How does ER stress cause apoptosis?

The execution phase of ER stress-induced apoptosis All upstream signals, such as the activation of transcription factors, kinase pathways and the regulation of BCL2 family members, ultimately lead to caspase activation, resulting in the ordered and sequential dismantling of the cell.

What induces ER stress?

ER stress may be caused by factors that impair protein glycosylation or disulfide bond formation, or by overexpression of or mutations in proteins entering the secretory pathway. Ultimately, signaling from these stress-sensing proteins protects the cell or, alternatively, promotes cell death.

Does oxidative stress cause ER stress?

As the protein folding process is dependent on redox homeostasis, the oxidative stress can disrupt the protein folding mechanism and enhance the production of misfolded proteins, causing further ER stress.

How is ER stress related to TXNIP expression?

TXNIP expression was significantly correlated with plasma fasting glucose, plasma triacylglycerol concentrations and specific UPR markers. Induction of ER stress in THP-1 cells or cultured HMDMs led to increased expression of UPR markers, TXNIP, NLRP3 and IL-1β.

How is ER stress related to the UPR?

This transduces the signal of misfolded protein accumulation in the ER, named as ER stress, to the nucleus as “unfolded protein response (UPR).” The ER stress-mediated IRE1α signaling pathway arbitrates the yin and yang of cell life.

What does TXNIP do to the TRX system?

Rather more importantly, TXNIP inhibits EMT, which is the driving force of tumorigenesis and tumour progression. With this background and also in hindsight, it is hardly surprising that there have been some early efforts to find other inhibitors of the TRX system.

Why is TXNIP a target for diabetes therapy?

Moreover, TXNIP expression is highly induced by glucose through the activation of the carbohydrate response element-binding protein, which binds the TXNIP promoter, making it an attractive target for diabetes therapy.