MetAP2

MetAP2 (methionine aminopeptidase 2) is a cytosolic metalloprotease that catalyzes the removal of N-terminal methionine residues from nascent proteins, a conserved processing step required for proper protein maturation and cellular function^[1]. Mechanistically, MetAP2 participates in N-terminal protein processing pathways and has been strongly linked to the regulation of endothelial cell proliferation and angiogenesis, making it a biologically important mediator of vascular growth programs^[2][3]. In disease-relevant contexts, elevated MetAP2 activity or expression has been associated with multiple cancer types, and experimental studies have demonstrated that MetAP2 contributes to tumor-associated processes including endothelial cell growth, angiogenesis, and vasculogenic mimicry^[4][5]. MetAP2 has also emerged as a valuable target in cancer research because inhibition of its enzymatic activity suppresses angiogenesis-dependent tumor progression in cellular and animal models^[2][6]. Compared with the related isoform MetAP1, MetAP2 exhibits distinct inhibitor sensitivity, as fumagillin, ovalicin, and their derivatives selectively target MetAP2 while sparing MetAP1, providing an experimentally useful distinction between the two methionine aminopeptidase family members^[2][3]. For experimental applications, natural-product inhibitors such as fumagillin and the semisynthetic analog TNP-470 have been widely used to interrogate MetAP2-dependent biology, whereas newer MetAP2-directed compounds have demonstrated antiangiogenic and antitumor activity in preclinical models^[5][6][7]. Consequently, MetAP2 remains a widely studied regulator of protein processing and angiogenesis and a practical molecular target for mechanistic and translational cancer research^[2][4].