Key result
Putative protein nitratases, which catalyze denitration of peroxynitrite-treated proteins, were detected in dog prostate extract and activated by m-calpain/Ca2+.
The study identifies putative protein nitratases in dog prostate that can denitrate peroxynitrite-treated proteins, suggesting a mechanism for reversing protein nitration.
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Supports denitration pathway in canine tissue; hypothesis-generating for nitrosative stress reversal in humans.
Putative "protein nitratases," which catalyze denitration of peroxynitrite (PN)-treated, proteins, were detected in the crude extract of dog prostate. Nitratase activity was monitored by the decreased intensity of nitrotyrosine immunoreactive-bands in Western blot and increased nitrate level in dialysate of incubation mixture, which contained prostate crude extract, protease inhibitors and a PN-treated substrate, such as treated histone (III-S), BSA, invertase, or polylysine. Nitratases were activated by preincubation with m-calpain/Ca2+. Furthermore, after denitration, the activity of PN/DTT-treated invertase decreased to the similar activity level of DTT-treated invertase. At least two different types of nitratases may occur: type I, reductant-dependent, and type II, reductant-independent.
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Kuo et al. (1999) studied this question. Protein nitratases from dog prostate extract was evaluated on Nitratase activity (decreased intensity of nitrotyrosine immunoreactive-bands and increased nitrate level). Putative protein nitratases, which catalyze denitration of peroxynitrite-treated proteins, were detected in dog prostate extract and activated by m-calpain/Ca2+.
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