VEGFA,B,PLGF bind to VEGFR1 leading to receptor dimerization

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).

VEGFR-1与VEGF-A、VEGF-B及PLGF同源二聚体结合。此相互作用对于正常的血管生成和造血过程至关重要，尽管从结合至生理后果的众多分子步骤尚不明确（Hickins和Ellis，2005）。VEGFR-1由1338个氨基酸残基组成，并包含三个区域：一个由7个免疫球蛋白样结构域组成的细胞外区域、一个跨膜（TM）结构域以及一个细胞质酪氨酸激酶（TK）结构域。可变剪接形式的可溶性VEGFR-1（sVEGFR1）亦能与VEGF蛋白结合，并在体内可能起到下调膜结合受体VEGF激活的作用。sVEGFR1（VEGF121）的过表达与妊娠期的主要并发症——子痫前期相关（Shibuya和Claesson-Welsh，2006；Levine等，2004）。