Factor de crecemento de fibroblastos básico: Diferenzas entre revisións

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O '''factor de crecemento de fibroblastos básico''' ('''bFGF'''), tamén chamado '''FGF2''' ou '''FGF-β''', é un [[factor de crecemento]] e [[proteína de sinalización]] codificada polo [[xene]] ''FGF2'' do [[cromosoma 4]] humano.<ref name="pmid1697263">{{citeCita journalpublicación periódica | vauthors = Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J | title = Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors | journal = The EMBO Journal | volume = 9 | issue = 9 | pages = 2685–92 | date = September 1990 | pmid = 1697263 | pmc = 551973 | doi = }}</ref><ref name="pmid9925931">{{citeCita journalpublicación periódica | vauthors = Kim HS | title = Assignment1 of the human basic fibroblast growth factor gene FGF2 to chromosome 4 band q26 by radiation hybrid mapping | journal = Cytogenetics and Cell Genetics | volume = 83 | issue = 1-2 | pages = 73 | year = 1998 | pmid = 9925931 | doi = 10.1159/000015129 }}</ref> Sintetízase inicialmente como un polipéptido de 155 [[aminoácido]]s, que orixina unha proteína de 18 kDa. Porén, hai catro [[codón de inicio|codóns de inicio]] alternativos que orixinan extensións N-terminais de 41, 46, 55 ou 133 aminoácidos, orixinando proteínas, respectivamente, de 22 kDa (196 aminoácidos en total), 22,5 kDa (201 aminoácidos en total), 24 kDa (210 aminoácidos en total) e 34 kDa (288 aminoácidos en total).<ref name="pmid 1785797">{{citeCita journalpublicación periódica | vauthors = Florkiewicz RZ, Shibata F, Barankiewicz T, Baird A, Gonzalez AM, Florkiewicz E, Shah N | title = Basic fibroblast growth factor gene expression | journal = Annals of the New York Academy of Sciences | volume = 638 | issue = 1 | pages = 109–26 | date = December 1991 | pmid = 1785797 | doi = 10.1111/j.1749-6632.1991.tb49022.x }}</ref> Xeralmente, a forma de 155 aminoácidos/18 kDa de baixo peso molecular (LMW) considérase citoplásmica e pode ser segregada da célula, mentres que as formas de alto peso molecular (HMW) son dirixidas ao [[núcleo celular]].<ref name="pmid 24780002">{{citeCita journalpublicación periódica | vauthors = Coleman SJ, Bruce C, Chioni AM, Kocher HM, Grose RP | title = The ins and outs of fibroblast growth factor receptor signalling | journal = Clinical Science | volume = 127 | issue = 4 | pages = 217–31 | date = August 2014 | pmid = 24780002 | doi = 10.1042/CS20140100 | url = http://www.clinsci.org/content/127/4/217 }}</ref>
 
A proteína [[factor de crecemento de fibroblastos]] foi purificada primeiramente en 1975, pero pouco despois illáronse outras similares utilizando diferentes condicións, como o FGF básico, o factor de crecemento que se une á heparina 2 e o factor de crecemento de célula endotelial 2. A secuenciación xénica revelou que FGF2 era un membro da [[factor de crecemento de fibroblastos|familia de FGF]] de proteínas.<ref name="pmid 1785797">< /ref><ref>{{citeCita publicación journalperiódica | vauthors = Burgess WH, Maciag T | title = The heparin-binding (fibroblast) growth factor family of proteins | journal = Annual Review of Biochemistry | volume = 58 | pages = 575–606 | date = 1989 | pmid = 2549857 | doi = 10.1146/annurev.bi.58.070189.003043 }}</ref> O FGF2 únese e exerce efectos por medio de proteínas específicas [[receptor do factor de crecemento de fibroblastos]] (FGFR) que constitúen unha familia de moléculas estreitamente relacionadas.
 
== Función ==
 
Como outros membros da familia FGF, o factor de crecemento de fibroblastos básico posúe amplas actividades mitoxénicas e de supervivencia celular e está implicado en diversos procesos biolóxicos, como o [[desenvolvemento embrionario]], [[crecemento celular]], [[morfoxénese]], [[reparación de tecidos]], crecemento e invasión tumoral.
 
