Recombinant Human EG-VEGF/PK1 Protein

Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also called prokineticin 1 (PK1), is a member of the prokineticin family of secreted proteins that share a common structural motif containing ten conserved cysteine residues that form five pairs of disulfide bonds (1, 2). Members of this family include the mammalian EG-VEGF/PK1 and PK2, as well as the venom protein A (VPRA) from the venom of black mamba snake and the frog Bombina variegata, Bv8 (1). Human EG-VEGF precursor is a 105 amino acid (aa) residue protein with a 19 aa signal peptide that is cleaved to yield a 86 aa mature protein (1, 2). EG-VEGF is expressed in multiple tissues including the gastrointestinal (GI) tract and steroidogenic glands (testis, ovary, placenta and adrenal glands). EG-VEGF has been shown to potently stimulate the contraction of GI smooth muscle. In addition, EG-VEGF is a tissue-specific angiogenic factor that exhibits biological activities similar to that of VEGF on select cells. It induces the proliferation, migration, and fenestration in cultured endocrine gland-derived capillary endothelial cells. EG-VEGF binds to and activates two closely related G protein-coupled receptors, EG‑VEGF/PK1-R1 and EG-VEGF/PK2-R2 (3, 4). Activation of the receptors leads to stimulation of phosphoinositide turnover and activation of p44/p42 MAP kinase signaling pathways.