Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
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DOI：
10.1006/abbi.1996.0362
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发表时间：
1996-09-01
影响因子：
3.9
通讯作者：
Ischiropoulos, H
中科院分区：
文献类型：
--
作者：
Gow, A;Duran, D;Ischiropoulos, H
反应性物质的产生与各种人类疾病和疾病实验模型中的组织损伤有关。过氧亚硝酸盐是一种具有多种反应途径的强氧化剂。一种可能特异于过氧亚硝酸盐的蛋白质修饰反应是酪氨酸残基的邻位硝化，硝基酪氨酸已被用作过氧亚硝酸盐介导的氧化应激的标记物。当过氧亚硝酸盐在生理PPP下与不含脂肪酸的牛血清白蛋白或与人血浆蛋白反应时，形成硝基酪氨酸。当蛋白质与一氧化氮、二氧化氮或一氧化氮加过氧化氢在亚铁或亚铁辣根过氧化物酶存在下孵育时，未形成硝基酪氨酸。低分子量的分子，如尿酸，抗坏血酸，和巯基抑制蛋白酪氨酸硝化在没有碳酸氢盐。碳酸氢根的加入能催化硝化反应，提高硝化产率，克服了抗氧化剂的抑制作用。Biclonal/CO2以浓度依赖性方式提高蛋白硝基酪氨酸的产量。通过CO2与过氧亚硝酸根阴离子的相互作用来实现对Mitration的催化。提出了一种涉及本领域ONOO（O）CO-中间体的机制，其容易以非自由基依赖性方式硝酸化酪氨酸残基。因此，过氧亚硝酸盐硝酸酪氨酸残基的机制，是由CO2在正常的生理条件下催化。(C)出版社：Academic Press，Inc.
Production of reactive species has been associated with tissue injury in diverse human disorders and experimental models of disease. Peroxynitrite is a strong oxidant with multiple pathways of reactivity. One protein modification reaction that may be specific to per-oxynitrite is the nitration of the ortho position of tyrosine residues and nitrotyrosine has been used as a marker for peroxynitrite-mediated oxidative stress. Nitrotyrosine was formed when peroxynitrite was reacted at physiological PPP with fatty acid-free bovine serum albumin or with human plasma proteins. Nitrotyrosine was not formed when proteins were incubated with nitric oxide, nitrogen dioxide, or nitric ox:ide plus hydrogen peroxide in the presence of ferrous iron or ferrihorseradish peroxidase. Low-molecular-weight molecules such as uric acid, ascorbate, and sulfhydryls inhibited protein tyrosine nitration in the absence of bicarbonate. Addition of bicarbonate catalytically enhanced the yield of nitration and overcame the inhibition of these antioxidants. Bicarbonate/CO2 enhanced the yield of protein nitrotyrosine in a concentration-dependent manner. Catalysis of mitration is achieved by the interaction of CO2 with the peroxynitrite anion. A mechanism is' proposed involving art ONOO(O)CO- intermediate, which readily nitrates tyrosine residues in a non-radical-dependent manner. Thus, peroxynitrite nitrates tyrosine residues by a mechanism that is catalyzed by CO2 under normal physiological conditions. (C) 1996 Academic Press, Inc.