No tecido normal, o bFGF está presente nas [[membrana basal|membranas basais]] e na [[matriz extracelular]] [[endotelio|subendotelial]] dos [[vaso sanguíneo|vasos sanguíneos]]. Permanece unido á [[membrana plasmática]] se non hai [[péptido sinal]].
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Hipotetizouse que, durante a [[curación de feridas]] en tecido normal e o desenvolvemento de [[tumor]]es, a acción dos [[encima]]s que degradan o [[heparán sulfato]] activan o bFGF, mediando así a formación de novos vasos sanguíneos, un proceso coñecido como [[anxioxénese]].
 
Ademais, é sintetizado e segregado polos [[adipocito]]s humanos e a concentración de FGF2 correlaciónase co [[índice de masa corporal|IMC]] en mostras sanguíneas. Tamén actúa sobre os [[preosteoblasto]]s, incrementando a [[proliferación celular]], despois de unirse ao [[receptor do factor de crecemento de fibroblastos 1]] e activando a [[fosfoinosítido 3-quinase]].<ref>{{citeCita journalpublicación periódica | vauthors = Kühn MC, Willenberg HS, Schott M, Papewalis C, Stumpf U, Flohé S, Scherbaum WA, Schinner S | title = Adipocyte-secreted factors increase osteoblast proliferation and the OPG/RANKL ratio to influence osteoclast formation | journal = Molecular and Cellular Endocrinology | volume = 349 | issue = 2 | pages = 180–8 | date = February 2012 | pmid = 22040599 | doi = 10.1016/j.mce.2011.10.018 }}</ref>
 
O FGF2 demostrou en estudos preliminares en animais protexer o corazón de danos asociados cos ataques ao corazón, reducindo a morte tisular e promovendo unha mellora da función despois da [[terapia de reperfusión|reperfusión]].<ref>{{citeCita journalpublicación periódica | vauthors = House SL, Bolte C, Zhou M, Doetschman T, Klevitsky R, Newman G, Schultz Jel J | title = Cardiac-specific overexpression of fibroblast growth factor-2 protects against myocardial dysfunction and infarction in a murine model of low-flow ischemia | journal = Circulation | volume = 108 | issue = 25 | pages = 3140–8 | date = December 2003 | pmid = 14656920 | doi = 10.1161/01.CIR.0000105723.91637.1C }}</ref>
 
Evidencias recentes indican que baixos niveis de FGF2 xogan un papel clave na incidencia da ansiedade excesiva.<ref name="pmid19439615">{{citeCita journalpublicación periódica | vauthors = Perez JA, Clinton SM, Turner CA, Watson SJ, Akil H | title = A new role for FGF2 as an endogenous inhibitor of anxiety | journal = The Journal of Neuroscience | volume = 29 | issue = 19 | pages = 6379–87 | date = May 2009 | pmid = 19439615 | pmc = 2748795 | doi = 10.1523/JNEUROSCI.4829-08.2009 }}</ref>
 
