Basic fibroblast growth factor

Fibroblast growth factor 2 (basic)
	; PDB rendering based on 1bas.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BAS, 1BFB, 1BFC, 1BFF, 1BFG, 1BLA, 1BLD, 1CVS, 1EV2, 1FGA, 1FQ9, 1II4, 1IIL, 2BFH, 2FGF, 4FGF
Identifiers
Symbols	FGF2; BFGF; FGF-2; FGFB; HBGF-2
External IDs	OMIM: 134920 MGI: 95516 HomoloGene: 1521 ChEMBL: 3107 GeneCards: FGF2 Gene
Gene Ontology
Molecular function	• fibroblast growth factor receptor binding; • cytokine activity; • protein binding; • growth factor activity; • heparin binding; • fibroblast growth factor binding; • ligand-dependent nuclear receptor transcription coactivator activity; • chemoattractant activity;
Cellular component	• extracellular region; • extracellular space; • nucleus; • cytosol;
Biological process	• activation of MAPKK activity; • activation of MAPK activity; • MAPK import into nucleus; • branching involved in ureteric bud morphogenesis; • organ induction; • positive regulation of endothelial cell proliferation; • cell migration involved in sprouting angiogenesis; • phosphatidylinositol biosynthetic process; • C21-steroid hormone biosynthetic process; • apoptotic process; • chemotaxis; • signal transduction; • epidermal growth factor receptor signaling pathway; • Ras protein signal transduction; • nervous system development; • positive regulation of cell proliferation; • negative regulation of cell proliferation; • insulin receptor signaling pathway; • fibroblast growth factor receptor signaling pathway; • organ morphogenesis; • glial cell differentiation; • negative regulation of fibroblast migration; • positive regulation of phospholipase C activity; • substantia nigra development; • positive regulation of cerebellar granule cell precursor proliferation; • hyaluronan catabolic process; • negative regulation of cell growth; • lung development; • inositol phosphate biosynthetic process; • wound healing; • positive regulation of cell fate specification; • positive regulation of blood vessel endothelial cell migration; • negative regulation of blood vessel endothelial cell migration; • positive regulation of phosphatidylinositol 3-kinase activity; • innate immune response; • positive regulation of osteoblast differentiation; • regulation of angiogenesis; • positive regulation of angiogenesis; • negative regulation of transcription, DNA-dependent; • positive regulation of transcription, DNA-dependent; • positive regulation of transcription from RNA polymerase II promoter; • regulation of retinal cell programmed cell death; • neurotrophin TRK receptor signaling pathway; • phosphatidylinositol-mediated signaling; • embryonic morphogenesis; • response to axon injury; • stem cell development; • positive chemotaxis; • release of sequestered calcium ion into cytosol; • regulation of cell cycle; • positive regulation of cell division; • positive regulation of cardiac muscle cell proliferation; • corticotropin hormone secreting cell differentiation; • thyroid-stimulating hormone-secreting cell differentiation; • negative regulation of cell death; • chondroblast differentiation; • mammary gland epithelial cell differentiation; • negative regulation of wound healing; • positive regulation of ERK1 and ERK2 cascade;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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Basic fibroblast growth factor, also known as bFGF, FGF2 or FGF-β,^[1] is a member of the fibroblast growth factor family.^[2]

Function [edit]

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^{[disambiguation needed]} - 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. [3]

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 chondorgenic differentiation than untreated stem cells.^[7]

Interactions [edit]

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

References [edit]

^ Horst Ibelgaufts' COPE: FGF-beta
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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
^ 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.
^ 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.
^ 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.