脓毒症患者体内表达的诱导型一氧化氮合酶（NOS2）在特定酪氨酸残基上发生硝化：对酶活性的影响。
Inducible nitric oxide synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: implications for enzymic activity.
作者信息
Lanone Sophie, Manivet Philippe, Callebert Jacques, Launay Jean-Marie, Payen Didier, Aubier Michel, Boczkowski Jorge, Mebazaa Alexandre
机构信息
Institut National de la Santé et de la Recherche Médicale (INSERM) U408 and IFR 02, Faculté X. Bichat, 75018 Paris, France.
出版信息
Biochem J. 2002 Sep 1;366(Pt 2):399-404. doi: 10.1042/BJ20020339.
Abstract
Tyrosine nitration is a post-translational protein modification with potentially significant biological implications. In the present study we demonstrate, for the first time, that tyrosine residues of human inducible nitric oxide synthase (NOS2) can be nitrated by peroxynitrite in vitro, leading to a decreased activity. Moreover, we show that NOS2 expressed in a skeletal muscle from septic patients is nitrated on selective tyrosine residues belonging to a canonic sequence. This phenomenon could be an endogenous mechanism of in vivo modulation of NOS2 enzymic activity.
摘要
酪氨酸硝化是一种具有潜在重大生物学意义的翻译后蛋白质修饰。在本研究中，我们首次证明，人诱导型一氧化氮合酶（NOS2）的酪氨酸残基在体外可被过氧亚硝酸盐硝化，导致活性降低。此外，我们表明，脓毒症患者骨骼肌中表达的NOS2在属于一个典型序列的选择性酪氨酸残基上被硝化。这种现象可能是体内调节NOS2酶活性的一种内源性机制。
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