Structure and function of human amphiregulin: a member of the epidermal growth factor family

Science. 1989 Feb 24;243(4894 Pt 1):1074-6. doi: 10.1126/science.2466334.


The complete amino acid sequence of amphiregulin, a bifunctional cell growth modulator, was determined. The truncated form contains 78 amino acids, whereas a larger form of amphiregulin contains six additional amino acids at the amino-terminal end. The amino-terminal half of amphiregulin is extremely hydrophilic and contains unusually high numbers of lysine, arginine, and asparagine residues. The carboxyl-terminal half of amphiregulin (residues 46 to 84) exhibits striking homology to the epidermal growth factor (EGF) family of proteins. Amphiregulin binds to the EGF receptor but not as well as EGF does. Amphiregulin fully supplants the requirement for EGF or transforming growth factor-alpha in murine keratinocyte growth, but it is a much weaker growth stimulator in other cell systems.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amphiregulin
  • Animals
  • Binding, Competitive
  • Cell Division
  • EGF Family of Proteins
  • Epidermal Cells
  • Epidermal Growth Factor / physiology
  • ErbB Receptors / metabolism
  • Glycoproteins / physiology*
  • Growth Substances / physiology*
  • Humans
  • Intercellular Signaling Peptides and Proteins*
  • Keratins / metabolism
  • Mice
  • Molecular Sequence Data
  • Radioligand Assay
  • Sequence Homology, Nucleic Acid
  • Transforming Growth Factors / physiology


  • AREG protein, human
  • Amphiregulin
  • Areg protein, mouse
  • EGF Family of Proteins
  • Glycoproteins
  • Growth Substances
  • Intercellular Signaling Peptides and Proteins
  • Epidermal Growth Factor
  • Keratins
  • Transforming Growth Factors
  • ErbB Receptors