Novel 28‐kDa secretory protein from rat olfactory epithelium

Abstract

We have isolated a novel secretory 28-kDa protein which is an abundant component of the rat olfactory mucosa. The partial sequence of the 28-kDa protein has been determined. The amino acid sequence of the 28-kDa protein is similar to that of non-selenium glutathione peroxidase from bovine ciliary body. The 28-kDa protein catalyzed decomposition of the hydrogen peroxide as well as organic hydroperoxides by reduced glutathion and seems to be a member of the glutathion peroxidases family.

1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage

“…Thus, C48 and H441 cells had similar potential to respond to a cytokine-induced stress and the relative resistance of C48 cells seems to be specific for the oxidant-mediated membrane lipid peroxidation pathway. Discussion 1-CysPrx is a recently described member of the peroxiredoxin family that is expressed at relatively high levels in the lungs, eyes, and olfactory epithelium (3,9,20,21). Overexpression of the protein in 3T3 cells has been shown to increase the ability of these cells to degrade H 2 O 2 and protects them against H 2 O 2 -mediated inactivation of glutamine synthetase (6).…”

“…Initial studies indicated that GSH could function as a reductant with 1-cysPrx isolated from bovine eye (20) or rat olfactory epithelium (21), although the latter result subsequently could not be reproduced (22). Studies with recombinant protein also have been inconclusive because GSH has been effective in some studies (7,23) but not in others (6).…”

An Antisense Oligonucleotide to 1-cys Peroxiredoxin Causes Lipid Peroxidation and Apoptosis in Lung Epithelial Cells

“…The 2-cysPrx, also referred to as thioredoxin peroxidases, reduce peroxides with electrons provided by thioredoxin (28,29). 1-cysPrx, also named Prx VI, is capable of reducing peroxides in the presence of small thiols such as dithiothreitol (1, 2, 7) or glutathione (2,3,4,6). We have recently demonstrated that depletion of glutathione diminishes activity of the enzyme in intact cells, indicating that it can serve as a physiological electron donor (23).…”

“…1-cysPrx, also named peroxiredoxin VI, is a member of this superfamily that can reduce phospholipid hydroperoxides (PLOOH) as well as organic peroxides and H 2 O 2 (1-3). 1-cysPrx has been isolated from bovine ciliary epithelium (4,5), rat olfactory epithelium (6,7), and rat and bovine lungs (8,9); Northern and immunoblot analyses of mammalian tissues show the presence of 1-cysPrx in all organs with especially high levels of 1-cysPrx protein and mRNA expression in lung (8,10). 1-cysPrx is a bifunctional enzyme with both glutathione peroxidase (GPx) and phospholipase A 2 (PLA 2 ) activities (3).…”

Seed 1-Cysteine Peroxiredoxin Antioxidants Are Not Involved in Dormancy, But Contribute to Inhibition of Germination during Stress

“…In plants, antioxidant activity has been demonstrated for the 2-Cys BAS1 (Baier and Dietz, 1997) and the 1-Cys PER1 (Stacy et al, 1996) of barley (Hordeum vulgare). Transgenic plants overexpressing the rice (Oryza sativa) 1-Cys Prx (R1C-Prx) exhibit higher resistance to oxidative stress, suggesting antioxidant activity (Lee et al, 2000) in accordance with the function of 1-Cys homologs in other organisms (Shichi and Demar, 1990;Netto and Stadtman, 1996;Peshenko et al, 1996).…”