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How do I detect ER stress?

Posted August 25, 2021


Answer

Excessive accumulation of misfolded proteins in the endoplasmic reticulum (ER) is the main cause of ER stress.

ER stress is detected using Thioflavin T (ThT). This is a relatively new method that is being used to detect endoplasmic reticulum (ER) stress in live cells.

Thioflavin T is a tiny molecule that exhibits enhanced fluorescence on binding to protein aggregates. The enhanced ThT-fluorescence correlates directly with proven indicators of UPR (unfolded protein response) activation. Thioflavin T enables researchers to detect ER stress induced by a variety of conditions and compounds within 20 minutes of applying the ER-stress inducing agent.

ER stress can also be detected indirectly by measuring the levels of specific UPR factors. Commonly measured indicators of UPR activation include: phosphorylated PERK, phosphorylated eIF2α, Gadd153/CHOP, ATF4, Grp78/BiP, Grp94, calreticulin, and protein disulphide isomerase (PDI). These are usually detected by immunoblot or immunohistochemistry.

Additional resources

Detection and quantification of endoplasmic reticulum stress in living cells using the fluorescent compound, Thioflavin T

Cell Navigator™ Live Cell Endoplasmic Reticulum (ER) Staining Kit *Red Fluorescence*

Thioflavin T acid