描述：
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF)
and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and
adult. It is a member of the PDGF family that is characterized by the presence of eight
conserved cysteine residues. In human, at least eight alternate splice isoforms of VEGF-A,
ranging from 206 amino acids (aa) to 121 aa in length, are known. In zebrafish, two VEGF
isoforms, a 165 aa and a 121 aa isoform, have been reported. Mature zebrafish VEGF 165
shares 64%, 62% and 62% aa sequence identity with frog, human, and mouse VEGF 165
,respectively. There are two tyrosine kinase receptors for VEGF reported in mammals termed
VEGF R1 and VEGF R2/FLK-1. One receptor has been identified in zebrafish(FLK-1), and this
may actually represent the orthologue to the early common ancestor for mammalian VEGF
R1 and R2. All receptors are type I transmembrane proteins that show seven immunoglobulin
like domains extracellularly and a split kinase domain intracellularly. In addition to the tyrosine
kinase receptors, neuropilin-1 (NRP-1) has been reported to be a coreceptor for VEGF binding.
It is proposed that the presence of NRP-1 lowers the concentration of VEGF necessary for
activation of VEGF R2. NRP-1 has been reported in both zebrafish and human. VEGF regulates
multiple biological functions in endothelial cells, including cell proliferation, migration
and survival. These functions of VEGF are mediated partly through the induction of nitric oxide
and prostacyclin, as well as upregulation of metalloproteinases. Together with other vascular
specific growth factors such as the Angiopoietins, VEGF have separate but complementary roles
in angiogenesis and vasculogenesis.
原厂资料：
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF)
and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and
adult. It is a member of the PDGF family that is characterized by the presence of eight
conserved cysteine residues. In human, at least eight alternate splice isoforms of VEGF-A,
ranging from 206 amino acids (aa) to 121 aa in length, are known. In zebrafish, two VEGF
isoforms, a 165 aa and a 121 aa isoform, have been reported. Mature zebrafish VEGF 165
shares 64%, 62% and 62% aa sequence identity with frog, human, and mouse VEGF 165
,respectively. There are two tyrosine kinase receptors for VEGF reported in mammals termed
VEGF R1 and VEGF R2/FLK-1. One receptor has been identified in zebrafish(FLK-1), and this
may actually represent the orthologue to the early common ancestor for mammalian VEGF
R1 and R2. All receptors are type I transmembrane proteins that show seven immunoglobulin
like domains extracellularly and a split kinase domain intracellularly. In addition to the tyrosine
kinase receptors, neuropilin-1 (NRP-1) has been reported to be a coreceptor for VEGF binding.
It is proposed that the presence of NRP-1 lowers the concentration of VEGF necessary for
activation of VEGF R2. NRP-1 has been reported in both zebrafish and human. VEGF regulates
multiple biological functions in endothelial cells, including cell proliferation, migration
and survival. These functions of VEGF are mediated partly through the induction of nitric oxide
and prostacyclin, as well as upregulation of metalloproteinases. Together with other vascular
specific growth factors such as the Angiopoietins, VEGF have separate but complementary roles
in angiogenesis and vasculogenesis.
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