = 272 | issue = 8 | pages = 2076–84 | date = Apr 2005 | pmid = 15819897 | doi = 10.1111/j.1742-4658.2005.04635.x }}
*{{cite journal  | author=Hünermund G, Schirmacher A, Ringelstein B, ''et al.'' |title=Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy. |journal=Muscle Nerve |volume=29 |issue= 4 |pages= 601-4 |year= 2004 |pmid= 15052627 |doi= 10.1002/mus.20009 }}
* {{cite journal | vauthors = Sawai H, Makino M, Mizutani Y, Ohta T, Sugimoto H, Uno T, Kawada N, Yoshizato K, Kitagawa T, Shiro Y | title = Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin | journal = Biochemistry | volume = 44 | issue = 40 | pages = 13257–65 | date = Oct 2005 | pmid = 16201751 | doi = 10.1021/bi050997o }}
*{{cite journal | author=de Sanctis D, Dewilde S, Pesce A, ''et al.'' |title=Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination. |journal=J. Mol. Biol. |volume=336 |issue= 4 |pages= 917-27 |year= 2004 |pmid= 15095869 |doi= }}
* {{cite journal | vauthors = Shaw RJ, Liloglou T, Rogers SN, Brown JS, Vaughan ED, Lowe D, Field JK, Risk JM | title = Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing | journal = British Journal of Cancer | volume = 94 | issue = 4 | pages = 561–8 | date = Feb 2006 | pmid = 16449996 | pmc = 2361183 | doi = 10.1038/sj.bjc.6602972 }}
*{{cite journal | author=Sugimoto H, Makino M, Sawai H, ''et al.'' |title=Structural basis of human cytoglobin for ligand binding. |journal=J. Mol. Biol. |volume=339 |issue= 4 |pages= 873-85 |year= 2004 |pmid= 15165856 |doi= 10.1016/j.jmb.2004.04.024 }}
* {{cite journal | vauthors = McRonald FE, Liloglou T, Xinarianos G, Hill L, Rowbottom L, Langan JE, Ellis A, Shaw JM, Field JK, Risk JM | title = Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression | journal = Human Molecular Genetics | volume = 15 | issue = 8 | pages = 1271–7 | date = Apr 2006 | pmid = 16510494 | doi = 10.1093/hmg/ddl042 }}
*{{cite journal | author=Fago A, Hundahl C, Dewilde S, ''et al.'' |title=Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44417-26 |year= 2004 |pmid= 15299006 |doi= 10.1074/jbc.M407126200 }}
* {{cite journal | vauthors = Xinarianos G, McRonald FE, Risk JM, Bowers NL, Nikolaidis G, Field JK, Liloglou T | title = Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer | journal = Human Molecular Genetics | volume = 15 | issue = 13 | pages = 2038–44 | date = Jul 2006 | pmid = 16698880 | doi = 10.1093/hmg/ddl128 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=Hyperthermal stability of neuroglobin and cytoglobin. |journal=FEBS J. |volume=272 |issue= 8 |pages= 2076-84 |year= 2005 |pmid= 15819897 |doi= 10.1111/j.1742-4658.2005.04635.x }}
*{{cite journal | author=Sawai H, Makino M, Mizutani Y, ''et al.'' |title=Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin. |journal=Biochemistry |volume=44 |issue= 40 |pages= 13257-65 |year= 2006 |pmid= 16201751 |doi= 10.1021/bi050997o }}
*{{cite journal | author=Shaw RJ, Liloglou T, Rogers SN, ''et al.'' |title=Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing. |journal=Br. J. Cancer |volume=94 |issue= 4 |pages= 561-8 |year= 2006 |pmid= 16449996 |doi= 10.1038/sj.bjc.6602972 }}
*{{cite journal | author=McRonald FE, Liloglou T, Xinarianos G, ''et al.'' |title=Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression. |journal=Hum. Mol. Genet. |volume=15 |issue= 8 |pages= 1271-7 |year= 2006 |pmid= 16510494 |doi= 10.1093/hmg/ddl042 }}
*{{cite journal | author=Xinarianos G, McRonald FE, Risk JM, ''et al.'' |title=Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer. |journal=Hum. Mol. Genet. |volume=15 |issue= 13 |pages= 2038-44 |year= 2006 |pmid= 16698880 |doi= 10.1093/hmg/ddl128 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 21:23, 28 February 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001[2] and named cytoglobin in 2002.[3] It is thought to protect against hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.[4]

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.[1][5]

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.[6]

References

  1. 1.0 1.1 "Entrez Gene: CYGB cytoglobin".
  2. 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.
  3. 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.
  4. "Why Diving Marine Mammals Resist Brain Damage from Low Oxygen". ScienceDaily. 20 December 2007.
  5. 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.
  6. 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.
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