描述：
Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability
factor (VPF), 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 and a cysteine knot structure. Humans express alternately
spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length. VEGF165
appears to be the most abundant and potent isoform, followed by VEGF 121 and VEGF 189.
VEGF 121 is the only form that lacks a basic heparin-binding region and is freely diffusible.
Mouse embryos expressing only the corresponding isoform (VEGF 120) do not survive to
term, and show defects in skeletogenesis. Human VEGF 121shares 87% aa sequence identity
with corresponding regions of mouse and rat, 93% with feline, equine and bovine, and 91%,
95% and 96% with ovine, canine and porcine VEGF, respectively. VEGF binds the type I
transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR)
on endothelial cells. Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears
to be the primary mediator of VEGF angiogenic activity. VEGF165 binds the semaphorin
receptor, Neuropilin-1; VEGF 121 binding has also been reported. VEGF is required during
embryogenesis to regulate the proliferation, migration, and survival of endothelial cells. In
adults, VEGF functions mainly in wound healing and the female reproductive cycle.
Pathologically, it is involved in tumor angiogenesis and vascular leakage. Circulating VEGF
levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis,
multiple sclerosis and systemic lupus erythematosus. VEGF is induced by hypoxia and
cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-α.
原厂资料：
Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability
factor (VPF), 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 and a cysteine knot structure. Humans express alternately
spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length. VEGF165
appears to be the most abundant and potent isoform, followed by VEGF 121 and VEGF 189.
VEGF 121 is the only form that lacks a basic heparin-binding region and is freely diffusible.
Mouse embryos expressing only the corresponding isoform (VEGF 120) do not survive to
term, and show defects in skeletogenesis. Human VEGF 121shares 87% aa sequence identity
with corresponding regions of mouse and rat, 93% with feline, equine and bovine, and 91%,
95% and 96% with ovine, canine and porcine VEGF, respectively. VEGF binds the type I
transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR)
on endothelial cells. Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears
to be the primary mediator of VEGF angiogenic activity. VEGF165 binds the semaphorin
receptor, Neuropilin-1; VEGF 121 binding has also been reported. VEGF is required during
embryogenesis to regulate the proliferation, migration, and survival of endothelial cells. In
adults, VEGF functions mainly in wound healing and the female reproductive cycle.
Pathologically, it is involved in tumor angiogenesis and vascular leakage. Circulating VEGF
levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis,
multiple sclerosis and systemic lupus erythematosus. VEGF is induced by hypoxia and
cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-α.
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