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vascular endothelial growth factor C; VEGF-C; vascular endothelial growth factor-related protein; VRP; Flt4 ligand; Flt4-L (VEGFC)

Function: - growth factor active in angiogenesis, & endothelial cell growth - stimulates endothelial cell proliferation & migration - has effects on the permeability of blood vessels - may function in angiogenesis of the venous & lymphatic vascular systems during embryogenesis, & in the maintenance of differentiated lymphatic endothelium in adults - binds & activates VEGFR-2 receptor (Flk1) & VEGFR-3 receptor (Flt4) - macrophage secretion of VEGF-C is stimulated by NFAT5 (TonEBP) that is produced in response to hypertonic conditions [3] - undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed activates VEGFR-2 - forms an antiparallel homodimer linked by disulfide bonds - before secretion, a cleavage occurs between Arg-227 & Ser-228 producing an 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 Structure: - homodimer; non-covalent & antiparallel - belongs to the PDGF/VEGF growth factor family Compartment: secreted Expression: - spleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon & small intestine & fetal liver, lung & kidney, but not in peripheral blood lymphocyte Pathology: - defects in macrophage NFAT5-stimulated VEGF-C secretion may play a role in salt-sensitive hypertension

General

vascular endothelial growth factor family protein (VEGF family)

Properties

SIZE: entity length = 419 aa MW = 47 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-31} cysteine residue {C131} MODIFICATION: cysteine residue {C173} cysteine residue {C156} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C162} MODIFICATION: cysteine residue {C209} cysteine residue {C165} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C166} MODIFICATION: cysteine residue {C211} cysteine residue {C173} MODIFICATION: cysteine residue {C131} N-glycosylation site {N175} N-glycosylation site {N205} cysteine residue {C209} MODIFICATION: cysteine residue {C162} cysteine residue {C211} MODIFICATION: cysteine residue {C166} N-glycosylation site {N240} repeats {280-362} MOTIF: consensus repeat {280-295} consensus repeat {304-319} consensus repeat {328-343} consensus repeat {347-362}

Database Correlations

OMIM 601528 UniProt P49767 PFAM correlations Entrez Gene 7424 Kegg hsa:7424

References

  1. UniProt :accession P49767
  2. Entrez Gene :accession 7424
  3. Machnik A et al Macrophages regulate salt-dependent volume and blood pressure by a vascular endothelial growth factor-C dependent buffering mechanism. Nat Med 2009 May; 15:545 PMID: 19412173