Recombinant Human VEGFD protein

Vascular endothelial growth factor D (VEGFD), also known as VEGF-D, is a key signaling protein involved in regulating angiogenesis (blood vessel formation) and lymphangiogenesis (lymphatic vessel development). It belongs to the VEGF family, which includes VEGFA, VEGFB, VEGFC, and placental growth factor (PLGF). Discovered in the late 1990s, VEGFD shares structural homology with VEGFC, both featuring conserved VEGF homology domains critical for receptor binding.

Biologically, VEGFD binds to tyrosine kinase receptors VEGFR-2 and VEGFR-3. While VEGFR-2 activation primarily drives blood vessel growth, VEGFR-3 is central to lymphatic endothelial cell proliferation. This dual receptor interaction allows VEGFD to modulate vascular permeability, cell migration, and survival in both circulatory systems. Its role in lymphangiogenesis has linked it to conditions like lymphedema and cancer metastasis, where lymphatic vessel expansion facilitates tumor spread.

Recombinant VEGFD protein is produced using biotechnological methods, often through expression in mammalian cell lines (e.g., HEK293) or bacterial systems. Post-translational processing, including proteolytic cleavage, enhances its receptor-binding capacity. Researchers utilize purified recombinant VEGFD in vitro and in vivo to study its physiological effects, drug discovery, and therapeutic potential. For instance, it’s explored for treating ischemic diseases by promoting collateral vessel formation, while inhibitors targeting VEGFD signaling are investigated in cancer therapy.

Despite therapeutic promise, challenges remain in understanding its context-dependent roles—whether promoting repair or pathology—and optimizing delivery mechanisms. Ongoing research continues to unravel its complex interactions in tissue microenvironments.