Crosstalk between endoplasmic reticulum stress and non‐coding RNAs in cardiovascular diseases

Abstract

Cells are exposed to various pathological stimulus within the cardiovascular system that challenge cells to adapt and survive. Several of these pathological stimulus alter the normal function of the endoplasmic reticulum (ER), leading to the accumulation of unfolded and misfolded proteins, thus triggering the unfolded protein response (UPR) to cope with the stress or trigger apoptosis of damaged cells. Downstream components of the UPR regulate transcription

PP2Ac knockdown attenuates lipotoxicity‑induced pancreatic β‑cell dysfunction and apoptosis

“…PP2Ac knockdown reduced PA-induced RoS levels and attenuated the PA-induced reduction in ATP production, indicating that it attenuated the level of oxidative stress in MIN6 cells. Sustained ER stress and mitochondrial damage eventually lead to apoptosis (10). This is consistent with the observation that increasing either the PA concentration or duration of exposure reduced the viability of MIN6 cells in the present study, and treatment with PA increased the rate of apoptosis, while knocking down PP2Ac reduced the rate of cell death.…”

“…Under lipotoxic conditions, the unfolded protein response (UPR) is activated, which relieves endoplasmic reticulum (ER) stress by preventing protein translation, increasing the expression of chaperone proteins that perform refolding, and accelerating ER-associated degradation processes. However, sustained lipotoxic stimulation may cause the UPR to be unable to maintain ER homeostasis, resulting in the disruption of ER integrity followed by cell apoptosis (8)(9)(10). In addition, lipotoxicity increases the accumulation of mitochondrial reactive oxygen species (RoS) and induces mitochondrial DNA mutations, leading to mitochondrial dysfunction and impairing cellular energy metabolism (11).…”