Vascular endothelial growth factor B

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Vascular endothelial growth factor B
Protein VEGFB PDB 2c7w.png
PDB rendering based on 2c7w.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM601398 MGI106199 HomoloGene87131 GeneCards: VEGFB Gene
RNA expression pattern
PBB GE VEGFB 203683 s at tn.png
More reference expression data
Species Human Mouse
Entrez 7423 22340
Ensembl ENSG00000173511 ENSMUSG00000024962
UniProt P49765 P49766
RefSeq (mRNA) NM_001243733 NM_001185164
RefSeq (protein) NP_001230662 NP_001172093
Location (UCSC) Chr 11:
64 – 64.01 Mb
Chr 19:
6.98 – 6.99 Mb
PubMed search [1] [2]

Vascular endothelial growth factor B also known as VEGF-B is a protein that, in humans, is encoded by the VEGF-B gene.[1] VEGF-B is a growth factor that belongs to the vascular endothelial growth factor family, of which VEGF-A is the best-known member.


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.[2] VEGF-B plays also an important role on several types of neurons. It is important for the protection of neurons in the retina[3] and the cerebral cortex during stroke [4] and of motoneurons during motor neuron diseases such as amyotrophic lateral sclerosis.[5]

VEGF-B exerts its effects via the FLT1 receptor.[6]

VEGF-B has also been found to control endothelial uptake and transport of fatty acids in heart and skeletal muscle.[7][8]


Vascular endothelial growth factor B has been shown to interact with FLT1.[9][10]


  1. ^ "Entrez Gene: VEGFB vascular endothelial growth factor B". 
  2. ^ Zhang F, Tang Z, Hou X, Lennartsson J, Li Y, Koch AW, Scotney P, Lee C, Arjunan P, Dong L, Kumar A, Rissanen TT, Wang B, Nagai N, Fons P, Fariss R, Zhang Y, Wawrousek E, Tansey G, Raber J, Fong GH, Ding H, Greenberg DA, Becker KG, Herbert JM, Nash A, Yla-Herttuala S, Cao Y, Watts RJ, Li X (April 2009). "VEGF-B is dispensable for blood vessel growth but critical for their survival, and VEGF-B targeting inhibits pathological angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 106 (15): 6152–7. doi:10.1073/pnas.0813061106. PMC 2669337. PMID 19369214. 
  3. ^ Li Y, Zhang F, Nagai N, Tang Z, Zhang S, Scotney P, Lennartsson J, Zhu C, Qu Y, Fang C, Hua J, Matsuo O, Fong GH, Ding H, Cao Y, Becker KG, Nash A, Heldin CH, Li X (March 2008). "VEGF-B inhibits apoptosis via VEGFR-1-mediated suppression of the expression of BH3-only protein genes in mice and rats". J. Clin. Invest. 118 (3): 913–23. doi:10.1172/JCI33673. PMC 2230661. PMID 18259607. 
  4. ^ 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". J. Cereb. Blood Flow Metab. 24 (10): 1146–52. doi:10.1097/01.wcb.0000134477.38980.38. PMID 15529014. 
  5. ^ Poesen K, Lambrechts D, Van Damme P, Dhondt J, Bender F, Frank N, Bogaert E, Claes B, Heylen L, Verheyen A, Raes K, Tjwa M, Eriksson U, Shibuya M, Nuydens R, Van Den Bosch L, Meert T, D'Hooge R, Sendtner M, Robberecht W, Carmeliet P (October 2008). "Novel role for vascular endothelial growth factor (VEGF) receptor-1 and its ligand VEGF-B in motor neuron degeneration". J. Neurosci. 28 (42): 10451–9. doi:10.1523/JNEUROSCI.1092-08.2008. PMID 18923022. 
  6. ^ Yamazaki Y, Morita T (November 2006). "Molecular and functional diversity of vascular endothelial growth factors". Mol. Divers. 10 (4): 515–27. doi:10.1007/s11030-006-9027-3. PMID 16972015. 
  7. ^ Muoio DM (July 2010). "Metabolism and vascular fatty acid transport". N. Engl. J. Med. 363 (3): 291–3. doi:10.1056/NEJMcibr1005397. PMID 20647206. 
  8. ^ Hagberg CE, Mehlem A, Falkevall A, Muhl L, Fam BC, Ortsäter H, Scotney P, Nyqvist D, Samén E, Lu L, Stone-Elander S, Proietto J, Andrikopoulos S, Sjöholm A, Nash A, Eriksson U (October 2012). "Targeting VEGF-B as a novel treatment for insulin resistance and type 2 diabetes". Nature 490 (7420): 426–30. doi:10.1038/nature11464. PMID 23023133. 
  9. ^ Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, Gunji Y, Jeltsch MM, Shibuya M, Alitalo K, Eriksson U (September 1998). "Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11709–14. doi:10.1073/pnas.95.20.11709. PMC 21705. PMID 9751730. 
  10. ^ Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K (July 1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". J. Biol. Chem. 274 (30): 21217–22. doi:10.1074/jbc.274.30.21217. PMID 10409677. 

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