Basic fibroblast growth factor: Difference between revisions

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__NOTOC__
{{Infobox_gene}}
[[Image:PBB Protein-FGF2 image.jpg|thumb|280px|Fibroblast growth factor 2 (basic)--source: [[Protein_Data_Bank|PDB]] rendering based on 1bas.]]
'''Basic fibroblast growth factor''', also known as '''bFGF''', '''FGF2''' or '''FGF-β''', is a member of the [[fibroblast growth factor]] family.<ref name="pmid9925931">{{cite journal | 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>
{{CMG}}


== Function ==
In normal tissue, basic fibroblast growth factor is present in [[basement membrane]]s and in the [[endothelium|subendothelial]] [[extracellular matrix]] of [[blood vessel]]s.  It stays [[plasma membrane|membrane]]-bound as long as there is no [[signal peptide]].


It has been hypothesized that, during both [[wound healing]] of normal tissues and [[tumor]] development, the action of [[heparan sulfate]]-degrading [[enzyme]]s activates bFGF, thus mediating the formation of new [[blood vessel]]s, a process known as [[angiogenesis]].


In addition, it is synthesized and secreted by human [[adipocyte]]s and the concentration of bFGF correlates with the BMI in blood samples. In this study, bFGF was also shown to act on [[preosteoblast]]s&nbsp;– in the form of an increased [[cell proliferation|proliferation]]&nbsp;– after binding to [[fibroblast growth factor receptor 1]] and activating [[phosphoinositide 3-kinase]].<ref>{{cite journal | 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 = Feb 2012 | pmid = 22040599 | doi = 10.1016/j.mce.2011.10.018 }}</ref>


'''Basic fibroblast growth factor''', also known as '''bFGF''' or '''FGF2''', is a member of the '''[[fibroblast growth factor]]''' family.
bFGF has been shown in preliminary animal studies to protect the heart from injury associated with a heart attack, reducing tissue death and promoting improved function after [[Reperfusion therapy|reperfusion]].<ref>{{cite journal | 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 = Dec 2003 | pmid = 14656920 | doi = 10.1161/01.CIR.0000105723.91637.1C }}</ref>


In normal tissue, basic fibroblast growth factor is present in [[basement membrane]]s and in the [[endothelium|subendothelial]] [[extracellular matrix]] of [[blood vessel]]s. It stays [[plasma membrane|membrane]]-bound as long as there is no signal [[peptide]].
Recent evidence has shown that low levels of FGF2 play a key role in the incidence of excessive anxiety.<ref name="pmid19439615">{{cite journal | vauthors = Perez JA, Clinton SM, Turner CA, Watson SJ, Akil H | title = A new role for FGF2 as an endogenous inhibitor of anxiety | journal = J. Neurosci. | volume = 29 | issue = 19 | pages = 6379–87 | year = 2009 | pmid = 19439615 | pmc = 2748795 | doi = 10.1523/JNEUROSCI.4829-08.2009 }}</ref>


It has been hypothesized that, during both [[wound healing]] of normal tissues and [[tumor]] development, the action of [[heparan sulphate]]-degrading [[enzyme]]s activates bFGF, thus mediating the formation of new [[blood vessel]]s, a process known as [[angiogenesis]].
Additionally, bFGF is a critical component of human [[embryonic stem cell]] culture medium; the growth factor is necessary for the cells to remain in an undifferentiated state, although the mechanisms by which it does this are poorly defined. It has been demonstrated to induce [[Gremlin (protein)|gremlin]] expression which in turn is known to inhibit the induction of differentiation by [[bone morphogenetic proteins]].<ref>{{cite journal | 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 = Dec 2000 | pmid = 11108268 | doi = 10.1210/en.141.12.4558 | url = http://endo.endojournals.org/cgi/pmidlookup?view=long&pmid=11108268 }}</ref> It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.<ref>{{cite journal | 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 = Jul 2006 | pmid = 16753134 | doi = 10.1016/j.bbrc.2006.05.086 }}</ref> FGF2, in conjunction with [[Bone morphogenetic protein 4|BMP4]], promote differentiation of stem cells to mesodermal lineages.  After differentiation, BMP4 and FGF2 treated cells generally produces higher amounts of [[Osteoblast|osteogenic]] and [[Chondrocyte|chondrogenic]] differentiation than untreated stem cells.<ref>{{cite journal | 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 = Jan 2013 | pmid = 23206696 | pmc =  | doi = 10.1016/j.bbrc.2012.11.067 }}</ref>


