Endoplasmic reticulum stress-related markers (UPR)

Endoplasmic reticulum (ER) stress-related markers refer to a group of proteins and signaling molecules that constitute the Unfolded Protein Response (UPR). When misfolded or unfolded proteins accumulate in the ER lumen, three primary sensors—PERK, IRE1, and ATF6—are activated to restore cellular homeostasis [11, 16]. These markers, including the molecular chaperone GRP78 (BiP) and the pro-apoptotic transcription factor CHOP, serve as critical indicators of the cell's physiological state and its capacity to manage proteotoxic stress [5, 13]. While the UPR initially functions as an adaptive survival mechanism, chronic or severe activation of these markers is a hallmark of various pathologies, including neurodegenerative diseases, type 2 diabetes, and cancer [3, 9, 12]. Consequently, components within this marker set are targeted by small molecules to either alleviate stress in degenerative conditions or selectively induce apoptosis in malignant cells [6, 16].

Other names

Unfolded Protein Response markersUPR markersER stress indicatorsEndoplasmic reticulum stress response pathway components

Modulation of the unfolded protein response (UPR) pathway to either enhance protein folding capacity, inhibit stress-induced translation, or regulate the switch between cell survival and apoptosis [1, 6].