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Dipeptidase 2 (DPEP2) is a membrane-bound dipeptidase enzyme anchored to the plasma membrane via glycosyl phosphatidylinositol[1][3]. It hydrolyzes a variety of dipeptides, including leukotriene D4 (LTD4), beta-lactam rings of some antibiotics, and cystinyl-bis-glycine. DPEP2 is highly expressed in lung, heart, and testis, with roles in regulating cell migration and invasion through effects on epithelial-mesenchymal transition (EMT), cancer stem cell transformation, and chemotherapy response in lung adenocarcinoma[1]. DPEP2 also acts as a key regulator in inflammatory signal transduction in macrophages by binding and modulating MAP3K members that activate NF-κB and p38 MAPK pathways[2]. Loss or degradation of DPEP2 (e.g., via Trim32-mediated ubiquitination) enhances pro-inflammatory signaling in macrophages[2]. DPEP2 serves as both a prognostic biomarker and potential therapeutic target in cancer and inflammation.
Cisplatin: increased sensitivity via inhibition of EMT and stem cell transformation markers. Beta-lactam antibiotics: hydrolysis of the beta-lactam ring.
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