Adicionalmente, o FGF2 é un compoñente crítico do medio de cultivo de [[célula nai embrionaria|células nais embrionarias]] humanas; o factor de crecemento é necesario para que as células permanezan nun estado indiferenciado, aínda que os mecanismos polos cales o fan non están ben definidos. Demostrouse que induce a expresión de [[gremlina]], a cal á súa vez inhibe a indución da diferenciación por [[proteína morfoxenética ósea|proteínas morfoxenéticas óseas]].<ref>{{citeCita journalpublicación periódica | vauthors = Pereira RC, Economides AN, Canalis E | title = Bone morphogenetic proteins induce gremlin, a protein that limits their activity in osteoblasts | journal = Endocrinology | volume = 141 | issue = 12 | pages = 4558–63 | date = December 2000 | pmid = 11108268 | doi = 10.1210/en.141.12.4558 | url = http://endo.endojournals.org/cgi/pmidlookup?view=long&pmid=11108268 }}</ref> É necesario nos sistemas de cultivo dependentes de células nutricias de rato (fibrobalstos embrionarios de rato que se engaden ao cultivo), así como en sistemas de cultivo libres de soro e células nutricias.<ref>{{citeCita journalpublicación periódica | vauthors = Liu Y, Song Z, Zhao Y, Qin H, Cai J, Zhang H, Yu T, Jiang S, Wang G, Ding M, Deng H | title = A novel chemical-defined medium with bFGF and N2B27 supplements supports undifferentiated growth in human embryonic stem cells | journal = Biochemical and Biophysical Research Communications | volume = 346 | issue = 1 | pages = 131–9 | date = July 2006 | pmid = 16753134 | doi = 10.1016/j.bbrc.2006.05.086 }}</ref> O FGF2, xunto coa [[proteína morfoxenética ósea 4|BMP4]], promove a [[diferenciación celular|diferenciación]] de [[célula nai|células nai]] orixinando liñaxes celulares mesodérmicas. Despois da diferenciación, as células tratadas con BMP4 e FGF2 xeralmente producen unha maior diferenciación [[Osteoblasto|osteoxénica]] e [[Condrocito|condroxénica]] que as células nais non tratadas.<ref>{{citeCita journalpublicación periódica | vauthors = Lee TJ, Jang J, Kang S, Jin M, Shin H, Kim DW, Kim BS | title = Enhancement of osteogenic and chondrogenic differentiation of human embryonic stem cells by mesodermal lineage induction with BMP-4 and FGF2 treatment | journal = Biochemical and Biophysical Research Communications | volume = 430 | issue = 2 | pages = 793–7 | date = January 2013 | pmid = 23206696 | pmc = | doi = 10.1016/j.bbrc.2012.11.067 }}</ref> Porén, unha baixa concentración de bFGF (10 &nbsp;ng/mL) pode exercer un efecto inhibitorio sobre a diferenciación dos [[osteoblasto]]s.<ref>{{citeCita journalpublicación periódica | vauthors = Del Angel-Mosqueda C, Gutiérrez-Puente Y, López-Lozano AP, Romero-Zavaleta RE, Mendiola-Jiménez A, Medina-De la Garza CE, Márquez-M M, De la Garza-Ramos MA | title = Epidermal growth factor enhances osteogenic differentiation of dental pulp stem cells in vitro | journal = Head & Face Medicine | volume = 11 | pages = 29 | date = September 2015 | pmid = 26334535 | doi = 10.1186/s13005-015-0086-5 }}</ref>
 
== Interaccións ==
 
O factor de crecemento de fibroblastos presenta [[interaccións proteína-proteína|interaccións]] coa [[caseína quinase 2, alfa 1]],<ref name=pmid12145206>{{citeCita journalpublicación periódica | vauthors = Skjerpen CS, Nilsen T, Wesche J, Olsnes S | title = Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity | journal = The EMBO Journal | volume = 21 | issue = 15 | pages = 4058–69 | date = August 2002 | pmid = 12145206 | pmc = 126148 | doi = 10.1093/emboj/cdf402 }}</ref> a [[RPL6]]<ref name=pmid9826564>{{citeCita journalpublicación periódica | vauthors = Shen B, Arese M, Gualandris A, Rifkin DB | title = Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107 | journal = Biochemical and Biophysical Research Communications | volume = 252 | issue = 2 | pages = 524–8 | date = November 1998 | pmid = 9826564 | doi = 10.1006/bbrc.1998.9677 }}</ref> e a [[proteína ribosómica S19]].<ref name=pmid11716516>{{citeCita journalpublicación periódica | vauthors = Soulet F, Al Saati T, Roga S, Amalric F, Bouche G | title = Fibroblast growth factor-2 interacts with free ribosomal protein S19 | journal = Biochemical and Biophysical Research Communications | volume = 289 | issue = 2 | pages = 591–6 | date = November 2001 | pmid = 11716516 | doi = 10.1006/bbrc.2001.5960 }}</ref>
 
== Notas ==
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=== Ligazóns externas ===
* {{MeshName|Basic+Fibroblast+Growth+Factor}}
* {{UCSC gene info|FGF2}}
 
 
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