Aminopeptidase Q (LVRN)

Aminopeptidase Q (LVRN; Laeverin) is a zinc-dependent metalloaminopeptidase and a novel member of the M1 family of aminopeptidases[1][2]. It is specifically expressed on the cell surface of human extravillous trophoblasts and is thought to be important for placental development and the maintenance of normal pregnancy[1][3]. LVRN cleaves the N-terminal amino acid from several placental peptide hormones, including angiotensin III, endokinin C, and kisspeptin-10, suggesting a regulatory role at the embryo-maternal interface[1][3]. Its enzymatic activity is sensitive to inhibitors like bestatin, and it possesses unique amino acid substitutions in its catalytic motif that influence substrate specificity[1]. LVRN is not widely implicated as a therapeutic target in disease, but its restricted placental localization makes it a potential biomarker for placental health or disease[1][2][3].

Other names

LaeverinLVRNAQPEPAP-QAPQFLJ90650TAQPEPCHL2 antigenAMPQ

Aminopeptidase inhibition (competitive inhibition by bestatin and natural placental peptides such as substance P, angiotensin IV, and bradykinin)