Fig. 2

Schematic representation of alternative splicing variants and proteolytic processing of vascular endothelial growth factors (VEGFs). a VEGF-A isoforms generated by alternative splicing including VEGF-A111, VEGF-A121, VEGF-A145, VEGF-A165, VEGF-A183, VEGF-A189, VEGF-A206, and VEGF165b. Each isoform is represented by its exon composition, highlighting the variations in exons 6A, 6B, 7, and 8 across the isoforms contributing to differences in receptor-binding affinities and functional properties. b Alternative splicing generates two VEGF-B isoforms, VEGF-B167 and VEGF-B186. These isoforms differ in their use of either exon 6A or 6B, which determines their specific molecular characteristics. c VEGF-C and VEGF-D exist in unprocessed dimerized forms, and their proteolytic processing occurs through cleavage by the protein convertases, kallikrein 3 (KLK3), cathepsin D (CTSD), or thrombin, resulting in mature, active forms with modified functional properties. Created in BioRendender.com