Additionally, bFGF is a critical component of human [[embryonic stem cell]] culture medium; the growth factor is necessary for the cells to remain in an undifferentiated state, although the mechanisms by which it does this are poorly defined. It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.<ref>{{cite journal |author=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=Biochem Biophys Res Commun |volume=346 |issue=1 |pages=131-9 |year=2006 |pmid=16753134}}</ref>
== Interactions ==
 
Basic fibroblast growth factor has been shown to [[Protein-protein interaction|interact]] with [[casein kinase 2, alpha 1]],<ref name=pmid12145206>{{cite journal | 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 = Aug 2002 | pmid = 12145206 | pmc = 126148 | doi = 10.1093/emboj/cdf402 }}</ref> [[RPL6]]<ref name=pmid9826564>{{cite journal | 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 = Nov 1998 | pmid = 9826564 | doi = 10.1006/bbrc.1998.9677 }}</ref> and [[ribosomal protein S19]].<ref name=pmid11716516>{{cite journal | 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 = Nov 2001 | pmid = 11716516 | doi = 10.1006/bbrc.2001.5960 }}</ref>


== See also ==
== See also ==
* [[Angiogenesis]]
* [[Anxiety disorder]]s
* [[Cytokine]]
* [[Fibroblast growth factor]]
* [[Fibroblast growth factor]]
* [[Growth factor]]
* [[Proteases in angiogenesis]]
* [[Receptor (biochemistry)]]
* [[Signal transduction]]
* [[Signal transduction]]
* [[Receptor (biochemistry)]]
{{-}}
* [[Growth Factor]]
== References ==
* [[Cytokine]]
{{Reflist|33em}}
* [[Angiogenesis]]


