描述：
Epidermal growth factor (EGF) is the founding member of the EGF family that also includes
TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparinbinding EGFlike 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 1217 amino acid (aa) mouse 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 mouse EGF shares 70% and 77% aa sequence identity with mature human 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 homoor
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
TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparinbinding EGFlike 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 1217 amino acid (aa) mouse 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 mouse EGF shares 70% and 77% aa sequence identity with mature human 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 homoor
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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