Basic fibroblast growth factor

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Fibroblast growth factor 2 (basic)
Protein FGF2 PDB 1bas.png
PDB rendering based on 1bas.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols FGF2 ; BFGF; FGF-2; FGFB; HBGF-2
External IDs OMIM134920 MGI95516 HomoloGene1521 ChEMBL: 3107 GeneCards: FGF2 Gene
RNA expression pattern
PBB GE FGF2 204422 s at tn.png
PBB GE FGF2 204421 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2247 14173
Ensembl ENSG00000138685 ENSMUSG00000037225
UniProt P09038 P15655
RefSeq (mRNA) NM_002006 NM_008006
RefSeq (protein) NP_001997 NP_032032
Location (UCSC) Chr 4:
122.83 – 122.9 Mb
Chr 3:
37.35 – 37.41 Mb
PubMed search [1] [2]

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


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]


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[edit]


  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. 

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