==References==
== Further reading ==
{{reflist|2}}
{{Refbegin|33em}}
* {{cite journal | vauthors = Ornitz DM, Itoh N | title = Fibroblast growth factors | journal = Genome Biology | volume = 2 | issue = 3 | pages = REVIEWS3005 | year = 2001 | pmid = 11276432 | pmc = 138918 | doi = 10.1186/gb-2001-2-3-reviews3005 }}
* {{cite journal | vauthors = Orpana A, Salven P | title = Angiogenic and lymphangiogenic molecules in hematological malignancies | journal = Leukemia & Lymphoma | volume = 43 | issue = 2 | pages = 219–24 | date = Feb 2002 | pmid = 11999550 | doi = 10.1080/10428190290005964 }}
* {{cite journal | vauthors = Marie PJ, Debiais F, Haÿ E | title = Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling | journal = Histology and Histopathology | volume = 17 | issue = 3 | pages = 877–85 | year = 2003 | pmid = 12168799 | doi =  }}
* {{cite journal | vauthors = Zhao XC, Zhang LM, Tong DY, An P, Jiang C, Zhao P, Chen WM, Wang J | title = Propofol increases expression of basic fibroblast growth factor after transient cerebral ischemia in rats | journal = Neurochemical Research | volume = 38 | issue = 3 | pages = 530–7 | date = Mar 2013 | pmid = 23247820 | pmc = 3574197 | doi = 10.1007/s11064-012-0945-4 }}
* {{cite journal | vauthors = Vincent T, Saklatvala J | title = Basic fibroblast growth factor: an extracellular mechanotransducer in articular cartilage? | journal = Biochemical Society Transactions | volume = 34 | issue = Pt 3 | pages = 456–7 | date = Jun 2006 | pmid = 16709186 | doi = 10.1042/BST0340456 }}
* {{cite journal | vauthors = Ribatti D, Vacca A, Rusnati M, Presta M | title = The discovery of basic fibroblast growth factor/fibroblast growth factor-2 and its role in haematological malignancies | journal = Cytokine & Growth Factor Reviews | volume = 18 | issue = 3-4 | pages = 327–34 | year = 2007 | pmid = 17537668 | doi = 10.1016/j.cytogfr.2007.04.011 }}
* {{cite journal | vauthors = Watson R, Anthony F, Pickett M, Lambden P, Masson GM, Thomas EJ | title = Reverse transcription with nested polymerase chain reaction shows expression of basic fibroblast growth factor transcripts in human granulosa and cumulus cells from in vitro fertilisation patients | journal = Biochemical and Biophysical Research Communications | volume = 187 | issue = 3 | pages = 1227–31 | date = Sep 1992 | pmid = 1417798 | doi = 10.1016/0006-291X(92)90434-M }}
* {{cite journal | vauthors = Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, Hsu BT, Rees DC | title = Three-dimensional structures of acidic and basic fibroblast growth factors | journal = Science | volume = 251 | issue = 4989 | pages = 90–3 | date = Jan 1991 | pmid = 1702556 | doi = 10.1126/science.1702556 }}
* {{cite journal | vauthors = Eriksson AE, Cousens LS, Weaver LH, Matthews BW | title = Three-dimensional structure of human basic fibroblast growth factor | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 8 | pages = 3441–5 | date = Apr 1991 | pmid = 1707542 | pmc = 51463 | doi = 10.1073/pnas.88.8.3441 }}
* {{cite journal | vauthors = Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y | title = Crystal structure of basic fibroblast growth factor at 1.6 A resolution | journal = Journal of Biochemistry | volume = 110 | issue = 3 | pages = 360–3 | date = Sep 1991 | pmid = 1769963 | doi =  }}
