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. In human, at least eight alternately spliced isoforms of VEGF
ranging from 206 amino acids (aa) to 121 aa in length are known. Three isoforms, VEGF188
, VEGF182, and VEGF164, have been identified in canine. Canine VEGF164 shares 91%, 90%,
and 98% aa sequence identity with the rat, mouse, and feline homologs, respectively. Two
type I transmembrane receptor tyrosine kinases, VEGF R1 and VEGF R2, that bind VEGF with
high affinity, have been identified. Neuropilin-1, a receptor for semaphorin, also binds VEGF
and acts as a coreceptor to enhance the affinity between VEGF and VEGF R2. Neuropilin1
alone can also mediate VEGFinduced endothelial cell migration. VEGF regulates cell
Proliferation, migration, and survival of endothelial cells. These functions are partially
mediated through the induction of nitric oxide, prostacyclin, and metalloproteinases. Together
with angiopoietins or other vascularspecific growth factors, VEGF plays a separate but
complementary role in angiogenesis and vasculogenesis.
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. In human, at least eight alternately spliced isoforms of VEGF
ranging from 206 amino acids (aa) to 121 aa in length are known. Three isoforms, VEGF188
, VEGF182, and VEGF164, have been identified in canine. Canine VEGF164 shares 91%, 90%,
and 98% aa sequence identity with the rat, mouse, and feline homologs, respectively. Two
type I transmembrane receptor tyrosine kinases, VEGF R1 and VEGF R2, that bind VEGF with
high affinity, have been identified. Neuropilin-1, a receptor for semaphorin, also binds VEGF
and acts as a coreceptor to enhance the affinity between VEGF and VEGF R2. Neuropilin1
alone can also mediate VEGFinduced endothelial cell migration. VEGF regulates cell
Proliferation, migration, and survival of endothelial cells. These functions are partially
mediated through the induction of nitric oxide, prostacyclin, and metalloproteinases. Together
with angiopoietins or other vascularspecific growth factors, VEGF plays a separate but
complementary role in angiogenesis and vasculogenesis.