描述：
Vascular endothelial growth factor B (VEGF-B; also known as VFR) is a member of the
VEGFPDGF supergene family of growth factor molecules. Five mouse members have
been identified, including VEGF-A, -B, -C, -D, and PlGF. VEGF family members are
disulfidelinked homo and heterodimeric proteins that areimportant regulators of
vasculogenesis and lymphangiogenesis. Mouse VEGF-B has two isoforms, a 32 kDa
single chain and a 21 kDa single chain form. The long form (VEGF-B186) is 207 amino
acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form
(VEGF-B167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa mature segment.
Each mature isoform shows the same Nterminal 94 aa that contains a cysteine knot VEGF
homology domain. VEGF-B186is Oglycosylated; VEGF-B167 is not. VEGF-B167 binds heparin;
VEGF-B186 does not. Thus, VEGF-B186 is secreted and freely diffusible in tissues. However,
the VEGF-B167 isoform is the predominant form in tissue. Mouse VEGF-B186 is 93% and
87% aa identical to bovine and human VEGF-B186, respectively; mouse VEGF-B167 is 90%
and 88% aa identical to bovine and human VEGF-B167, respectively . The mouse VEGF-B167
homodimer is 42 kDa in size, while the VEGF-B186 homodimer is 62 kDa in size. Unlike
VEGF167, VEGF-B186 undergoes proteolytic processing that creates a partially processed 48
kDa homodimer and a fully processed 32 kDa homodimer. Processing appears to occur at
Arg127 of the mature form. Both forms of VEGF-B can heterodimerize with VEGF. Both VEGF-B
isoforms bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3. VEGF-B167
also binds neuropilin1, but only the 127 aa processed form of VEGF-B186 binds neuropilin1.
As a dimer, full length VEGF-B186 does not interact with neuropilin1, while any dimer that
contains the processed VEGF-B127 subunit will interact with neuropilin1. The importance of
differential neuropilin binding is unclear. VEGF-B deficient mice display an atrial conduction
deficit. On endothelial cells, ligation of VEGF R1 by VEGF-B has been shown to regulate the
expression and activity of urokinase type plasminogen activator and plasminogen activator inhibitor 1.
原厂资料：
Vascular endothelial growth factor B (VEGF-B; also known as VFR) is a member of the
VEGFPDGF supergene family of growth factor molecules. Five mouse members have
been identified, including VEGF-A, -B, -C, -D, and PlGF. VEGF family members are
disulfidelinked homo and heterodimeric proteins that areimportant regulators of
vasculogenesis and lymphangiogenesis. Mouse VEGF-B has two isoforms, a 32 kDa
single chain and a 21 kDa single chain form. The long form (VEGF-B186) is 207 amino
acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form
(VEGF-B167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa mature segment.
Each mature isoform shows the same Nterminal 94 aa that contains a cysteine knot VEGF
homology domain. VEGF-B186is Oglycosylated; VEGF-B167 is not. VEGF-B167 binds heparin;
VEGF-B186 does not. Thus, VEGF-B186 is secreted and freely diffusible in tissues. However,
the VEGF-B167 isoform is the predominant form in tissue. Mouse VEGF-B186 is 93% and
87% aa identical to bovine and human VEGF-B186, respectively; mouse VEGF-B167 is 90%
and 88% aa identical to bovine and human VEGF-B167, respectively . The mouse VEGF-B167
homodimer is 42 kDa in size, while the VEGF-B186 homodimer is 62 kDa in size. Unlike
VEGF167, VEGF-B186 undergoes proteolytic processing that creates a partially processed 48
kDa homodimer and a fully processed 32 kDa homodimer. Processing appears to occur at
Arg127 of the mature form. Both forms of VEGF-B can heterodimerize with VEGF. Both VEGF-B
isoforms bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3. VEGF-B167
also binds neuropilin1, but only the 127 aa processed form of VEGF-B186 binds neuropilin1.
As a dimer, full length VEGF-B186 does not interact with neuropilin1, while any dimer that
contains the processed VEGF-B127 subunit will interact with neuropilin1. The importance of
differential neuropilin binding is unclear. VEGF-B deficient mice display an atrial conduction
deficit. On endothelial cells, ligation of VEGF R1 by VEGF-B has been shown to regulate the
expression and activity of urokinase type plasminogen activator and plasminogen activator inhibitor 1.
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