FBLN7 (fibulin 7) is a secreted glycoprotein and matricellular adhesion molecule that functions as an extracellular matrix regulator with diverse tissue-specific roles. Originally identified in developing teeth where it supports odontoblast differentiation and dentin formation [UniProt], FBLN7 is expressed in specialized tissues including cartilage, eye, placenta, and vascular tissue 1. Mechanistically, FBLN7 binds multiple partners through its N-terminal coiled-coil domain and EGF-like domains: it interacts with heparan sulfate proteoglycans for cell surface anchoring 2, binds EGFR to activate FAK/AKT signaling 3, engages integrin α5β1 for cell adhesion 4, and modulates angiopoietin-1/Tie2 signaling 5. Pathologically, FBLN7 promotes adverse cardiac remodeling and fibrosis after myocardial infarction 3, mediates renal tubular calcification and calcium oxalate-induced kidney injury through crystal binding 26, and is overexpressed in glioblastomas where it drives aberrant neovascularization 5. Conversely, its C-terminal fragment exhibits antiangiogenic activity through VEGFR2 inhibition 4. Rare variants in FBLN7 associate with varicose vein susceptibility 7. These findings suggest FBLN7's therapeutic potential both as a target for inhibition in fibrotic/angiogenic diseases and as a bioactive fragment for antiangiogenic applications.