Nitration of cytochrome C by peroxynitrite: a putative anti-apoptotic pathway mediated by prostaglandin H2 synthase (PGHS) and nitric oxide (NO) synthase.
Nitration of cytochrome C by peroxynitrite: a putative anti-apoptotic pathway mediated by prostaglandin H2 synthase (PGHS) and nitric oxide (NO) synthase.
复制标题
过氧亚硝酸盐对细胞色素 C 的硝化：由前列腺素 H2 合酶 (PGHS) 和一氧化氮 (NO) 合酶介导的推定抗凋亡途径。
DOI：
10.1007/978-1-4615-0193-0_66
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发表时间：
2002
影响因子：
--
通讯作者：
Kim,Hyesook
中科院分区：
文献类型：
--
作者：
Roberts-Kirchhoff,ElizabethS;Kim,CherylK;Kim,Hyesook
Overexpression of PGHS form-2 (PGHS-2) induces inhibition of apoptosis1. Increased expression of both inducible NO synthase and PGHS-2 has been reported in intestinal inflammation2-4. The anti-apoptotic effect of PGHS-2 may be a result of increased or decreased activity of enzymes or proteins involved in the apoptotic pathway. Nitration is one of the mechanisms which modulates the activity of the enzymes or proteins in the apoptotic pathway. Indeed, S-nitration of a cysteine residue of caspase-3 inhibited apoptosis5. Cytochrome c induces apoptosis by translocation from the mitochondrial membrane to the cytoplasm followed by binding to the apoptotic protease activating factor-1 (Apaf-1) which activates caspases6. Nitration of cytochrome c in mitochondria or in cytosol after translocation may inhibit the caspase activation. Peroxynitrite, formed by reaction of NO with superoxide produced under oxidative stress, mediates nitration of several amino acid residues of proteins. Nitration of caspase-35ribonucleotide reductase7and cytochrome P450 2B18resulted in loss of catalytic activity. Interestingly, nitration of a cysteine residue of ovine PGHS-1 enhanced catalytic activity by alteration of the secondary structure of the enzyme9. In this study, we investigated the nitration of cytochrome c by peroxynitrite and PGHS-2 catalysis-dependent nitration of cytochrome c.
