Figure 6.
Figure 6. Interaction of vascular endothelial growth factor (VEGF) family members with their cognate receptors on endothelial cells. / The VEGF receptors harbor seven extracellular immunoglobulin (Ig)-homology domains. The fifth Ig domain of VEGFR-3 is cleaved after biosynthesis to yield a stable disulfide bond linking the Ig subunits. VEGFR-1 and VEGFR-2 initiate signals essential to the angiogenic response, whereas VEGFR-3 regulates lymph angiogenesis. NRP-1 (neuropilin-1) binds to the carboxy-terminal sequence of VEGF165 to enhance binding of the angiogenic molecule to the VEFGR-2 receptor. / Abbreviations: TK, tyrosine kinase; MMP, matrix metalloproteases; PIGF, placental growth factor.

Interaction of vascular endothelial growth factor (VEGF) family members with their cognate receptors on endothelial cells.

The VEGF receptors harbor seven extracellular immunoglobulin (Ig)-homology domains. The fifth Ig domain of VEGFR-3 is cleaved after biosynthesis to yield a stable disulfide bond linking the Ig subunits. VEGFR-1 and VEGFR-2 initiate signals essential to the angiogenic response, whereas VEGFR-3 regulates lymph angiogenesis. NRP-1 (neuropilin-1) binds to the carboxy-terminal sequence of VEGF165 to enhance binding of the angiogenic molecule to the VEFGR-2 receptor.

Abbreviations: TK, tyrosine kinase; MMP, matrix metalloproteases; PIGF, placental growth factor.

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