S-nitrosylation signaling in cell biology.
S-nitrosylation signaling in cell biology.
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DOI：
10.1124/mi.3.5.253
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发表时间：
2003-08-01
影响因子：
--
通讯作者：
Palmer, Lisa A
中科院分区：
文献类型：
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作者：
Gaston, Benjamin M;Carver, Jeannean;Palmer, Lisa A
S-Nitrosylated proteins form when a cysteine thiol reacts with nitric oxide (NO) in the presence of an electron acceptor to form an S-NO bond. Under physiological conditions, this posttranslational modification affects the function a wide array of cell proteins, ranging from ion channels to nuclear regulatory proteins. Recent evidence suggests that 1) S-nitrosylated proteins can be synthesized by exposure of specific redox-active motifs to NO, through transnitrosation/transfer reactions, or through metalloprotein-catalyzed reactions; 2) S-nitrosothiols can be sequestered in membranes, lipophilic protein folds, or in vesicles to preserve their activity; and 3) S-nitrosothiols can be degraded by a number of enzymes systems. These recent insights regarding the bioactivities, molecular signaling pathways, and metabolism of endogenous S-nitrosothiols have suggested several new therapies for disease ranging from cystic fibrosis to pulmonary hypertension.