* {{cite journal | 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 =  | pages = 109–26 | year = 1992 | pmid = 1785797 | doi = 10.1111/j.1749-6632.1991.tb49022.x }}
* {{cite journal | vauthors = Zhang JD, Cousens LS, Barr PJ, Sprang SR | title = Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 8 | pages = 3446–50 | date = Apr 1991 | pmid = 1849658 | pmc = 51464 | doi = 10.1073/pnas.88.8.3446 }}
* {{cite journal | vauthors = Wu DQ, Kan MK, Sato GH, Okamoto T, Sato JD | title = Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors | journal = The Journal of Biological Chemistry | volume = 266 | issue = 25 | pages = 16778–85 | date = Sep 1991 | pmid = 1885605 | doi =  }}
* {{cite journal | vauthors = Fukushima Y, Byers MG, Fiddes JC, Shows TB | title = The human basic fibroblast growth factor gene (FGFB) is assigned to chromosome 4q25 | journal = Cytogenetics and Cell Genetics | volume = 54 | issue = 3-4 | pages = 159–60 | year = 1991 | pmid = 2265560 | doi = 10.1159/000132983 }}
* {{cite journal | vauthors = Lafage-Pochitaloff M, Galland F, Simonetti J, Prats H, Mattei MG, Birnbaum D | title = The human basic fibroblast growth factor gene is located on the long arm of chromosome 4 at bands q26-q27 | journal = Oncogene Research | volume = 5 | issue = 3 | pages = 241–4 | year = 1990 | pmid = 2320377 | doi =  }}
* {{cite journal | vauthors = Story MT, Esch F, Shimasaki S, Sasse J, Jacobs SC, Lawson RK | title = Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue | journal = Biochemical and Biophysical Research Communications | volume = 142 | issue = 3 | pages = 702–9 | date = Feb 1987 | pmid = 2435284 | doi = 10.1016/0006-291X(87)91471-9 }}
* {{cite journal | vauthors = Kurokawa T, Sasada R, Iwane M, Igarashi K | title = Cloning and expression of cDNA encoding human basic fibroblast growth factor | journal = FEBS Letters | volume = 213 | issue = 1 | pages = 189–94 | date = Mar 1987 | pmid = 2435575 | doi = 10.1016/0014-5793(87)81489-8 }}
* {{cite journal | vauthors = Prats H, Kaghad M, Prats AC, Klagsbrun M, Lélias JM, Liauzun P, Chalon P, Tauber JP, Amalric F, Smith JA | title = High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 6 | pages = 1836–40 | date = Mar 1989 | pmid = 2538817 | pmc = 286799 | doi = 10.1073/pnas.86.6.1836 }}
* {{cite journal | vauthors = Florkiewicz RZ, Sommer A | title = Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 11 | pages = 3978–81 | date = Jun 1989 | pmid = 2726761 | pmc = 287371 | doi = 10.1073/pnas.86.11.3978 }}
* {{cite journal | vauthors = Abraham JA, Whang JL, Tumolo A, Mergia A, Fiddes JC | title = Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells | journal = Cold Spring Harbor Symposia on Quantitative Biology | volume = 51 Pt 1 | issue =  | pages = 657–68 | year = 1987 | pmid = 3472745 | doi = 10.1101/sqb.1986.051.01.078 }}
* {{cite journal | vauthors = Sommer A, Brewer MT, Thompson RC, Moscatelli D, Presta M, Rifkin DB | title = A form of human basic fibroblast growth factor with an extended amino terminus | journal = Biochemical and Biophysical Research Communications | volume = 144 | issue = 2 | pages = 543–50 | date = Apr 1987 | pmid = 3579930 | doi = 10.1016/S0006-291X(87)80001-3 }}
{{Refend}}
{{PDB Gallery|geneid=2247}}


