Activation of in situ tissue transglutaminase by intracellular reactive oxygen species
Activation of in situ tissue transglutaminase by intracellular reactive oxygen species
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DOI：
10.1016/s0006-291x(03)00835-0
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发表时间：
2003-06-06
影响因子：
3.1
通讯作者：
Ha, KS
中科院分区：
文献类型：
--
作者：
Lee, ZW;Kwon, SM;Ha, KS
我们在Swiss 3T3成纤维细胞中研究了细胞内活性氧（ROS）在溶血磷脂酸（LPA）和转化生长因子- β (tgf - β)激活原位组织转谷氨酰胺酶（tTGase）中的新功能。LPA诱导细胞内ROS的短暂增加，在10 min时达到最大值，这被ROS清除剂、n -乙酰- l-半胱氨酸和过氧化氢酶阻断。LPA对tTGase的激活作用在I时最大，而这一作用被胱胺和ROS清除剂所抑制。外源性H2O2活化tTGase孵育。tgf - β也能激活tTGase，并在2 h达到最大激活，而tTGase的激活被活性氧清除剂抑制。C3转移酶的剪贴加载抑制了ROS的产生和LPA和tgf - β对原位tTGase的激活，并且外源H2O2逆转了C3转移酶的抑制作用。微量注射GTPgammaS可抑制LPA、tgf - β和maitotoxin刺激的tTGase的转氨化活性。这些结果表明，在LPA和tgf - β的作用下，细胞内ROS对原位tTGase的激活至关重要。(C) 2003 Elsevier Science（美国）版权所有。
We have investigated the novel function of intracellular reactive oxygen species (ROS) in the activation of in situ tissue transglutaminase (tTGase) by lysophosphatidic acid (LPA) and transforming growth factor-beta (TGF-beta) in Swiss 3T3 fibroblasts. LPA induced a transient increase of intracellular ROS with a maximal increase at 10 min, which was blocked by ROS scavengers, N-acetyl-L-cysteine and catalase. LPA activated tTGase with a maximal increase at I It, which was inhibited by cystamine and ROS scavengers. Incubation with exogenous H2O2 activated tTGase. TGF-beta also activated tTGase with a maximal activation at 2 h and the tTGase activation was inhibited by the ROS scavengers. Scrape-loading of C3 transferase inhibited the ROS production and in situ tTGase activation by LPA and TGF-beta, and the inhibitory effect of C3 transferase was reversed by exogenous H2O2. Microinjection of GTPgammaS inhibited transamidating activity of tTGase stimulated by LPA, TGF-beta, and maitotoxin. These results suggested that intracellular ROS was essential for the activation of in situ tTGase in response to LPA and TGF-beta. (C) 2003 Elsevier Science (USA). All rights reserved.