描述：
Epidermal growth factor (EGF) is the founding member of the EGF family that also includes
TGF-α, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth
factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through 6. Members of the EGF family
share a structural motif, the EGF-like domain, which is characterized by three intramolecular
disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF
family members are synthesized as type I transmembrane precursor proteins that may contain
several EGF domains in the extracellular region. The mature proteins are released from the cell
surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains
nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is
generated by proteolytic excision of the EGF domain proximal to the transmembrane region.
Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is
present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic
juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases
including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members.
These receptors undergo a complex pattern of ligand induced homo or heterodimerization to
transduce EGF family signals. EGF binds ErbB1 and depending on the context, induces the
formation of homodimers or heterodimers containing ErbB2. Dimerization results in
autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a
variety of signaling molecules. Biological activities ascribed to EGF include epithelial development,
angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation
of epidermal cells in culture.
原厂资料：
Epidermal growth factor (EGF) is the founding member of the EGF family that also includes
TGF-α, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth
factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through 6. Members of the EGF family
share a structural motif, the EGF-like domain, which is characterized by three intramolecular
disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF
family members are synthesized as type I transmembrane precursor proteins that may contain
several EGF domains in the extracellular region. The mature proteins are released from the cell
surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains
nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is
generated by proteolytic excision of the EGF domain proximal to the transmembrane region.
Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is
present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic
juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases
including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members.
These receptors undergo a complex pattern of ligand induced homo or heterodimerization to
transduce EGF family signals. EGF binds ErbB1 and depending on the context, induces the
formation of homodimers or heterodimers containing ErbB2. Dimerization results in
autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a
variety of signaling molecules. Biological activities ascribed to EGF include epithelial development,
angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation
of epidermal cells in culture.
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