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Vascular endothelial growth factor B

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
VEGFB
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2C7W,2VWE,2XAC

Identifiers
AliasesVEGFB, VEGFL, VRF, vascular endothelial growth factor B
External IDsOMIM:601398;MGI:106199;HomoloGene:87131;GeneCards:VEGFB;OMA:VEGFB - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for VEGFB
Genomic location for VEGFB
Band11q13.1Start64,234,584bp[1]
End64,239,264bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for VEGFB
Genomic location for VEGFB
Band19|19 AStart6,959,841bp[2]
End6,965,019bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • apex of heart

  • right auricle of heart

  • right coronary artery

  • left coronary artery

  • popliteal artery

  • tibial arteries

  • Descending thoracic aorta

  • ascending aorta

  • muscle of thigh

  • muscle layer of sigmoid colon
Top expressed in
  • myocardium

  • myocardium of ventricle

  • right ventricle

  • interventricular septum

  • cardiac muscles

  • muscle of thigh

  • extraocular muscle

  • cardiac muscle tissue of left ventricle

  • digastric muscle

  • plantaris muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7423

22340

Ensembl

ENSG00000173511

ENSMUSG00000024962

UniProt

P49765

P49766

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 MbChr 19: 6.96 – 6.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vascular endothelial growth factor B also known asVEGF-B is aprotein that, in humans, is encoded by theVEGF-Bgene.[5] VEGF-B is agrowth factor that belongs to thevascular endothelial growth factor family, of whichVEGF-A is the best-known member.

Function

[edit]

In contrast toVEGF-A, VEGF-B plays a less pronounced role in the vascular system: Whereas VEGF-A is important for the formation ofblood 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 theretina[7] and thecerebral cortex duringstroke,[8] and ofmotor neurons duringmotor neuron diseases such asamyotrophic lateral sclerosis.[9]

VEGF-B exerts its effects via theFLT1 receptor.[10] But the role ofco-receptorNRP in VEGF-B-mediated effects is still unclear.[11]

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

Interactions

[edit]

Vascular endothelial growth factor B has been shown tointeract withFLT1,NRP1 andNRP2.[14][15][16][17]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000173511Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000024962Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^"Entrez Gene: VEGFB vascular endothelial growth factor B".
  6. ^Zhang F, Tang Z, Hou X, Lennartsson J, Li Y, Koch AW, et al. (April 2009)."VEGF-B is dispensable for blood vessel growth but critical for their survival, and VEGF-B targeting inhibits pathological angiogenesis".Proceedings of the National Academy of Sciences of the United States of America.106 (15):6152–6157.Bibcode:2009PNAS..106.6152Z.doi:10.1073/pnas.0813061106.PMC 2669337.PMID 19369214.
  7. ^Li Y, Zhang F, Nagai N, Tang Z, Zhang S, Scotney P, et al. (March 2008)."VEGF-B inhibits apoptosis via VEGFR-1-mediated suppression of the expression of BH3-only protein genes in mice and rats".The Journal of Clinical Investigation.118 (3):913–923.doi:10.1172/JCI33673.PMC 2230661.PMID 18259607.
  8. ^Sun Y, Jin K, Childs JT, Xie L, Mao XO, Greenberg DA (October 2004)."Increased severity of cerebral ischemic injury in vascular endothelial growth factor-B-deficient mice".Journal of Cerebral Blood Flow and Metabolism.24 (10):1146–1152.doi:10.1097/01.wcb.0000134477.38980.38.PMID 15529014.
  9. ^Poesen K, Lambrechts D, Van Damme P, Dhondt J, Bender F, Frank N, et al. (October 2008)."Novel role for vascular endothelial growth factor (VEGF) receptor-1 and its ligand VEGF-B in motor neuron degeneration".The Journal of Neuroscience.28 (42):10451–10459.doi:10.1523/JNEUROSCI.1092-08.2008.PMC 6671326.PMID 18923022.
  10. ^Yamazaki Y, Morita T (November 2006). "Molecular and functional diversity of vascular endothelial growth factors".Molecular Diversity.10 (4):515–527.doi:10.1007/s11030-006-9027-3.PMID 16972015.S2CID 28692204.
  11. ^Mallick R, Ylä-Herttuala S (December 2022)."Therapeutic Potential of VEGF-B in Coronary Heart Disease and Heart Failure: Dream or Vision?".Cells.11 (24): 4134.doi:10.3390/cells11244134.PMC 9776740.PMID 36552897.
  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.Bibcode:2012Natur.490..426H.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.Bibcode:1998PNAS...9511709O.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.
  16. ^Mallick R, Ylä-Herttuala S (December 2022)."Therapeutic Potential of VEGF-B in Coronary Heart Disease and Heart Failure: Dream or Vision?".Cells.11 (24): 4134.doi:10.3390/cells11244134.PMC 9776740.PMID 36552897.
  17. ^Mallick R, Gurzeler E, Toivanen PI, Nieminen T, Ylä-Herttuala S (2022-08-04)."Novel Designed Proteolytically Resistant VEGF-B186R127S Promotes Angiogenesis in Mouse Heart by Recruiting Endothelial Progenitor Cells".Frontiers in Bioengineering and Biotechnology.10 907538.doi:10.3389/fbioe.2022.907538.PMC 9385986.PMID 35992336.

Further reading

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External links

[edit]
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Vascular endothelial growth factor B
PDB gallery
  • 2c7w: CRYSTAL STRUCTURE OF HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR-B: IDENTIFICATION OF AMINO ACIDS IMPORTANT FOR ANGIOGENINC ACTIVITY
    2c7w: CRYSTAL STRUCTURE OF HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR-B: IDENTIFICATION OF AMINO ACIDS IMPORTANT FOR ANGIOGENINC ACTIVITY
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