Related Experiment Video

Updated: Jun 27, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Prion protein expression in muscle cells and toxicity of a prion protein fragment

D R Brown1, B Schmidt, M H Groschup

  • 1Institut für Neuropathologie, Universität Göttingen, Germany.

European Journal of Cell Biology
|April 2, 1998
PubMed

Insights

Cellular prion protein (PrPc) expression in skeletal muscle regulates resistance to oxidative stress. PrPc deficiency in muscle cells impairs the antioxidant response and increases susceptibility to prion peptide toxicity.

Area of Science:

  • Neuroscience
  • Skeletal Muscle Physiology
  • Cellular Biology

Background:

  • The prion protein (PrP) is a glycoprotein typically found on neuronal surfaces.
  • Prion protein expression in skeletal muscle suggests a potential physiological role in this tissue.
  • Prion protein (PrP) is a cell surface glycoprotein normally associated with neurones.

Purpose of the Study:

  • To investigate the role of cellular prion protein (PrPc) in skeletal muscle.
  • To examine the relationship between PrPc expression, differentiation, and oxidative stress resistance in muscle cells.
  • To assess the impact of PrPc deficiency on muscle cell response to prion peptide toxicity.

Main Methods:

  • Cultured mouse myoblasts and myotubes were used to study PrP expression and differentiation.
  • Cu/Zn superoxide dismutase (SOD-1) levels were measured during myoblast to myotube differentiation.
  • Muscle cells from PrPc-deficient mice were exposed to a neurotoxic prion protein peptide (PrP106-126) in the presence of microglia.

Main Results:

  • Prion protein expression and SOD-1 levels are upregulated during myoblast to myotube differentiation.
  • PrPc-deficient muscle cells show a diminished SOD-1 increase upon differentiation.
  • PrP106-126 toxicity in the presence of microglia is significantly greater in myotubes than myoblasts, and absent in PrPc-deficient cells.

Conclusions:

  • Cellular prion protein (PrPc) expression is linked to the regulation of cellular resistance to oxidative stress in skeletal muscle.
  • PrPc plays a role in modulating the antioxidant response during muscle cell differentiation.
  • PrPc expression influences muscle cell susceptibility to prion peptide-induced toxicity, particularly in differentiated myotubes.

More Related Videos

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

High-throughput Screening for Protein-based Inheritance in S. cerevisiae08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Related Concept Videos

Amyloid Fibrils03:03

Amyloid 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...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...