Endoplasmic reticulum metallopeptidase 1 (ERMP1)

Endoplasmic reticulum metallopeptidase 1 (ERMP1) is a zinc-dependent, membrane-bound metallopeptidase of the M28 family, localized to the endoplasmic reticulum. It is broadly expressed in several human cancers and is crucial for mediating the unfolded protein response (UPR) and cellular defense against oxidative stress. ERMP1 supports cancer cell proliferation, migration, and invasiveness under stress by promoting activation of UPR sensors (such as PERK) and induction of stress chaperones (such as GRP78/BiP). In the ovary, ERMP1 is required for follicle organization. High ERMP1 expression is associated with tumorigenesis and may serve as a biomarker and potential therapeutic target for anti-cancer strategies, particularly those disrupting UPR mechanisms in tumors[1][2][3][4].

Other names

FLJ23309FXNAKIAA1815FxnAFelix-inaaminopeptidase FxnabA207C16.3

Inhibition of ERMP1 impairs the UPR and oxidative stress response in cancer cells, potentially sensitizing them to stress and blocking survival pathways[1][2][3]. (No specific drugs yet identified that directly inhibit ERMP1; mechanisms are theoretical and based on gene silencing or antibody strategies.)