Vascular endothelial growth factor B

{{Short description|Protein-coding gene in the species Homo sapiens}}

Vascular endothelial growth factor B also known as VEGF-B is a protein that, in humans, is encoded by the VEGF-B gene.{{cite web | title = Entrez Gene: VEGFB vascular endothelial growth factor B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7423}} 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

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.{{cite journal | vauthors = 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 | display-authors = 6 | title = VEGF-B is dispensable for blood vessel growth but critical for their survival, and VEGF-B targeting inhibits pathological angiogenesis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 15 | pages = 6152–6157 | date = April 2009 | pmid = 19369214 | pmc = 2669337 | doi = 10.1073/pnas.0813061106 | bibcode = 2009PNAS..106.6152Z | doi-access = free }}

VEGF-B plays also an important role on several types of neurons. It is important for the protection of neurons in the retina{{cite journal | vauthors = 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 | display-authors = 6 | title = VEGF-B inhibits apoptosis via VEGFR-1-mediated suppression of the expression of BH3-only protein genes in mice and rats | journal = The Journal of Clinical Investigation | volume = 118 | issue = 3 | pages = 913–923 | date = March 2008 | pmid = 18259607 | pmc = 2230661 | doi = 10.1172/JCI33673 }} and the cerebral cortex during stroke,{{cite journal | vauthors = Sun Y, Jin K, Childs JT, Xie L, Mao XO, Greenberg DA | title = Increased severity of cerebral ischemic injury in vascular endothelial growth factor-B-deficient mice | journal = Journal of Cerebral Blood Flow and Metabolism | volume = 24 | issue = 10 | pages = 1146–1152 | date = October 2004 | pmid = 15529014 | doi = 10.1097/01.wcb.0000134477.38980.38 | doi-access = free }} and of motor neurons during motor neuron diseases such as amyotrophic lateral sclerosis.{{cite journal | vauthors = 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 | display-authors = 6 | title = Novel role for vascular endothelial growth factor (VEGF) receptor-1 and its ligand VEGF-B in motor neuron degeneration | journal = The Journal of Neuroscience | volume = 28 | issue = 42 | pages = 10451–10459 | date = October 2008 | pmid = 18923022 | pmc = 6671326 | doi = 10.1523/JNEUROSCI.1092-08.2008 | doi-access = free }}

VEGF-B exerts its effects via the FLT1 receptor.{{cite journal | vauthors = Yamazaki Y, Morita T | title = Molecular and functional diversity of vascular endothelial growth factors | journal = Molecular Diversity | volume = 10 | issue = 4 | pages = 515–527 | date = November 2006 | pmid = 16972015 | doi = 10.1007/s11030-006-9027-3 | s2cid = 28692204 }} But the role of co-receptor NRP in VEGF-B-mediated effects is still unclear.{{cite journal | vauthors = Mallick R, Ylä-Herttuala S | title = Therapeutic Potential of VEGF-B in Coronary Heart Disease and Heart Failure: Dream or Vision? | journal = Cells | volume = 11 | issue = 24 | pages = 4134 | date = December 2022 | pmid = 36552897 | doi = 10.3390/cells11244134 | pmc = 9776740 | doi-access = free }}

VEGF-B has also been found to control endothelial uptake and transport of fatty acids in heart and skeletal muscle.{{cite journal | vauthors = Muoio DM |author-link1=Deborah Muoio| title = Metabolism and vascular fatty acid transport | journal = The New England Journal of Medicine | volume = 363 | issue = 3 | pages = 291–293 | date = July 2010 | pmid = 20647206 | doi = 10.1056/NEJMcibr1005397 }}{{cite journal | vauthors = 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 | display-authors = 6 | title = Targeting VEGF-B as a novel treatment for insulin resistance and type 2 diabetes | journal = Nature | volume = 490 | issue = 7420 | pages = 426–430 | date = October 2012 | pmid = 23023133 | doi = 10.1038/nature11464 | bibcode = 2012Natur.490..426H | s2cid = 4315297 }}

Interactions

Vascular endothelial growth factor B has been shown to interact with FLT1, NRP1 and NRP2.{{cite journal | vauthors = Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, Gunji Y, Jeltsch MM, Shibuya M, Alitalo K, Eriksson U | display-authors = 6 | title = Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 20 | pages = 11709–11714 | date = September 1998 | pmid = 9751730 | pmc = 21705 | doi = 10.1073/pnas.95.20.11709 | bibcode = 1998PNAS...9511709O | doi-access = free }}{{cite journal | vauthors = Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K | display-authors = 6 | title = Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 30 | pages = 21217–21222 | date = July 1999 | pmid = 10409677 | doi = 10.1074/jbc.274.30.21217 | doi-access = free }}{{cite journal | vauthors = Mallick R, Ylä-Herttuala S | title = Therapeutic Potential of VEGF-B in Coronary Heart Disease and Heart Failure: Dream or Vision? | journal = Cells | volume = 11 | issue = 24 | pages = 4134 | date = December 2022 | pmid = 36552897 | pmc = 9776740 | doi = 10.3390/cells11244134 | doi-access = free }}{{cite journal | vauthors = Mallick R, Gurzeler E, Toivanen PI, Nieminen T, Ylä-Herttuala S | title = Novel Designed Proteolytically Resistant VEGF-B186R127S Promotes Angiogenesis in Mouse Heart by Recruiting Endothelial Progenitor Cells | journal = Frontiers in Bioengineering and Biotechnology | volume = 10 | pages = 907538 | date = 2022-08-04 | pmid = 35992336 | pmc = 9385986 | doi = 10.3389/fbioe.2022.907538 | doi-access = free }}

References

External links

[https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P49765 PDBe-KB] provides an overview of all the structure information available in the PDB for Human Vascular endothelial growth factor B

Vascular endothelial growth factor B

Function

Interactions

References

Further reading

External links