Related Experiment Video
Updated: May 13, 2026
11:57
Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase
Published on: June 24, 2025
Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
Ping Chen1, Ruo-Ran Wang, Xiao-Jie Ma
1Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Department of Marine Biology, Shenzhen University, Shenzhen 518060, China. liuqiong@szu.edu.cn.
International Journal of Molecular Sciences
|February 27, 2013
Summary
Selenoprotein M (SelM) plays a crucial role in preventing Alzheimer's disease by reducing beta-amyloid aggregation and oxidative stress. Selenium supplementation enhances SelM's protective effects against neurodegeneration.
Area of Science:
- Biochemistry
- Neuroscience
- Cell Biology
Background:
- Selenoprotein M (SelM) is highly expressed in the human brain and implicated in neuroprotection.
- Alzheimer's disease (AD) is characterized by beta-amyloid (Aβ) aggregation and oxidative stress.
- Understanding SelM's role in AD pathogenesis is crucial for developing therapeutic strategies.
Purpose of the Study:
- To investigate the effect of Selenoprotein M (SelM) on beta-amyloid (Aβ) aggregation and oxidative stress in vitro.
- To determine the influence of sodium selenite on SelM expression and its functional activity.
- To evaluate the neuroprotective potential of full-length SelM and its variant (SelM') against Aβ-induced cellular damage.
Main Methods:
- Overexpression of human SelM in HEK293T cells.
- Treatment with sodium selenite (Na(2)SeO(3)) to modulate SelM expression.
- Cotransfection with Aβ(42) peptide to induce aggregation and cellular stress.
- Assessment of Aβ(42) aggregation rates and mitochondrial morphology.
Main Results:
- Sodium selenite promoted full-length SelM expression and inhibited truncated SelM.
- Full-length SelM and SelM' significantly inhibited Aβ(42) aggregation and mitigated Aβ-induced mitochondrial swelling.
- SelM' exhibited higher antioxidant activity than the mutated form.
- Absence of sodium selenite led to increased Aβ(42) aggregation and failed to protect mitochondria.
Conclusions:
- Full-length SelM and its variant SelM' demonstrate potential in preventing Aβ aggregation.
- Selenium supplementation enhances SelM's protective effects against oxidative stress and Aβ toxicity.
- SelM may serve as a therapeutic target for Alzheimer's disease by combating Aβ-induced cellular damage.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:26Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.