Vascular endothelial growth factor B

Last updated
VEGFB
Protein VEGFB PDB 2c7w.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases VEGFB , VEGFL, VRF, vascular endothelial growth factor B
External IDs OMIM: 601398 MGI: 106199 HomoloGene: 87131 GeneCards: VEGFB
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003377
NM_001243733

NM_001185164
NM_011697

RefSeq (protein)

NP_001230662
NP_003368

NP_001172093
NP_035827

Location (UCSC) Chr 11: 64.23 – 64.24 Mb Chr 19: 6.96 – 6.97 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Vascular endothelial growth factor B also known as VEGF-B is a protein that, in humans, is encoded by the VEGF-B gene. [5] VEGF-B is a growth factor that belongs to the vascular endothelial growth factor family, of which VEGF-A is the best-known member.

Contents

Function

In contrast to VEGF-A, VEGF-B plays a less pronounced role in the vascular system: Whereas VEGF-A is important for the formation of blood vessels, such as during development or in pathological conditions, VEGF-B seems to play a role only in the maintenance of newly formed blood vessels during pathological conditions. [6] VEGF-B plays also an important role on several types of neurons. It is important for the protection of neurons in the retina [7] and the cerebral cortex during stroke, [8] and of motor neurons during motor neuron diseases such as amyotrophic lateral sclerosis. [9]

VEGF-B exerts its effects via the FLT1 receptor. [10] But the role of co-receptor NRP in VEGF-B-mediated effects is still unclear. [11]

VEGF-B has also been found to control endothelial uptake and transport of fatty acids in heart and skeletal muscle. [12] [13]

Interactions

Vascular endothelial growth factor B has been shown to interact with FLT1, NRP1 and NRP2. [14] [15] [16] [17]

Related Research Articles

<span class="mw-page-title-main">Angiogenesis</span> Blood vessel formation, when new vessels emerge from existing vessels

Angiogenesis is the physiological process through which new blood vessels form from pre-existing vessels, formed in the earlier stage of vasculogenesis. Angiogenesis continues the growth of the vasculature by processes of sprouting and splitting. Vasculogenesis is the embryonic formation of endothelial cells from mesoderm cell precursors, and from neovascularization, although discussions are not always precise. The first vessels in the developing embryo form through vasculogenesis, after which angiogenesis is responsible for most, if not all, blood vessel growth during development and in disease.

<span class="mw-page-title-main">Platelet-derived growth factor</span> Signaling glycoprotein regulating cell proliferation

Platelet-derived growth factor (PDGF) is one among numerous growth factors that regulate cell growth and division. In particular, PDGF plays a significant role in blood vessel formation, the growth of blood vessels from already-existing blood vessel tissue, mitogenesis, i.e. proliferation, of mesenchymal cells such as fibroblasts, osteoblasts, tenocytes, vascular smooth muscle cells and mesenchymal stem cells as well as chemotaxis, the directed migration, of mesenchymal cells. Platelet-derived growth factor is a dimeric glycoprotein that can be composed of two A subunits (PDGF-AA), two B subunits (PDGF-BB), or one of each (PDGF-AB).

Vascular endothelial growth factor, originally known as vascular permeability factor (VPF), is a signal protein produced by many cells that stimulates the formation of blood vessels. To be specific, VEGF is a sub-family of growth factors, the platelet-derived growth factor family of cystine-knot growth factors. They are important signaling proteins involved in both vasculogenesis and angiogenesis.

An angiogenesis inhibitor is a substance that inhibits the growth of new blood vessels (angiogenesis). Some angiogenesis inhibitors are endogenous and a normal part of the body's control and others are obtained exogenously through pharmaceutical drugs or diet.

<span class="mw-page-title-main">Angiopoietin</span> Protein family

Angiopoietin is part of a family of vascular growth factors that play a role in embryonic and postnatal angiogenesis. Angiopoietin signaling most directly corresponds with angiogenesis, the process by which new arteries and veins form from preexisting blood vessels. Angiogenesis proceeds through sprouting, endothelial cell migration, proliferation, and vessel destabilization and stabilization. They are responsible for assembling and disassembling the endothelial lining of blood vessels. Angiopoietin cytokines are involved with controlling microvascular permeability, vasodilation, and vasoconstriction by signaling smooth muscle cells surrounding vessels. There are now four identified angiopoietins: ANGPT1, ANGPT2, ANGPTL3, ANGPT4.

<span class="mw-page-title-main">Neuropilin</span>

Neuropilin is a protein receptor active in neurons.

<span class="mw-page-title-main">VEGF receptor</span> Protein family

VEGF receptors are receptors for vascular endothelial growth factor (VEGF). There are three main subtypes of VEGFR, numbered 1, 2 and 3. Also, they may be membrane-bound (mbVEGFR) or soluble (sVEGFR), depending on alternative splicing.

<span class="mw-page-title-main">VEGFR1</span> Protein-coding gene in the species Homo sapiens

Vascular endothelial growth factor receptor 1 is a protein that in humans is encoded by the FLT1 gene.

