FGF-2 (basic)

FGF2 (basic) is one of at least 23 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans (HSPG) are likely. FGF2 has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF2 retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF2 are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF2 in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF2 stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. The cells include fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, osteoblasts, smooth muscle cells, and melanocytes. FGF2 is chemotactic and mitogenic for endothelial cells in vitro. FGF2 induces neuron differentiation, survival and regeneration. The 17 kDa porcine sequence has 95% aa identity with human and sheep FGF basic.