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. 2007 Apr-Jun;1(2):56–61. doi: 10.4161/cam.1.2.4490

Figure 2.

Figure 2

(A) Schematic view of the VEGF exon organization. Amino acid residues encoded by exons 3 and 4, respectively, are responsible for interaction with VEGFR-1 and VEGFR-2, respectively. Exons 6 and 7 represent the VEGF heparan sulphate proteoglycan (HSPG) binding domains. Exons 7 and 8 are involved in NRP binding. The asterisks represent the two major targets of therapeutics, (VEGFR-2 and NRP). (B) Strategies to inhibit VEGF165 signaling through VEGFR-2. These include VEGFR-2 kinase inhibitors (e.g., PTK787), soluble VEGFRs (e.g., VEGF-trap), antibodies against VEGFR-2 (e.g., DC101) and antibodies against VEGF (Bevacizumab, Ranibizumab). (C) Strategies to target VEGF165 interaction with neuropilins. These include: anti-NRP1 antibodies, soluble NRP isoforms and semaphorins (e.g., SEMA3A, SEMA3B, SEMA3F). In addition, there are a number of peptide-mimetics of VEGF165 exons 7/8 which block interaction with NRPs such as VEGF165 (137–160), A7R, EG3287, Tuftsin and its analog TKPPR (see Table 2).