Related Experiment Video
Updated: May 28, 2026

Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
The new murine hepatic 3A cell line responds to stress stimuli by activating an efficient Unfolded Protein Response
Barbara Guantario1, Alice Conigliaro, Laura Amicone
1National Research Institute on Food and Nutrition (INRAN), Rome, Italy.
Abstract:
In the present study we have investigated the properties of a novel cell line (3A cells) obtained from the liver of 14.5 days post coitum (dpc) wild-type mouse embryo. 3A cells morphology was characterized by fluorescent localization of F-actin and β-catenin. The expression of specific genes and proteins essential to liver function in these cells was comparable or even more efficient then in the differentiated hepatocytic cell line MMH-D6. 3A cells also showed the capability to excrete molecules in extracellular spaces resembling functional bile canaliculi, glycogen storage activity and the ability to control retinol-binding protein 4 secretion in response to retinol deprivation. Their response to the exogenous stress stimulus induced by tunicamycin was analysed by PCR Pathway Array containing 84 genes involved in the Unfolded Protein Response (UPR). 3A cells were shown to activate the UPR following a typical stressful event, indicating that this cellular model could be further exploited to investigate hepatic proteins secretion and specific reaction to different injuries.
Related Concept Videos
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
Role of ER in the Secretory Pathway
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Other Stress Responses in Bacteria
Export of Misfolded Proteins out of the ER
Stringent Response in E. coli
