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), 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 1133 amino acid (aa)
rat 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 rat EGF shares 70% and 77% aa sequence identity with
mature human and mouse EGF, respectively. 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 hetero-dimerization 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), 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 1133 amino acid (aa)
rat 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 rat EGF shares 70% and 77% aa sequence identity with
mature human and mouse EGF, respectively. 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 hetero-dimerization 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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