Characterization of the VEGF-D (Cys117Ala) N- and C-terminal variants. (A) Alignment of the human (h) and mouse (m) VEGF-D sequences. The amino acid residue differences are indicated. The N-terminal residues 89, 92, and 100 and the C-terminal residues 195 and 205 of the deletion variants of human VEGF-D are labeled. The residues visible in the crystal structure are colored in yellow and magenta. The residues colored in yellow are between the 2 proteolytic sites.¹⁷  (B) VEGFR-2/BaF and VEGFR-3/BaF cell survival induced with the VEGF-D variants. The variants are labeled according to the residue numbering. (C) Comparison of the wt VEGF-D short form (Dwt, residues 89-205 without the Cys117Ala mutation), VEGF-D D_89-195 and D_100-195 variant induced VEGFR-2 and VEGFR-3 phosphorylation in HDME cells. The VEGF-D concentrations (ng/mL) are indicated above the lanes. (D) Comparison of the wt VEGF-C short form (Cwt, residues 112-215),²³  VEGF-D D_89-195 and D_100-195 variant induced VEGFR-2 and VEGFR-3 phosphorylation in PAE–VEGFR-2 and PAE–VEGFR-3 cells, respectively. The concentrations (ng/mL) of growth factors are indicated above the lanes.