The role of corneal crystallins in the cellular defense mechanisms against oxidative stress.
The refracton hypothesis describes the lens and cornea together as a functional unit that provides the proper ocular transparent and refractive properties for the basis of normal vision. Similarities between the lens and corneal crystallins also suggest that both elements of the refracton may also contribute to the antioxidant defenses of the entire eye. The cornea is the primary physical barrier against environmental assault to the eye and functions as a dominant filter of UV radiation. It is routinely exposed to reactive oxygen species (ROS)-generating UV light and molecular O(2) making it a target vulnerable to UV-induced damage. The cornea is equipped with several defensive mechanisms to counteract the deleterious effects of UV-induced oxidative damage. These comprise both non-enzymatic elements that include proteins and low molecular weight compounds (ferritin, glutathione, NAD(P)H, ascorbate and alpha-tocopherol) as well as various enzymes (catalase, glucose-6-phosphate dehydrogenase, glutathione peroxidase, glutathione reductase, and superoxide dismutase). Several proteins accumulate in the cornea at unusually high concentrations and have been classified as corneal crystallins based on the analogy of these proteins with the abundant taxon-specific lens crystallins. In addition to performing a structural role related to ocular transparency, corneal crystallins may also contribute to the corneal antioxidant systems through a variety of mechanisms including the direct scavenging of free radicals, the production of NAD(P)H, the metabolism and/or detoxification of toxic compounds (i.e. reactive aldehydes), and the direct absorption of UV radiation. In this review, we extend the discussion of the antioxidant defenses of the cornea to include these highly expressed corneal crystallins and address their specific capacities to minimize oxidative damage.
Lassen
Natalie
N
Molecular Toxicology and Environmental Health Sciences Program, Department of Pharmaceutical Sciences, University of Colorado Health Sciences Center, Denver, CO 80262, USA.
Black
William J
WJ
Estey
Tia
T
Vasiliou
Vasilis
V
D000444:Aldehyde Dehydrogenase / Q000378:metabolism / Q000502:physiology; D000818:Animals; D000975:Antioxidants / Q000378:metabolism / Q000502:physiology*; D014408:Biomarkers, Tumor / Q000378:metabolism / Q000502:physiology; D002374:Catalase / Q000378:metabolism / Q000502:physiology; D003315:Cornea / Q000201:enzymology / Q000378:metabolism* / Q000502:physiology; D003459:Crystallins / Q000378:metabolism / Q000502:physiology*; D021984:Cyclophilin A / Q000378:metabolism / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000502:physiology; D005979:Glutathione Peroxidase / Q000378:metabolism / Q000502:physiology; D006801:Humans; D007521:Isocitrate Dehydrogenase / Q000378:metabolism / Q000502:physiology; D008954:Models, Biological; D018384:Oxidative Stress / Q000502:physiology*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism / Q000502:physiology; D017382:Reactive Oxygen Species / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism / Q000502:physiology; D013482:Superoxide Dismutase / Q000378:metabolism / Q000502:physiology; D014174:Transketolase / Q000378:metabolism / Q000502:physiology; D025521:Tumor Suppressor Proteins / Q000378:metabolism / Q000502:physiology; D014466:Ultraviolet Rays / Q000009:adverse effects
D000975:Antioxidants; D014408:Biomarkers, Tumor; D003459:Crystallins; D004268:DNA-Binding Proteins; D017382:Reactive Oxygen Species; D012709:Serum Albumin; D025521:Tumor Suppressor Proteins; D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+); D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D000444:Aldehyde Dehydrogenase; D014174:Transketolase; C095157:ENO1 protein, human; D010751:Phosphopyruvate Hydratase; D021984:Cyclophilin A