Figure 3
From: VEGF-A splice variants bind VEGFRs with differential affinities
SPR sensograms for VEGFA165a, -A121, and -A165b binding VEGFR1 and VEGFR2. (A) Kinetic response curve of VEGFA165a–VEGFR1 and (D) VEGFR2 binding confirmed previous high affinity measurements to both receptors. (B) Both VEGFA121 and the anti-angiogenic VEGFA165b variants bind VEGFR1 with affinities 3 orders of magnitude weaker than VEGFA165a. (E) VEGFA121 binds VEGFR2 with the weakest affinity, and (F) the anti-angiogenic VEGFA165b binds VEGFR2 with a strong affinity that could displace the angiogenic form. Receptors were immobilized on BIAcore CM5 sensors. All kinetic studies were obtained by simultaneously injecting ligand across VEGFR1, VEGFR2, and Angiopoietin-4, a non-VEGFA binding protein used for reference subtraction. The following curves were obtained by subtracting this reference signal from the raw receptor-ligand interaction curve, removing signals associated with non-specific interactions.
