Citoglobina: Diferenzas entre revisións
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===Outras lecturas=== |
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*{{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 }} |
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*{{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 }} |
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*{{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= }} |
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*{{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= }} |
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*{{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 | pmc=139241 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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=10.1016/j.jmb.2003.12.063 }} |
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*{{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 }} |
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*{{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 }} |
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*{{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 | pmc=528928 }} |
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*{{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 }} |
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*{{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 }} |
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*{{cite journal | author=Shaw RJ, Liloglou T, Rogers SN, ''et al.'' |title=Promoter methylation of P16, RARβ, 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 | pmc=2361183 }} |
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*{{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 }} |
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*{{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 }} |
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}} |
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[[Categoría:Hemoproteínas]] |
[[Categoría:Hemoproteínas]] |
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Revisión como estaba o 29 de marzo de 2014 ás 13:03
 | Este artigo está a ser traducido ao galego por un usuario desta Wikipedia; por favor, non o edite. O usuario Miguelferig (conversa · contribucións) realizou a última edición na páxina hai 10 anos. Se o usuario non publica a tradución nun prazo de trinta días, procederase ó seu borrado rápido. |
A citoglobina (ou histoglobina) é unha globina respiratoria que consta no home de 190 aminoácidos, producida polo xene CYGB, situado no cromosoma 17. A diferenza doutras globinas específicas de tecido, como a hemoglobina producida polos glóbulos vermellos, a mioglobina do músculo, e a neuroglobina do sistema nervioso, esta proteína é ubicua e exprésase en todos os tecidos do organismo.[1].
O xene da citoglobina
Os estudos filoxenéticos feitos cos xenes das globinas mostran que a citoglobina e a mioglobina pertencen a un mesmo clado distinto do da hemoglobina e a neuroglobina. A globina ancestral da que proceden remóntase a máis de 450 millóns de anos.
A citoglobina de mamíferos ten unha lonxitude maior (190 aminoácidos) que a das outras globinas (140-150 aminoácidos). Isto débese a que ten unha estensión duns 20 aminoácidos en cada extremo. A citoglobina prégase en oito hélices α (ver pregamento de globina). Os residuos implicados nas globinas na fixación do oxíxeno están conservados tamén na citoglobina. Ademais dous dous intrónss (B12.2 e G7.0) contidos nos xenes das outras globinas, o xene da citoglobina (CYGB) ten un terceiro intrón, o HC11.2, preto do extremo 3’ da rexión codificante. O último exón do extremo 3’ está ausente nos peixes, xa que foi adquirido máis tarde no decurso da evolución dos tetrápodos.[1].
Expresión e función da citoglobina
A citoglobina atópase no citoplasma da maior parte dos tipos celulares, pero a súa taxa de produción revelada pola técnica de Northern blot difire dun tecido a outro. Esta distribución da expresión non concorda con que a súa función sexa exclusivamente respiratoria. De feito, segundo outros estudos, a citoglobina sintetízase preerentemente nas células do tecido conxuntivo (fibroblastos) e células de sostén (condrocitos e osteoblastos), o que apoia a hipótese de que está implicada na síntese do coláxeno. É posible que a citoglobina forneza oxíxeno á prolil-4-hidroxilase (EC 1.14.11.2), un ferroencima clave que cataliza a hidroxilación dos residuos de prolina da molécula de procoláxeno.[2]
En condicións de hipoxia, duplícase a síntese de citoglobina, e aínda máis no corazón e fígado.[3] Este mecanismo pode explicarse polo feito de que a citoglobina seve para almacenar e facilitar o transporte de oxíxeno cara á cadea respiratoria mitocondrial.[4] A presenza de citoglobina nas neuronas formula varias cuestións sobre as súas funcións no sistema nervioso central, xa que este tecido posúe xa unha globina específica, a neuroglobina. Considérase o seu papel potencial como doante de O2 para certas reaccións encimáticas, entre outras a síntese do NO a partir de arxinina polas NO sintases[5].
Notas
- ↑ 1,0 1,1 Thorsten Burmester, Bettina Ebner, Bettina Weich and Thomas Hankeln, (2002). Cytoglobin: A Novel Globin Type Ubiquitously Expressed in Vertebrate Tissues. Mol Biol and Evol 19; 416-421.[1]
- ↑ Kivirikko K. I., and Myllyharju J., (1998). Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 16; 357-368.
