Epidermal growth factor (EGF) was isolated in 1969 by Stanley Cohen in the submaxillary gland of the rat, and its structure was described by Taylor and Cohen in 1972. EGF is a 53-residue polypeptide, weighing 6372 daltons. It is synthesized in a precursor form, as Prepro-EGF, and is secreted into the saliva, intestine and urine. The degradation of EGF takes place primarily in the liver and secondarily in the digestive tract and kidney. EGF is a powerful mitogen, acting upon several types of cells. The epidermal growth factor receptor (EGF-R) is a 170,000 dalton glycoprotein which binds equally to EGF and transforming growth factor alpha (TGF-alpha), a constituent closely homologous to EGF. Presently, published studies concerning the use of EGF in parenteral and enteral nutrition are limited to experimental animals, in which clear effects on cellular proliferation have been observed. It has an important function in the digestive tract, protecting the gastric mucosa from stress and necrotizing agents. Thus, it might be useful in a new nutritional strategies, serving to combine the clearly beneficial effects provided by protein intake (non amino acid with those of the intestinal trophic and growth factors, in both parenteral and enteral nutrition.