Epidermal Growth Factor (EGF) is a small polypeptide consisting of 53 amino acid residues with a molecular mass of approximately 6000 daltons . It was first identified and isolated by Stanley Cohen in 1962 . EGF is a potent mitogen, meaning it stimulates cell division and proliferation, particularly in epithelial cells. This growth factor plays a crucial role in various physiological processes, including cell growth, differentiation, and survival.
EGF is known for its significant role in epithelial cell renewal, which is essential for maintaining the integrity of tissues that undergo constant wear and tear, such as the skin and the lining of the gastrointestinal tract . In rats, EGF has been shown to have profound effects on gastrointestinal cell proliferation and crypt fission, which are mechanisms that increase tissue mass .
EGF exerts its effects by binding to the Epidermal Growth Factor Receptor (EGFR) on the cell surface. This binding triggers a cascade of intracellular signaling pathways that lead to various cellular responses, including DNA synthesis and cell division . The EGF-EGFR interaction is also implicated in the regulation of gastric acid secretion and has a cytoprotective effect on the gastroduodenal mucosa .
Studies have shown that continuous infusion of EGF in rats significantly increases epithelial cell proliferation and crypt and villus area in the small intestine . In the colon, EGF causes a twofold increase in epithelial cell proliferation and alters crypt fission, with its actions being most pronounced during short-term infusion . These findings highlight the potential of EGF as a therapeutic agent for conditions involving impaired epithelial cell proliferation and tissue repair.