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 cystine 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 VEGF121 and VEGF189. Isoforms other
than VEGF121 contain basic heparinbinding regions and are not freely diffusible. Human
VEGF 165 shares 88% aa sequence identity with corresponding regions of mouse and rat, 96%
with porcine, 95% with canine, and 93% with feline, equine and bovine 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.
VEGF 165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation
with VEGF R2. 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 cystine 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 VEGF121 and VEGF189. Isoforms other
than VEGF121 contain basic heparinbinding regions and are not freely diffusible. Human
VEGF 165 shares 88% aa sequence identity with corresponding regions of mouse and rat, 96%
with porcine, 95% with canine, and 93% with feline, equine and bovine 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.
VEGF 165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation
with VEGF R2. 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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