Biology:VEGFR1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

Function

FLT1 is a member of VEGF receptor gene family. It encodes a receptor tyrosine kinase which is activated by VEGF-A, VEGF-B, and placental growth factor. The sequence structure of the FLT1 gene resembles that of the FMS (now CSF1R) gene; hence, Yoshida et al. (1987) proposed the name FLT as an acronym for FMS-like tyrosine kinase.[2]

The ablation of VEGFR1 by chemical and genetic means has also recently been found to augment the conversion of white adipose tissue to brown adipose tissue as well as increase brown adipose angiogenesis in mice.[3]

Functional genetic variation in FLT1 (rs9582036) has been found to affect non-small cell lung cancer survival.[4]

Interactions

FLT1 has been shown to interact with PLCG1[5] and vascular endothelial growth factor B (VEGF-B).[6][7]

See also

  • VEGF receptors

References

  1. "Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family". Oncogene 5 (4): 519–24. April 1990. PMID 2158038. 
  2. "FLT1 fms related receptor tyrosine kinase 1 [ Homo sapiens (human) "]. National Center for Biotechnology Information. https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2321. 
  3. "Ablation of endothelial VEGFR1 improves metabolic dysfunction by inducing adipose tissue browning". The Journal of Experimental Medicine 215 (2): 611–626. February 2018. doi:10.1084/jem.20171012. PMID 29305395. 
  4. "Functional FLT1 Genetic Variation is a Prognostic Factor for Recurrence in Stage I-III Non-Small-Cell Lung Cancer". Journal of Thoracic Oncology 10 (7): 1067–75. July 2015. doi:10.1097/JTO.0000000000000549. PMID 26134224. 
  5. "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites". Biochemical and Biophysical Research Communications 240 (3): 635–9. November 1997. doi:10.1006/bbrc.1997.7719. PMID 9398617. 
  6. "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): 11709–14. September 1998. doi:10.1073/pnas.95.20.11709. PMID 9751730. 
  7. "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". The Journal of Biological Chemistry 274 (30): 21217–22. July 1999. doi:10.1074/jbc.274.30.21217. PMID 10409677. 

Further reading