- ↑ Marc Schmidt, Frank Gerlach, Aaron Avivi, Thorsten Burmester et al., (2004). Cytoglobin Is a Respiratory Protein in Connective Tissue and Neurons, Which Is Up-regulated by Hypoxia. J. Biol. Chem. 279(9); 8063-8069.
- ↑ Sawai H., Kawada N., Yoshizato K., Nakajima H., Aono S., Shiro Y., (2003). Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. Biochemistry 42(17); 5133-42.
- ↑ Leone A. M., Palmer R. M., Knowles R. G., Francis P. L., Ashton D. S., and Moncada S., (1991). Constitutive and inducible nitric oxide synthases incorporate molecular oxygen into both nitric oxide and citrulline. J. Biol. Chem. 266; 23790-23795.
Véxase tamén
Outros artigos
Ligazóns externas
- Cursos e artigos
- O modelo {{PDF}} debe ter un argumento. PDF Transport de l'oxygène dans le sang: Cours.
- O modelo {{PDF}} debe ter un argumento. PDF Cytoglobin: A Novel Globin Type Ubiquitously Expressed in Vertebrate Tissues: Découverte de la cytoglobine.
- O modelo {{PDF}} debe ter un argumento. PDF Cytoglobin Is a Respiratory Protein in Connective Tissue and Neurons, Which Is Up-regulated by Hypoxia: Article fondamental.
- Bancos de datos biolóxicos
- Crystal structure of human cytoglobin at 1.68 angstroms resolution : Structure 3D et modèle interactif (java) de la cytoglobine par la Protein Data Bank (RCSB PDB). Attention: Si ce lien ne fonctionne pas, effectuez vous même une recherche sur ce site avec le mot clé cytoglobin.
- Q8WWM9 Human cytoglobin gene (Swiss-Prot) : Séquence complète et autres informations sur le gène humain de la cytoglobine (CYGB) par la Swiss-Prot.
- Pubmed: Pour consulter l'actualité biologique et médicale sur ce sujet NLM.
Outras lecturas
- 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. PMID 11320098. doi:10.1074/jbc.M102630200.
- Trent JT, Hargrove MS (2002). "A ubiquitously expressed human hexacoordinate hemoglobin.". J. Biol. Chem. 277 (22): 19538–45. PMID 11893755. doi:10.1074/jbc.M201934200.
- 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. PMC 139241. PMID 12477932. doi:10.1073/pnas.242603899.
- 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. PMID 12718557. doi:10.1021/bi027067e.
- Geuens E, Brouns I, Flamez D; et al. (2003). "A globin in the nucleus!". J. Biol. Chem. 278 (33): 30417–20. PMID 12796507. doi:10.1074/jbc.C300203200.
- 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. PMID 14530264. doi:10.1074/jbc.M309396200.
- 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. PMID 14660570. doi:10.1074/jbc.M310540200.
- 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. PMID 14702039. doi:10.1038/ng1285.
- 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. PMID 15052627. doi:10.1002/mus.20009.
- 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. doi:10.1016/j.jmb.2003.12.063.
- Sugimoto H, Makino M, Sawai H; et al. (2004). "Structural basis of human cytoglobin for ligand binding". J. Mol. Biol. 339 (4): 873–85. PMID 15165856. doi:10.1016/j.jmb.2004.04.024.
- 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. PMID 15299006. doi:10.1074/jbc.M407126200.
- 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. PMC 528928. PMID 15489334. doi:10.1101/gr.2596504.
- Hamdane D, Kiger L, Dewilde S; et al. (2005). "Hyperthermal stability of neuroglobin and cytoglobin". FEBS J. 272 (8): 2076–84. PMID 15819897. doi:10.1111/j.1742-4658.2005.04635.x.
- 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. PMID 16201751. doi:10.1021/bi050997o.
- Shaw RJ, Liloglou T, Rogers SN; et al. (2006). "Promoter methylation of P16, RARβ, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing". Br. J. Cancer 94 (4): 561–8. PMC 2361183. PMID 16449996. doi:10.1038/sj.bjc.6602972.
- 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. PMID 16510494. doi:10.1093/hmg/ddl042.
- 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. PMID 16698880. doi:10.1093/hmg/ddl128.
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