Related Experiment Video
Updated: Jun 12, 2025
09:33
An Anaerobic Biosensor Assay for the Detection of Mercury and Cadmium
Published on: December 17, 2018
10.2K
Cadmium toxicity on endoplasmic reticulum functioning
Shivani Mishra1, Ramakrushna Paul1, Vibha Rani2
1Gene Expression and Signaling Lab., Department of Zoology, Mahatma Gandhi Central University Motihari, Bihar 845401, India.
International Journal of Biochemistry and Molecular Biology
|September 23, 2024
Summary
Cadmium toxicity disrupts endoplasmic reticulum (ER) function by impairing protein folding, calcium homeostasis, and lipid metabolism. This review explores how cadmium exposure leads to cellular dysfunction and diseases, highlighting the need for therapeutic strategies.
Area of Science:
- Environmental Toxicology
- Cellular Biology
- Pathology
Background:
- Cadmium (Cd) is a pervasive heavy metal pollutant from industrial and agricultural sources.
- Cadmium toxicity significantly impacts cellular function, particularly endoplasmic reticulum (ER) homeostasis.
- Understanding these mechanisms is crucial for addressing Cd-related health issues.
Purpose of the Study:
- To review the mechanisms by which cadmium impairs ER functioning.
- To examine the role of ER stress, calcium signaling, and lipid metabolism in cadmium toxicity.
- To discuss the link between cadmium-induced ER dysfunction and diseases like cancer and neurodegenerative disorders.
Main Methods:
- Literature review of studies on cadmium toxicity and ER stress.
- Analysis of molecular mechanisms underlying cadmium's effects on protein folding, UPR activation, and calcium signaling.
- Examination of cadmium's impact on lipid metabolism and oxidative stress.
Main Results:
- Cadmium disrupts protein folding, activating the unfolded protein response (UPR) via IRE1, PERK, and ATF6.
- Cd inhibits the SERCA pump, disrupting ER calcium homeostasis and increasing oxidative stress.
- Cadmium affects lipid metabolism, contributing to cellular dysfunction and pathogenesis.
Conclusions:
- Cadmium toxicity severely disrupts ER function, leading to unfolded protein accumulation, calcium dysregulation, and oxidative stress.
- These ER disruptions contribute to the pathogenesis of various diseases, including cancer and neurodegenerative disorders.
- Further research into therapeutic strategies is essential to mitigate cadmium's adverse health effects.
Related Concept Videos
01:32Export of Misfolded Proteins out of the ER
3.5K
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...
3.5K
01:21Smooth Endoplasmic Reticulum
5.7K
Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
5.7K
01:39Endoplasmic Reticulum
94.4K
The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
94.4K
01:17Role of ER in the Secretory Pathway
5.3K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as 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...
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...
5.3K
01:43The Endoplasmic Reticulum
12.3K
The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
12.3K
01:37The Unfolded Protein Response
4.5K
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...
4.5K