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,[1] is a member of the fibroblast growth factor family.[2]


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.[3]

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.[4]

Recent evidence has shown that low levels of FGF2 play a key role in the incidence of excessive anxiety.[5]

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.[6] It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.[7] 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.[8]


Basic fibroblast growth factor has been shown to interact with casein kinase 2, alpha 1,[9] RPL6[10] and ribosomal protein S19.[11]

See also[edit]


  1. ^ Horst Ibelgaufts' COPE: FGF-beta
  2. ^ Kim HS (1998). "Assignment1 of the human basic fibroblast growth factor gene FGF2 to chromosome 4 band q26 by radiation hybrid mapping". Cytogenet. Cell Genet. 83 (1-2): 73. doi:10.1159/000015129. PMID 9925931. 
  3. ^ Kühn MC, Willenberg HS, Schott M, Papewalis C, Stumpf U, Flohé S, Scherbaum WA, Schinner S. (2012). "Adipocyte-secreted factors increase osteoblast proliferation and the OPG/RANKL ratio to influence osteoclast formation.". Mol Cell Endocrinol. 349 (2): 180–188. doi:10.1016/j.mce.2011.10.018. PMID 22040599. 
  4. ^ House SL, Bolte C, Zhou M, Doetschman T, Klevitsky R, Newman G, Schultz Jel J. (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 (1): 3140–3148. doi:10.1161/01.CIR.0000105723.91637.1C. PMID 14656920. 
  5. ^ Perez, Javier; Clinton, Sarah; Turner, Cortney; Watson, Huda; Akil, Stanleydate=. "A New Role for FGF2 as an Endogenous Inhibitor of Anxiety". J. Neurosci. 29 (19): 6379–87. Retrieved 13 April 2015. 
  6. ^ Pereira RC, Economides AN, Canalis E (December 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. 
  7. ^ Liu Y, Song Z, Zhao Y, Qin H, Cai J, Zhang H, Yu T, Jiang S, Wang G, Ding M, Deng H (2006). "A novel chemical-defined medium with bFGF and N2B27 supplements supports undifferentiated growth in human embryonic stem cells". Biochem Biophys Res Commun 346 (1): 131–9. doi:10.1016/j.bbrc.2006.05.086. PMID 16753134. 
  8. ^ Lee, T. J.; Jang, J.; Kang, S.; Jin, M.; Shin, H.; Kim, D. W.; Kim, B. S. (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): 793–797. doi:10.1016/j.bbrc.2012.11.067. PMID 23206696.  edit
  9. ^ Skjerpen, Camilla Skiple; Nilsen Trine; Wesche Jørgen; Olsnes Sjur (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. (England) 21 (15): 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206. 
  10. ^ Shen, B; Arese M; Gualandris A; Rifkin D B (November 1998). "Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107". Biochem. Biophys. Res. Commun. (UNITED STATES) 252 (2): 524–8. doi:10.1006/bbrc.1998.9677. ISSN 0006-291X. PMID 9826564. 
  11. ^ Soulet, F; Al Saati T; Roga S; Amalric F; Bouche G (November 2001). "Fibroblast growth factor-2 interacts with free ribosomal protein S19". Biochem. Biophys. Res. Commun. (United States) 289 (2): 591–6. doi:10.1006/bbrc.2001.5960. ISSN 0006-291X. PMID 11716516. 

Further reading[edit]

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