Fibroblast growth factor-2

• Published in: The international journal of biochemistry & cell biology 2000-02, Vol.32 (2), p.115-120
• Main Authors: Nugent, Matthew A, Iozzo, Renato V
• Format: Article
• Language: English
• Subjects: Animals; Fibroblast growth factor; Fibroblast Growth Factor 2 - chemistry; Fibroblast Growth Factor 2 - pharmacology; Fibroblast Growth Factor 2 - physiology; Heparan sulfate; Heparan Sulfate Proteoglycans - metabolism; Heparin - metabolism; Heparitin Sulfate - metabolism; Humans; Models, Biological; Models, Molecular; Protein Conformation; Proteoglycans; Signal Transduction
• ISSN: 1357-2725; 1878-5875
• DOI: 10.1016/S1357-2725(99)00123-5

Fibroblast growth factor-2 (FGF-2) is a member of a large family of proteins that bind heparin and heparan sulfate and modulate the function of a wide range of cell types. FGF-2 stimulates the growth and development of new blood vessels (angiogenesis) that contribute to the pathogenesis of several diseases (i.e. cancer, atherosclerosis), normal wound healing and tissue development. FGF-2 contains a number of basic residues (p I 9.6) and consists of 12 anti-parallel β-sheets organized into a trigonal pyrimidal structure. FGF-2 binds to four cell surface receptors expressed as a number of splice variants. Many of the biological activities of FGF-2 have been found to depend on its receptor's intrinsic tyrosine kinase activity and second messengers such as the mitogen activated protein kinases. However, considerable evidence suggest that intracellular FGF-2 might have a direct biological role particularly within the nucleus. In addition, heparan sulfate proteoglycans have been demonstrated to enhance and inhibit FGF-2 activity. The possibility that FGF-2 activity can be manipulated through alterations in heparan sulfate-binding is currently being exploited in the development of clinical applications aimed at modulating either endogenous or administered FGF-2 activity.