==Further reading==
== External links ==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Ornitz DM, Itoh N |title=Fibroblast growth factors. |journal=Genome Biol. |volume=2 |issue= 3 |pages= REVIEWS3005 |year= 2001 |pmid= 11276432 |doi=  }}
*{{cite journal  | author=Orpana A, Salven P |title=Angiogenic and lymphangiogenic molecules in hematological malignancies. |journal=Leuk. Lymphoma |volume=43 |issue= 2 |pages= 219-24 |year= 2003 |pmid= 11999550 |doi=  }}
*{{cite journal  | author=Marie PJ, Debiais F, Haÿ E |title=Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling. |journal=Histol. Histopathol. |volume=17 |issue= 3 |pages= 877-85 |year= 2003 |pmid= 12168799 |doi=  }}
*{{cite journal  | author=Vincent T, Saklatvala J |title=Basic fibroblast growth factor: an extracellular mechanotransducer in articular cartilage? |journal=Biochem. Soc. Trans. |volume=34 |issue= Pt 3 |pages= 456-7 |year= 2006 |pmid= 16709186 |doi= 10.1042/BST0340456 }}
*{{cite journal  | author=Ribatti D, Vacca A, Rusnati M, Presta M |title=The discovery of basic fibroblast growth factor/fibroblast growth factor-2 and its role in haematological malignancies. |journal=Cytokine Growth Factor Rev. |volume=18 |issue= 3-4 |pages= 327-34 |year= 2007 |pmid= 17537668 |doi= 10.1016/j.cytogfr.2007.04.011 }}
*{{cite journal  | author=Watson R, Anthony F, Pickett M, ''et al.'' |title=Reverse transcription with nested polymerase chain reaction shows expression of basic fibroblast growth factor transcripts in human granulosa and cumulus cells from in vitro fertilisation patients. |journal=Biochem. Biophys. Res. Commun. |volume=187 |issue= 3 |pages= 1227-31 |year= 1992 |pmid= 1417798 |doi=  }}
*{{cite journal  | author=Zhu X, Komiya H, Chirino A, ''et al.'' |title=Three-dimensional structures of acidic and basic fibroblast growth factors. |journal=Science |volume=251 |issue= 4989 |pages= 90-3 |year= 1991 |pmid= 1702556 |doi=  }}
*{{cite journal  | author=Eriksson AE, Cousens LS, Weaver LH, Matthews BW |title=Three-dimensional structure of human basic fibroblast growth factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 3441-5 |year= 1991 |pmid= 1707542 |doi=  }}
*{{cite journal  | author=Ago H, Kitagawa Y, Fujishima A, ''et al.'' |title=Crystal structure of basic fibroblast growth factor at 1.6 A resolution. |journal=J. Biochem. |volume=110 |issue= 3 |pages= 360-3 |year= 1992 |pmid= 1769963 |doi=  }}
*{{cite journal  | author=Florkiewicz RZ, Shibata F, Barankiewicz T, ''et al.'' |title=Basic fibroblast growth factor gene expression. |journal=Ann. N. Y. Acad. Sci. |volume=638 |issue=  |pages= 109-26 |year= 1992 |pmid= 1785797 |doi=  }}
*{{cite journal  | author=Zhang JD, Cousens LS, Barr PJ, Sprang SR |title=Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 3446-50 |year= 1991 |pmid= 1849658 |doi=  }}
*{{cite journal  | author=Wu DQ, Kan MK, Sato GH, ''et al.'' |title=Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors. |journal=J. Biol. Chem. |volume=266 |issue= 25 |pages= 16778-85 |year= 1991 |pmid= 1885605 |doi=  }}
*{{cite journal  | author=Fukushima Y, Byers MG, Fiddes JC, Shows TB |title=The human basic fibroblast growth factor gene (FGFB) is assigned to chromosome 4q25. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 3-4 |pages= 159-60 |year= 1991 |pmid= 2265560 |doi=  }}
*{{cite journal  | author=Lafage-Pochitaloff M, Galland F, Simonetti J, ''et al.'' |title=The human basic fibroblast growth factor gene is located on the long arm of chromosome 4 at bands q26-q27. |journal=Oncogene Res. |volume=5 |issue= 3 |pages= 241-4 |year= 1990 |pmid= 2320377 |doi=  }}
*{{cite journal  | author=Story MT, Esch F, Shimasaki S, ''et al.'' |title=Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue. |journal=Biochem. Biophys. Res. Commun. |volume=142 |issue= 3 |pages= 702-9 |year= 1987 |pmid= 2435284 |doi=  }}
*{{cite journal  | author=Kurokawa T, Sasada R, Iwane M, Igarashi K |title=Cloning and expression of cDNA encoding human basic fibroblast growth factor. |journal=FEBS Lett. |volume=213 |issue= 1 |pages= 189-94 |year= 1987 |pmid= 2435575 |doi=  }}
*{{cite journal  | author=Prats H, Kaghad M, Prats AC, ''et al.'' |title=High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 6 |pages= 1836-40 |year= 1989 |pmid= 2538817 |doi=  }}
*{{cite journal  | author=Florkiewicz RZ, Sommer A |title=Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 11 |pages= 3978-81 |year= 1989 |pmid= 2726761 |doi=  }}
*{{cite journal  | author=Abraham JA, Whang JL, Tumolo A, ''et al.'' |title=Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=51 Pt 1 |issue=  |pages= 657-68 |year= 1987 |pmid= 3472745 |doi=  }}
*{{cite journal  | author=Sommer A, Brewer MT, Thompson RC, ''et al.'' |title=A form of human basic fibroblast growth factor with an extended amino terminus. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 2 |pages= 543-50 |year= 1987 |pmid= 3579930 |doi=  }}
}}
{{refend}}
 
