Abstract
Glutathione peroxidase (GPX) reduces peroxides using reduced glutathione as the electron donor. Glutathione-dependent peroxidase activity in the soluble fraction of whole rat eye extracts (n = 3 or 4 at each stage) was the highest in the pre-natal stage (31.0 ± 1.9 mU/mg protein) and gradually declined thereafter. The lowest value was 15.3 ± 2.3 mU/mg protein at day 9. When the protein levels of the major selenium-containing glutathione peroxidase, GPX1, and the recently identified non-selenium-containing glutathione peroxidase, peroxiredoxin 6, were evaluated by immunoblotting using specific antibodies, they gradually declined after birth. An immunohistochemical analysis was carried out to identify the cells that express GPX1. Although the presence of GPX1 was evident only in restricted tissues, such as the corneal and lens epithelia in the adult, its levels were transiently augmented in ganglion cells, the layer of rods and cones, and pigment cells in the retina from 6 to 12 days after birth and then declined afterward. At the adult stage, the expression of GPX1 was negligible in these cells. Thus GPX1 appears to play a major role at this neonatal stage, corresponding to the period for eyelid opening. The decline in GPX1 levels after birth suggests that the detoxification of peroxides is important at this particular stage or that other, as yet unidentified peroxide-detoxifying enzymes are induced during this period.
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