BFGF

This MedLibrary.org supplementary page on BFGF is provided directly from the open source Wikipedia as a service to our readers. Please see the note below on authorship of this content, as well as the Wikipedia usage guidelines. To search for other content from our encyclopedia supplement, please use the form below:

Related Sponsors

BM Pharmacy Generic pharmaceuticals at unbeatable prices. Insomnia, men's health, hair health, pain control. bmpharmacy.com
Online Pharmacy Carisoprodol, tadalafil, sildenafil, vardenafil and more... xlpharmacy.com
MedBasket.com Discreet. Inexpensive. Fast shipping. Great selection. What more can we say? medbasket.com
Frugalmed 2000 reasons to shop with us first. frugalmed.com
Ads by Tiva

Fibroblast growth factor 2 (basic)
PDB rendering based on 1bas.
Available structures: 1bas, 1bfb, 1bfc, 1bff, 1bfg, 1bla, 1bld, 1cvs, 1ev2, 1fga, 1fq9, 1ii4, 1iil, 2bfh, 2fgf, 4fgf
Identifiers
Symbols FGF2; BFGF; FGFB; HBGH-2
External IDs OMIM: 134920 MGI: 95516 HomoloGene: 1521
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 2247 14173
Ensembl ENSG00000138685 ENSMUSG00000037225
Uniprot P09038 Q541T2
Refseq NM_002006 (mRNA)
NP_001997 (protein)		 NM_008006 (mRNA)
NP_032032 (protein)
Location Chr 4: 123.97 - 124.04 Mb Chr 3: 37.54 - 37.6 Mb
Pubmed search [1] [2]

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

Contents

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.

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.[2] It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.[3]

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". Cytogenet. Cell Genet. 83 (1-2): 73. doi:10.1159/000015129. PMID 9925931. 
  2. ^ 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. PMID 11108268. 
  3. ^ 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. 