==External links==
* {{MeshName|Basic+Fibroblast+Growth+Factor}}
* {{MeshName|Basic+Fibroblast+Growth+Factor}}
 
* {{UCSC gene info|FGF2}}


{{Signaling proteins}}
{{Signaling proteins}}
{{Growth factor receptor modulators}}


[[Category:Growth factors]]
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Basic fibroblast growth factor, also known as bFGF, FGF2 or FGF-β, is a member of the fibroblast growth factor family.[1]

Function

In normal tissue, basic fibroblast growth factor is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. It stays membrane-bound as long as there is no signal peptide.

It has been hypothesized that, during both wound healing of normal tissues and tumor development, the action of heparan sulfate-degrading enzymes activates bFGF, thus mediating the formation of new blood vessels, a process known as angiogenesis.

In addition, it is synthesized and secreted by human adipocytes and the concentration of bFGF correlates with the BMI in blood samples. In this study, bFGF was also shown to act on preosteoblasts – in the form of an increased proliferation – after binding to fibroblast growth factor receptor 1 and activating phosphoinositide 3-kinase.[2]

bFGF has been shown in preliminary animal studies to protect the heart from injury associated with a heart attack, reducing tissue death and promoting improved function after reperfusion.[3]

Recent evidence has shown that low levels of FGF2 play a key role in the incidence of excessive anxiety.[4]

Additionally, bFGF is a critical component of human embryonic stem cell culture medium; the growth factor is necessary for the cells to remain in an undifferentiated state, although the mechanisms by which it does this are poorly defined. It has been demonstrated to induce gremlin expression which in turn is known to inhibit the induction of differentiation by bone morphogenetic proteins.[5] It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.[6] FGF2, in conjunction with BMP4, promote differentiation of stem cells to mesodermal lineages. After differentiation, BMP4 and FGF2 treated cells generally produces higher amounts of osteogenic and chondrogenic differentiation than untreated stem cells.[7]

Interactions

Basic fibroblast growth factor has been shown to interact with casein kinase 2, alpha 1,[8] RPL6[9] and ribosomal protein S19.[10]

See also

References

  1. ↑ Kim HS (1998). "Assignment1 of the human basic fibroblast growth factor gene FGF2 to chromosome 4 band q26 by radiation hybrid mapping". Cytogenetics and Cell Genetics. 83 (1–2): 73. doi:10.1159/000015129. PMID 9925931.
  2. ↑ Kühn MC, Willenberg HS, Schott M, Papewalis C, Stumpf U, Flohé S, Scherbaum WA, Schinner S (Feb 2012). "Adipocyte-secreted factors increase osteoblast proliferation and the OPG/RANKL ratio to influence osteoclast formation". Molecular and Cellular Endocrinology. 349 (2): 180–8. doi:10.1016/j.mce.2011.10.018. PMID 22040599.
  3. ↑ House SL, Bolte C, Zhou M, Doetschman T, Klevitsky R, Newman G, Schultz Jel J (Dec 2003). "Cardiac-specific overexpression of fibroblast growth factor-2 protects against myocardial dysfunction and infarction in a murine model of low-flow ischemia". Circulation. 108 (25): 3140–8. doi:10.1161/01.CIR.0000105723.91637.1C. PMID 14656920.
  4. ↑ Perez JA, Clinton SM, Turner CA, Watson SJ, Akil H (2009). "A new role for FGF2 as an endogenous inhibitor of anxiety". J. Neurosci. 29 (19): 6379–87. doi:10.1523/JNEUROSCI.4829-08.2009. PMC 2748795. PMID 19439615.
  5. ↑ Pereira RC, Economides AN, Canalis E (Dec 2000). "Bone morphogenetic proteins induce gremlin, a protein that limits their activity in osteoblasts". Endocrinology. 141 (12): 4558–63. doi:10.1210/en.141.12.4558. PMID 11108268.
  6. ↑ Liu Y, Song Z, Zhao Y, Qin H, Cai J, Zhang H, Yu T, Jiang S, Wang G, Ding M, Deng H (Jul 2006). "A novel chemical-defined medium with bFGF and N2B27 supplements supports undifferentiated growth in human embryonic stem cells". Biochemical and Biophysical Research Communications. 346 (1): 131–9. doi:10.1016/j.bbrc.2006.05.086. PMID 16753134.
  7. ↑ Lee TJ, Jang J, Kang S, Jin M, Shin H, Kim DW, Kim BS (Jan 2013). "Enhancement of osteogenic and chondrogenic differentiation of human embryonic stem cells by mesodermal lineage induction with BMP-4 and FGF2 treatment". Biochemical and Biophysical Research Communications. 430 (2): 793–7. doi:10.1016/j.bbrc.2012.11.067. PMID 23206696.
  8. ↑ Skjerpen CS, Nilsen T, Wesche J, Olsnes S (Aug 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". The EMBO Journal. 21 (15): 4058–69. doi:10.1093/emboj/cdf402. PMC 126148. PMID 12145206.
  9. ↑ Shen B, Arese M, Gualandris A, Rifkin DB (Nov 1998). "Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107". Biochemical and Biophysical Research Communications. 252 (2): 524–8. doi:10.1006/bbrc.1998.9677. PMID 9826564.
  10. ↑ Soulet F, Al Saati T, Roga S, Amalric F, Bouche G (Nov 2001). "Fibroblast growth factor-2 interacts with free ribosomal protein S19". Biochemical and Biophysical Research Communications. 289 (2): 591–6. doi:10.1006/bbrc.2001.5960. PMID 11716516.

Further reading

External links


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