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Selective oxidation of methionine residues in prion proteins

B S Wong1, H Wang, D R Brown

  • 1NERC Institute of Virology and Environmental Microbiology, Oxford, OX1 3SR.

Biochemical and Biophysical Research Communications
|June 11, 1999
PubMed

Insights

Normal prion protein (PrP) may protect cells from oxidative stress. Researchers found that methionine residues in PrP are highly susceptible to oxidation, suggesting a key role in antioxidant activity.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Oxidative Stress

Background:

  • Prion proteins are implicated in neurodegenerative diseases.
  • The normal cellular function of prion protein (PrP) is not fully understood.
  • PrP may play a role in cellular response to oxidative stress.

Purpose of the Study:

  • To investigate the antioxidant activity of normal prion protein.
  • To identify specific residues involved in PrP's antioxidant mechanism.

Main Methods:

  • Purified recombinant mouse and chicken PrP were used.
  • Proteins were refolded in the presence of copper (II).
  • Susceptibility of methionine residues to oxidation was analyzed.

Main Results:

  • Methionine residues in PrP were found to be uniquely susceptible to oxidation.
  • This susceptibility suggests a potential mechanism for antioxidant activity.

Conclusions:

  • Methionine residues are likely crucial for the antioxidant function of normal prion protein.
  • Understanding this mechanism could offer insights into neuroprotection.

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