<span class="mw-page-title-main">Kinase insert domain receptor</span> Protein-coding gene in the species Homo sapiens

Kinase insert domain receptor also known as vascular endothelial growth factor receptor 2 (VEGFR-2) is a VEGF receptor. KDR is the human gene encoding it. KDR has also been designated as CD309. KDR is also known as Flk1.

<span class="mw-page-title-main">Neuropilin 2</span> Protein-coding gene in the species Homo sapiens

Neuropilin 2 (NRP2) is a protein that in humans is encoded by the NRP2 gene.

<span class="mw-page-title-main">Vascular endothelial growth factor C</span> Growth factor protein found in humans

Vascular endothelial growth factor C (VEGF-C) is a protein that is a member of the platelet-derived growth factor / vascular endothelial growth factor (PDGF/VEGF) family. It is encoded in humans by the VEGFC gene, which is located on chromosome 4q34.

<span class="mw-page-title-main">Neuropilin 1</span> Protein-coding gene in the species Homo sapiens

Neuropilin-1 is a protein that in humans is encoded by the NRP1 gene. In humans, the neuropilin 1 gene is located at 10p11.22. This is one of two human neuropilins.

<span class="mw-page-title-main">PEDF</span> Protein-coding gene in the species Homo sapiens

Pigment epithelium-derived factor (PEDF) also known as serpin F1 (SERPINF1), is a multifunctional secreted protein that has anti-angiogenic, anti-tumorigenic, and neurotrophic functions. Found in vertebrates, this 50 kDa protein is being researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer. In humans, pigment epithelium-derived factor is encoded by the SERPINF1 gene.

<span class="mw-page-title-main">Placental growth factor</span> Protein-coding gene in the species Homo sapiens

Placental growth factor(PlGF) is a protein that in humans is encoded by the PGF gene.

<span class="mw-page-title-main">C-fos-induced growth factor</span> Mammalian protein found in Homo sapiens

C-fos-induced growth factor (FIGF) is a vascular endothelial growth factor that in humans is encoded by the FIGF gene.

<span class="mw-page-title-main">Vascular endothelial growth factor A</span> Protein involved in blood vessel growth

Vascular endothelial growth factor A (VEGF-A) is a protein that in humans is encoded by the VEGFA gene.

<span class="mw-page-title-main">FLT4</span> Protein-coding gene in the species Homo sapiens

Fms-related tyrosine kinase 4, also known as FLT4, is a protein which in humans is encoded by the FLT4 gene.

Angiogenesis is the process of forming new blood vessels from existing blood vessels, formed in vasculogenesis. It is a highly complex process involving extensive interplay between cells, soluble factors, and the extracellular matrix (ECM). Angiogenesis is critical during normal physiological development, but it also occurs in adults during inflammation, wound healing, ischemia, and in pathological conditions such as rheumatoid arthritis, hemangioma, and tumor growth. Proteolysis has been indicated as one of the first and most sustained activities involved in the formation of new blood vessels. Numerous proteases including matrix metalloproteinases (MMPs), a disintegrin and metalloproteinase domain (ADAM), a disintegrin and metalloproteinase domain with throbospondin motifs (ADAMTS), and cysteine and serine proteases are involved in angiogenesis. This article focuses on the important and diverse roles that these proteases play in the regulation of angiogenesis.

<span class="mw-page-title-main">Kari Alitalo</span> Finnish MD and a medical researcher

Kari Kustaa Alitalo is a Finnish MD and a medical researcher. He is a foreign associated member of the National Academy of Sciences of the US. He became famous for his discoveries of several receptor tyrosine kinases (RTKs) and the first growth factor capable of inducing lymphangiogenesis: vascular endothelial growth factor C (VEGF-C). In the years 1996–2007 he was Europe's second most cited author in the field of cell biology. Alitalo is currently serving as an Academy Professor for the Academy of Finland.

Neuroangiogenesis is the coordinated growth of nerves and blood vessels. The nervous and blood vessel systems share guidance cues and cell-surface receptors allowing for this synchronised growth. The term neuroangiogenesis only came into use in 2002 and the process was previously known as neurovascular patterning. The combination of neurogenesis and angiogenesis is an essential part of embryonic development and early life. It is thought to have a role in pathologies such as endometriosis, brain tumors, and Alzheimer's disease.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000173511 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024962 - Ensembl, May 2017
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  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  12. Muoio DM (July 2010). "Metabolism and vascular fatty acid transport". The New England Journal of Medicine. 363 (3): 291–293. doi:10.1056/NEJMcibr1005397. PMID   20647206.
  13. Hagberg CE, Mehlem A, Falkevall A, Muhl L, Fam BC, Ortsäter H, et al. (October 2012). "Targeting VEGF-B as a novel treatment for insulin resistance and type 2 diabetes". Nature. 490 (7420): 426–430. doi:10.1038/nature11464. PMID   23023133. S2CID   4315297.
  14. Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, et al. (September 1998). "Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells". Proceedings of the National Academy of Sciences of the United States of America. 95 (20): 11709–11714. doi: 10.1073/pnas.95.20.11709 . PMC   21705 . PMID   9751730.
  15. Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, et al. (July 1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". The Journal of Biological Chemistry. 274 (30): 21217–21222. doi: 10.1074/jbc.274.30.21217 . PMID   10409677.
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Further reading