Further reading

  • Ornitz DM, Itoh N (2001). "Fibroblast growth factors.". Genome Biol. 2 (3): REVIEWS3005. doi:10.1186/gb-2001-2-3-reviews3005. PMID 11276432. 
  • Orpana A, Salven P (2003). "Angiogenic and lymphangiogenic molecules in hematological malignancies.". Leuk. Lymphoma 43 (2): 219–24. doi:10.1080/10428190290005964. PMID 11999550. 
  • Marie PJ, Debiais F, Haÿ E (2003). "Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling.". Histol. Histopathol. 17 (3): 877–85. PMID 12168799. 
  • Vincent T, Saklatvala J (2006). "Basic fibroblast growth factor: an extracellular mechanotransducer in articular cartilage?". Biochem. Soc. Trans. 34 (Pt 3): 456–7. doi:10.1042/BST0340456. PMID 16709186. 
  • Ribatti D, Vacca A, Rusnati M, Presta M (2007). "The discovery of basic fibroblast growth factor/fibroblast growth factor-2 and its role in haematological malignancies.". Cytokine Growth Factor Rev. 18 (3-4): 327–34. doi:10.1016/j.cytogfr.2007.04.011. PMID 17537668. 
  • Watson R, Anthony F, Pickett M, et al. (1992). "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.". Biochem. Biophys. Res. Commun. 187 (3): 1227–31. doi:10.1016/0006-291X(92)90434-M. PMID 1417798. 
  • Zhu X, Komiya H, Chirino A, et al. (1991). "Three-dimensional structures of acidic and basic fibroblast growth factors.". Science 251 (4989): 90–3. doi:10.1126/science.1702556. PMID 1702556. 
  • Eriksson AE, Cousens LS, Weaver LH, Matthews BW (1991). "Three-dimensional structure of human basic fibroblast growth factor.". Proc. Natl. Acad. Sci. U.S.A. 88 (8): 3441–5. doi:10.1073/pnas.88.8.3441. PMID 1707542. 
  • Ago H, Kitagawa Y, Fujishima A, et al. (1992). "Crystal structure of basic fibroblast growth factor at 1.6 A resolution.". J. Biochem. 110 (3): 360–3. PMID 1769963. 
  • Florkiewicz RZ, Shibata F, Barankiewicz T, et al. (1992). "Basic fibroblast growth factor gene expression.". Ann. N. Y. Acad. Sci. 638: 109–26. doi:10.1111/j.1749-6632.1991.tb49022.x. PMID 1785797. 
  • Zhang JD, Cousens LS, Barr PJ, Sprang SR (1991). "Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta.". Proc. Natl. Acad. Sci. U.S.A. 88 (8): 3446–50. doi:10.1073/pnas.88.8.3446. PMID 1849658. 
  • Wu DQ, Kan MK, Sato GH, et al. (1991). "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors.". J. Biol. Chem. 266 (25): 16778–85. PMID 1885605. 
  • Fukushima Y, Byers MG, Fiddes JC, Shows TB (1991). "The human basic fibroblast growth factor gene (FGFB) is assigned to chromosome 4q25.". Cytogenet. Cell Genet. 54 (3-4): 159–60. doi:10.1159/000132983. PMID 2265560. 
  • Lafage-Pochitaloff M, Galland F, Simonetti J, et al. (1990). "The human basic fibroblast growth factor gene is located on the long arm of chromosome 4 at bands q26-q27.". Oncogene Res. 5 (3): 241–4. PMID 2320377. 
  • Story MT, Esch F, Shimasaki S, et al. (1987). "Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue.". Biochem. Biophys. Res. Commun. 142 (3): 702–9. doi:10.1016/0006-291X(87)91471-9. PMID 2435284. 
  • Kurokawa T, Sasada R, Iwane M, Igarashi K (1987). "Cloning and expression of cDNA encoding human basic fibroblast growth factor.". FEBS Lett. 213 (1): 189–94. doi:10.1016/0014-5793(87)81489-8. PMID 2435575. 
  • Prats H, Kaghad M, Prats AC, et al. (1989). "High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons.". Proc. Natl. Acad. Sci. U.S.A. 86 (6): 1836–40. doi:10.1073/pnas.86.6.1836. PMID 2538817. 
  • Florkiewicz RZ, Sommer A (1989). "Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons.". Proc. Natl. Acad. Sci. U.S.A. 86 (11): 3978–81. doi:10.1073/pnas.86.11.3978. PMID 2726761. 
  • Abraham JA, Whang JL, Tumolo A, et al. (1987). "Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells.". Cold Spring Harb. Symp. Quant. Biol. 51 Pt 1: 657–68. PMID 3472745. 
  • Sommer A, Brewer MT, Thompson RC, et al. (1987). "A form of human basic fibroblast growth factor with an extended amino terminus.". Biochem. Biophys. Res. Commun. 144 (2): 543–50. doi:10.1016/S0006-291X(87)80001-3. PMID 3579930. 

External links


 This article on a gene on chromosome 4 is a stub. You can help Wikipedia by expanding it.
v • d • e
Growth factors
Fibroblast
FGF receptor ligands: 1 (acidic)/2 (basic)/5 · 3/4/6 · KGF (7/10/22) · 8/17/18 · 9/16/20

FGF homologous factors: 11 · 12 · 13 · 14

hormone-like: 19 · 21 · 23
EGF-like domain
TGFβ pathway
TGFβ (1, 2, 3)
Insulin-like
1 · 2
Platelet-derived
A · B · C · D
Vascular endothelial
A · B · C · D · PGF
Other

Wikipedia content modification information:

  • This page was last modified on 26 September 2008, at 22:45.

Wikipedia Authorship and Review

Wikipedia content provided here is not reviewed directly by MedLibrary.org. Wikipedia content is authored by an open community of volunteers and is not produced by or in any way affiliated with MedLibrary.org.

Wikipedia Usage Guidelines

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article on "BFGF".

The URL for this specific entry is:

All Wikipedia text is available under the terms of the GNU Free Documentation License. (See Copyrights for details). Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc.