VEGFR1 VEGF-A,B,PLGF bind to VEGFR1 leading to receptor dimerization Authored: Krupa, S, Gopinathrao, G, 2007-03-08 22:07:59 Edited: Gopinathrao, G, 2007-04-08 21:14:18 Pubmed11387210 Pubmed12871269 Pubmed14764923 Pubmed15585754 Pubmed16336962 Pubmed2479986 Pubmed8637916 Pubmed9207067 Pubmed9722576 Reactome Database ID Release 43194311 Reactome, http://www.reactome.org ReactomeREACT_12556 Reviewed: Claesson-Welsh, L, 2008-02-28 00:15:17 VEGFR-1 binds VEGF-A, VEGF-B, and PLGF homodimers. This interaction is required for normal angiogenesis and hematopoiesis, although many of the detailed molecular steps from binding to these physiological consequences remain unclear (Hickins and Ellis, 2005). VEGFR-1 is made up of 1338 aa and has three regions: an extracellular region consisting of 7 immunoglobin-like domains, a transmembrane (TM) domain and a cytosolic tyrosine kinase (TK) domain. An alternatively spliced form, soluble VEGFR-1 (sVEGFR1), also binds VEGF proteins and may serve in the body to down-regulate VEGF activation of membrane-bound receptors. Overexpression of sVEGFR1 (VEGF121) is associated with preeclampsia, a major disorder of pregnancy (Shibuya and Claesson-Welsh 2006; Levine et al. 2004). has a Stoichiometric coefficient of 2 VEGFA,B,PLGF