VEGFC

The protein encoded by this gene is a member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. The encoded protein promotes angiogenesis and endothelial cell growth, and can also affect the permeability of blood vessels. The proprotein is further cleaved into a fully processed form that can bind and activate VEGFR-2 and VEGFR-3 receptors.

Vascular Endothelial Growth Factor C

Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors.

Biological Process animal organ morphogenesis Source:Ensembl
Biological Process cellular response to leukemia inhibitory factor Source:Ensembl
Biological Process glial cell proliferation Source:Ensembl
Biological Process induction of positive chemotaxis Source:UniProtKB1 Publication
Biological Process morphogenesis of embryonic epithelium Source:Ensembl
Biological Process negative regulation of blood pressure Source:Ensembl
Biological Process negative regulation of osteoblast differentiation Source:Ensembl
Biological Process positive regulation of angiogenesis Source:GO_Central1 Publication
Biological Process positive regulation of blood vessel endothelial cell migration Source:Ensembl
Biological Process positive regulation of cell division Source:UniProtKB-KW
Biological Process positive regulation of cell population proliferation Source:ProtInc1 Publication
Biological Process positive regulation of endothelial cell proliferation Source:GO_Central1 Publication
Biological Process positive regulation of glial cell proliferation Source:Ensembl
Biological Process positive regulation of lymphangiogenesis Source:Ensembl
Biological Process positive regulation of mast cell chemotaxis Source:UniProtKB1 Publication
Biological Process positive regulation of mesenchymal stem cell proliferation Source:Ensembl
Biological Process positive regulation of neuroblast proliferation Source:Ensembl
Biological Process positive regulation of protein autophosphorylation Source:Ensembl
Biological Process positive regulation of protein kinase activity Source:Ensembl
Biological Process positive regulation of protein phosphorylation Source:GO_Central1 Publication
Biological Process positive regulation of protein secretion Source:Ensembl
Biological Process regulation of vascular endothelial growth factor receptor signaling pathway Source:Ensembl
Biological Process response to hypoxia Source:GO_Central1 Publication
Biological Process response to xenobiotic stimulus Source:Ensembl
Biological Process signal transduction Source:ProtInc1 Publication
Biological Process sprouting angiogenesis Source:GO_Central1 Publication
Biological Process substrate-dependent cell migration Source:ProtInc1 Publication
Biological Process vascular endothelial growth factor receptor signaling pathway Source:UniProtKB1 Publication
Biological Process vascular endothelial growth factor signaling pathway Source:GO_Central1 Publication

Secreted

Lymphatic malformation 4 (LMPHM4):
A form of primary lymphedema, a disease characterized by swelling of body parts due to developmental anomalies and functional defects of the lymphatic system. Patients with lymphedema may suffer from recurrent local infections. LMPHM4 is an autosomal dominant form with onset at birth or in early childhood. Affected individuals manifest lymphedema of lower limbs with prominent veins, and impaired lymphatic uptake and drainage. Additional features are nail dysplasia, skin hyperkeratosis and papillomatosis.

Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-227 and Ser-228 producing a heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions.