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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

Summary

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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.

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.

Related Experiment Videos

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.