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Related Experiment Videos

Antioxidant enzymes in human tears.

R K Crouch1, P Goletz, A Snyder

  • 1Department of Ophthalmology, Medical University of South Carolina.

Journal of Ocular Pharmacology
|January 1, 1991
PubMed
Summary

Human tears contain superoxide dismutase but lack enzymes to neutralize hydrogen peroxide. This suggests tears offer limited protection against disinfectant solutions, potentially harming the cornea.

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Area of Science:

  • Ophthalmology
  • Biochemistry
  • Tear Film Research

Background:

  • Antioxidant enzymes are crucial for cellular protection against oxidative stress.
  • Hydrogen peroxide is a component in some contact lens disinfectants.
  • The protective mechanisms within the human tear film are not fully understood.

Purpose of the Study:

  • To investigate the presence and activity of major antioxidant enzymes in human tears.
  • To assess the susceptibility of tear film components to hydrogen peroxide.
  • To evaluate the implications for contact lens wear and disinfectant safety.

Main Methods:

  • Collection of minimally stimulated human tear samples.
  • Assay for superoxide dismutase, catalase, and glutathione peroxidase activity.
  • Exposure of tear samples to hydrogen peroxide to assess enzyme inactivation.

Main Results:

  • Catalase and glutathione peroxidase activity were undetectable in human tears.
  • CuZn superoxide dismutase was present but inactivated by 0.2 mM hydrogen peroxide.
  • Tear film lacks robust defense against hydrogen peroxide toxicity.

Conclusions:

  • Human tears possess superoxide dismutase but lack protective enzymes against hydrogen peroxide.
  • The tear film is vulnerable to oxidative damage from hydrogen peroxide-based disinfectants.
  • This vulnerability may pose risks to the cornea and ocular surface during contact lens wear.

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