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 two sets of
alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length.
VEGF 165 appears to be the most abundant and potent of the angiogenic isoform set,
followed by VEGF121 and VEGF189. The antiangiogenic or “b” set of isoforms is differentially
spliced to contain six alternate amino acids at the C-terminus, and are the more highly
expressed isoforms in normal adult tissue. VEGF 165b, like VEGF 121 but unlike most angiogenic
isoforms, does not bind heparins and is therefore diffusible. Human VEGF 165b 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 165b, respectively. VEGFs bind 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. The affinity of VEGF 165b for VEGF R2
is similar to that of VEGF165, but VEGF 165b only partially activates VEGF R2 such that the
kinase regulatory site Y1054 is not phosphorylated. VEGF 165b also does not bind neuropilin-1,
suggesting that the functional difference between VEGF 165 and VEGF 165b maybe due to
either the lack of neuropilin-1 co-signaling or unique downstream signaling activated by VEGF
165b. Since VEGF 165b may compete with angiogenic VEGFs for VEGF R2 sites, its ectopic
expression in tumors has been shown to inhibit their growth.
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 two sets of
alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length.
VEGF 165 appears to be the most abundant and potent of the angiogenic isoform set,
followed by VEGF121 and VEGF189. The antiangiogenic or “b” set of isoforms is differentially
spliced to contain six alternate amino acids at the C-terminus, and are the more highly
expressed isoforms in normal adult tissue. VEGF 165b, like VEGF 121 but unlike most angiogenic
isoforms, does not bind heparins and is therefore diffusible. Human VEGF 165b 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 165b, respectively. VEGFs bind 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. The affinity of VEGF 165b for VEGF R2
is similar to that of VEGF165, but VEGF 165b only partially activates VEGF R2 such that the
kinase regulatory site Y1054 is not phosphorylated. VEGF 165b also does not bind neuropilin-1,
suggesting that the functional difference between VEGF 165 and VEGF 165b maybe due to
either the lack of neuropilin-1 co-signaling or unique downstream signaling activated by VEGF
165b. Since VEGF 165b may compete with angiogenic VEGFs for VEGF R2 sites, its ectopic
expression in tumors has been shown to inhibit their growth.
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