S-nitrosylation of proteins: a new insight into endothelial cell function regulated by eNOS-derived NO.

S-nitrosylation of proteins: a new insight into endothelial cell function regulated by eNOS-derived NO.
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DOI:
10.1016/j.niox.2011.04.014
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发表时间:
2011-08-01
期刊:
Nitric oxide : biology and chemistry
影响因子:
--
通讯作者:
Iwakiri Y
Iwakiri Y
中科院分区:
其他
文献类型:
--
作者:
Iwakiri Y

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一氧化氮(NO)是一种高度扩散和短暂的信使分子。尽管这两个特征似乎不适合细胞内反应,但NO通过S-亚硝基化机制调节多种细胞过程。决定S-亚硝基化作为信号传导机制的特异性的一个重要因素是一氧化氮合酶(NOS)与其靶蛋白的区室化。内皮型一氧化氮合酶(eNOS)是唯一的NOS家族成员,主要定位在特定的细胞内膜结构域,包括高尔基体的细胞质面和质膜小窝。由位于高尔基体上的eNOS产生的一氧化氮可以通过氧化还原机制与附近高尔基体蛋白上的巯基反应,导致这些蛋白质的S-亚硝基化。这种修饰影响它们作为细胞过程如蛋白质运输(例如,胞吐作用和胞吞作用)、氧化还原状态和细胞周期。因此,eNOS衍生的NO调节广泛的内皮细胞功能,如炎症、凋亡、渗透性、迁移和细胞生长。
Nitric oxide (NO) is a messenger molecule that is highly diffusible and short-lived. Despite these two characteristics, seemingly unsuitable for intracellular reactions, NO modulates a variety of cellular processes via the mechanism of S-nitrosylation. An important factor that determines the specificity of S-nitrosylation as a signaling mechanism is the compartmentalization of nitric oxide synthase (NOS) with its target proteins. Endothelial NOS (eNOS) is unique among the NOS family members by being localized mainly near specific intracellular membrane domains including the cytoplasmic face of the Golgi apparatus and plasma membrane caveolae. Nitric oxide produced by eNOS localized on the Golgi apparatus can react with thiol groups on nearby Golgi proteins via a redox mechanism resulting in S-nitrosylation of these proteins. This modification influences their function as regulators of cellular processes such as protein trafficking (e.g., exocytosis and endocytosis), redox state, and cell cycle. Thus, eNOS-derived NO regulates a wide range of endothelial cell functions, such as inflammation, apoptosis, permeability, migration and cell growth.
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