Basic fibroblast growth factor

FGF2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases FGF2, BFGF, FGF-2, FGFB, HBGF-2, fibroblast growth factor 2
External IDs MGI: 95516 HomoloGene: 1521 GeneCards: FGF2
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

2247

14173

Ensembl

ENSG00000138685

ENSMUSG00000037225

UniProt

P09038

P15655

RefSeq (mRNA)

NM_002006

NM_008006

RefSeq (protein)

NP_001997.5

NP_032032.1

Location (UCSC) Chr 4: 122.83 – 122.9 Mb Chr 3: 37.35 – 37.41 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Basic fibroblast growth factor, also known as bFGF, FGF2 or FGF-β, is a member of the fibroblast growth factor family.[3]

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.[4]

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.[5]

Recent evidence has shown that low levels of FGF2 play a key role in the incidence of excessive anxiety.[6]

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.[7] It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.[8] 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.[9]

Interactions

Basic fibroblast growth factor has been shown to interact with casein kinase 2, alpha 1,[10] RPL6[11] and ribosomal protein S19.[12]

See also

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. 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.
  4. 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.
  5. 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.
  6. 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 2748795Freely accessible. PMID 19439615.
  7. 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.
  8. 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.
  9. 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.
  10. 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 126148Freely accessible. PMID 12145206.
  11. 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.
  12. 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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