VEGFB, as known as VRF, is a member of the VEGF family of growth factors that share structural and functional similarity. By alternative splicing, two isoforms of mature VEGF-B containing 167 or 186 amino acid (aa) residues exist. VEGF-B is expressed in most tissues, especially in heart, skeletal muscle and pancreas. The two VEGF-B isoforms have identical amino-terminal cysteine-knot VEGF homology domains but the carboxyl end of VEGF-B167 differs from that of VEGF-B186 by the presence of a highly basic cysteine-rich heparin binding domain. VEGF-B167 and a proteolytically processed form of VEGF-B186 also bind neuropilin-1, a type I transmembrane receptor for semaphorins/collapsins, ligands involved in neuron guidance.
Vascular Endothelial Growth Factor (VEGF)-C is a member of the VEGF family, a group of polypeptide growth factors which play key roles in the physiology and pathology of many aspects of the cardiovascular system, including vasculogenesis, hematopoiesis, angiogenesis and vascular permeability. While VEGFC is homologous to other members of the VEGF/PDGF family, it contains the C-terminal propeptide which has an unusual structure with tandemly repeated cysteine-rich motifs. Upon biosynthesis, VEGFC is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGF signalling in endothelial cells occurs through three tyrosine kinase receptors (VEGFRs) expressed by endothelial cells and hematopoietic precursors, and VEGF-C is a ligand for two receptors, VEGFR-3 (Flt4), and VEGFR-2. It is indicated that VEGFC undergoes a complex proteolytic maturation generating a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGFC may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Knockout of the VEGF-C gene is embryonic lethal late in development, and although cells differentiate into the lymphatic lineage, they fail to sprout and form lymphatic vessels. Inactivation of a single VEGF-C allele results in the development of cutaneous lymphatic hypoplasia and lymphedema.
Vascular endothelial growth factor D (VEGF-D) is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. It is highly expressed in lung, heart, small intestine and fetal lung, and at lower levels in skeletal muscle, colon, and pancreas. VEGF-D is growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. It may function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. It undergoes a complex proteolytic maturation, generating multiple processed forms that bind and activate VEGFR-2 and VEGFR-3 receptors.
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family and often exists as a disulfide-linked homodimer. VEGF-A protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, inhibiting apoptosis and tumor growth. VEGF-A protein is also a vasodilator that increases microvascular permeability, thus it was originally referred to as vascular permeability factor.
Vascular endothelial growth factor receptor 1, also known as VEGFR-1, Fms-like tyrosine kinase 1, Tyrosine-protein kinase FRT, Tyrosine-protein kinase receptor FLT, Vascular permeability factor receptor and FLT1, is a single-pass type I membrane protein and secreted protein which belongs to theprotein kinase superfamily, Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR-1 / FLT1 contains sevenIg-like C2-type (immunoglobulin-like) domains and oneprotein kinase domain. VEGFR-1 / FLT1 is expressed mostly in normal lung, but also in placenta, liver, kidney, heart and brain tissues. It is specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. VEGFR-1 / FLT1 is not expressed in tumor cell lines. VEGFR-1 / FLT1 is an essential receptor tyrosine kinase that regulates mammalian vascular development and embryogenesis. EGF-induced angiogenesis requires inverse regulation of VEGFR-1 and VEGFR-2 in tumor-associated endothelial cells. VEGFR-1 / FLT1 is a receptor for VEGF, VEGFB and PGF. It has a tyrosine-protein kinase activity. The VEGF-kinase ligand/receptor signaling system plays a key role in vascular development and regulation of vascular permeability.
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