Epidermal growth factor or EGF is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds.
Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell increase, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha metamorphosing growing component (hTGF alpha), which equals a competitor for EGF receptor sites. EGF is a small 53 amino acid residue long protein that contains three disulfide briges. The activity of epidermal growth factor family members is mediated by the epidermal growth factor (EGFR/ErbB) receptor tyrosine kinases. Members of epidermal growth factor family are known to be involved in tumor formation. The mediations of EGF therapy are so far mainly based on inhibiting the EGF receptor.
The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. EGF is part of a complex network of growth factors and receptors that together help to modulate the growth of cells. EGF is released by cells, and then is picked up either by the cell itself, stimulating its own growth, or by neighboring cells, stimulating their ability to divide.
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