Peroxiredoxin in bovine ocular tissues: immunohistochemical localization and in situ hybridization.
Peroxiredoxins are widely distributed in nature and constitute a molecular family of antioxidant enzymes which decompose hydrogen peroxide and alkyl hydroperoxides. We have previously characterized a peroxiredoxin from bovine ciliary body and deduced its amino acid sequence from analysis of cDNA clones encoding the protein. In this work, we investigated the immunolocalization of this novel antioxidant enzyme and its mRNA expression in bovine eye tissues. High levels of immunoreactivity and mRNA for the enzyme were detected in corneal epithelium. Distinct immunoreactivity and mRNA expression for peroxiredoxin were also detected in uveal tissues, some of the retinal cell layers and ocular vasculature.
Singh
A K
AK
Department of Ophthalmology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
Shichi
H
H
D000818:Animals; D000975:Antioxidants / Q000378:metabolism*; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D019573:Epithelium, Corneal / Q000201:enzymology; D005123:Eye / Q000201:enzymology*; D007124:Immunoenzyme Techniques; D017403:In Situ Hybridization; D010446:Peptide Fragments; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism*; D054464:Peroxiredoxins; D012333:RNA, Messenger / Q000378:metabolism; D011817:Rabbits; D012160:Retina / Q000201:enzymology; D014602:Uvea / Q000201:enzymology
D000975:Antioxidants; D010446:Peptide Fragments; D012333:RNA, Messenger; D010544:Peroxidases; D054464:Peroxiredoxins