LVRN (laeverin) is a cell-surface zinc metalloaminopeptidase with distinctive enzymatic properties defined by a nonconserved histidine residue at position 379 1. Primarily expressed on extravillous trophoblasts, LVRN cleaves N-terminal amino acids from peptides including angiotensin-3, kisspeptin-10, and endokinin C, with marked preference for leucine-containing substrates. In normal placentation, LVRN facilitates trophoblast invasion and spiral artery remodeling by regulating peptide bioactivity and promoting epithelial-mesenchymal transition through interactions with integrins and matrix metalloprotease 1 2. LVRN also mediates immunotolerance by inducing indoleamine 2,3-dioxygenase-1 production in monocytes, creating an immunosuppressive environment at the maternal-fetal interface 3. Abnormal LVRN expression associates with preeclampsia: ectopic cytoplasmic localization and leakage into fetal capillaries correlate with impaired trophoblast invasion 24. LVRN also represents a novel cell-surface target for metastasizing cancer cells, with expression detected in circulating tumor cells and invasion lesions across multiple cancer types 5. Amniotic fluid LVRN levels correlate with fetoplacental growth parameters, suggesting biomarker potential 6. Downregulated LVRN expression associates with kidney stone pathogenesis 7.