Heat shock protein family E member 1 (HSPE1)

Heat shock protein family E member 1 (HSPE1), commonly referred to as Hsp10, is a mitochondrial chaperonin that forms a heptameric ring structure. It partners with Hsp60 (encoded by HSPD1) in the mitochondrial matrix to facilitate the correct folding and assembly of imported proteins, an ATP-dependent process critical for mitochondrial and cellular function[1][2][3][4][5]. HSPE1 is also implicated in the immunomodulatory regulation of inflammation, acting to suppress NF-κB activation and key inflammatory mediators[1][3]. It is well known as early-pregnancy factor (EPF), important for immune tolerance during early pregnancy in mammals[3]. HSPE1 is highly conserved, essential for cell survival, and associated with pathologies linked to protein misfolding, cellular stress, and immune dysregulation[1][3][4][5].

Other names

Hsp10Chaperonin 10CPN10EPFGroESEarly-pregnancy factorHeat shock 10 kDa protein 1chaperonin 10

Drugs modulating HSPE1 would typically act by altering its co-chaperonin activity, influencing protein folding and cellular stress pathways (hypothetical; not well established clinically) Potential modulation of immune response through regulation of inflammatory mediators[1][3]