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Vascular endothelial growth factor B

From Wikipedia, the free encyclopedia
VEGFB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesVEGFB, VEGFL, VRF, vascular endothelial growth factor B
External IDsOMIM: 601398; MGI: 106199; HomoloGene: 87131; GeneCards: VEGFB; OMA:VEGFB - orthologs
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 MbChr 19: 6.96 – 6.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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.

Function

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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

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

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000173511Ensembl, May 2017
  2. ^ a b c GRCm38: 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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  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Vascular endothelial growth factor B