During embryonic development angiogenesis is initiated as mesoderm mesenchyme cells are specified to differentiate into angioblasts, expressing the Vascular Endothelial Growth Factor Receptor (VEGFR-2).

These cells will secrete the signaling molecule vascular endothelial factor A (VEGFA) which will recruit the angioblasts expressing its partnering receptor to the site of future angiogenesis.

The angioblasts will create scaffolding structures that form the primary capillary plexus from where the local vasculature system will develop.

VEGFA is essential for adults during organ remodeling and diseases that involve blood vessels, for example, in wound healing, tumor angiogenesis, diabetic retinopathy, and age-related macular degeneration.

Anti-VEGFA therapy can be used to treat patients with undesirable angiogenesis and vascular leakage in cancer and eye diseases but also could result in the inhibition of neurogenesis and neuroprotection.

These two receptors act through different pathways to contribute to endothelial cell proliferation and migration, and formation of tubular structures.

Following this dimerization, through the action of the receptor itself, a phosphate group is added to certain tyrosines within the molecule in a process called auto-phosphorylation.

[18] The autophosphorylation of these amino acids allows for signalling molecules within to the cell to bind to the receptor and become activated.

[23] PKC phosphorylates the mitogen-activated protein kinase (MAPK) ERK which then moves to the nucleus of the cell and takes part in nuclear signalling.

[24] Once in the nucleus, ERK activates various transcription factors which initiate expression of genes involved in cellular proliferation.

[33][34] Vascular endothelial growth factor A has been shown to interact with: This article incorporates text from the United States National Library of Medicine, which is in the public domain.