Related Experiment Video

Updated: May 18, 2026

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

CHOP and caspase 3 induction underlie glioblastoma cell death in response to endoplasmic reticulum stress

Quincy A Quick1, Milton O Faison

  • 1Department of Biology, Southern University at New Orleans, New Orleans, LA 70126;

Experimental and Therapeutic Medicine
|September 13, 2012
PubMed

Insights

Endoplasmic reticulum stress inducers thapsigargin and tunicamycin effectively kill glioblastoma cells. This programmed cell death, triggered by endoplasmic reticulum stress, halts tumor cell reproduction.

Area of Science:

  • Oncology
  • Cellular Biology
  • Molecular Biology

Background:

  • The unfolded protein response (UPR) in the endoplasmic reticulum (ER) plays a crucial role in cellular homeostasis and protection.
  • Targeting ER stress pathways offers a potential strategy for cancer therapy due to their involvement in tumor cell survival.
  • Glioblastomas are aggressive brain tumors with limited treatment options, necessitating novel therapeutic approaches.

Purpose of the Study:

  • To investigate the efficacy of ER stress inducers, thapsigargin and tunicamycin, in eliminating glioblastoma cells.
  • To determine the mechanism of glioblastoma cell death induced by ER stress.
  • To establish ER stress induction as a potential therapeutic strategy against glioblastomas.

Main Methods:

  • Treatment of glioblastoma cells with clinically relevant concentrations of thapsigargin and tunicamycin.
  • Assessment of glioblastoma cell reproductive capacity and cell death.
  • Measurement of C/EBP homologous protein (CHOP) levels and caspase 3 activity as indicators of apoptosis.

Main Results:

  • Thapsigargin and tunicamycin at clinically relevant concentrations significantly reduced glioblastoma cell reproductive capacity.
  • Induction of ER stress led to glioblastoma cell death.
  • Elevated levels of CHOP and caspase 3 activity confirmed apoptosis as the mode of cell death.

Conclusions:

  • Glioblastomas are susceptible to cell death induction via ER stress.
  • ER stress inducers demonstrate potential as a therapeutic strategy for glioblastoma eradication.
  • Targeting the ER stress pathway represents a promising avenue for glioblastoma treatment.

More Related Videos

Caspase-3 Activity in the Rat Amygdala Measured by Spectrofluorometry After Myocardial Infarction08:41

Caspase-3 Activity in the Rat Amygdala Measured by Spectrofluorometry After Myocardial Infarction

Published on: January 12, 2016

Monitoring Cleaved Caspase-3 Activity and Apoptosis of Immortalized Oligodendroglial Cells using Live-cell Imaging and Cleaveable Fluorogenic-dye Substrates Following Potassium-induced Membrane Depolarization10:45

Monitoring Cleaved Caspase-3 Activity and Apoptosis of Immortalized Oligodendroglial Cells using Live-cell Imaging and Cleaveable Fluorogenic-dye Substrates Following Potassium-induced Membrane Depolarization

Published on: January 13, 2012

Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Overview of Cell Death01:30

Overview of Cell Death

Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
Cell death was observed in the early 19th century, but there was no experimental evidence to prove it. In 1842, Carl Vogt first discovered cell death in a metamorphic toad; however, it was not termed ‘cell death.’ Scientists discovered different cell death pathways only in the 20th century...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...