Epidermal growth factor-like domain-containing protein 7 (EGFL7)

Epidermal growth factor-like domain-containing protein 7 (EGFL7) is a secreted protein primarily expressed by endothelial cells, with expression also observed in trophoblasts and during early embryonic development[1][2][3]. Structurally, EGFL7 contains an N-terminal signal peptide, two centrally located EGF-like domains (one being a Ca^2+-binding type), and an EMI (elastin microfibril interface) domain[2][3]. EGFL7 plays a crucial role in the regulation of vascular development, angiogenesis, endothelial cell migration, and vascular tube formation[3]. Functionally, EGFL7 influences critical endothelial and tumor cell behaviors by modulating signaling pathways such as MAPK, PI3K, Notch, and EGFR activation[1]. It is intimately associated with fibronectin in the extracellular matrix and serves as a ligand for integrins[3]. EGFL7 is upregulated in several cancers, where it enhances cell migration and invasion but does not directly promote proliferation; its high expression has been proposed as a biomarker of malignant transformation and a contributor to tumor angiogenesis[4]. Targeting EGFL7 experimentally may disrupt pathological angiogenesis, but further clinical development and validation are ongoing. No significant spelling or nomenclature issues are present with "Epidermal growth factor-like domain-containing protein 7", and it refers to a distinct, recognized therapeutic target in angiogenesis and cancer.

Other names

EGFL7EGF-like domain 7VE-statinZneu1

Antibodies or inhibitors may block EGFL7's ability to regulate endothelial cell migration, angiogenesis, or interaction with integrins and EGFR pathways[1][3]. May disrupt pathological neovascularization or tumor angiogenesis[4].