Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1.
Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1.
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Peroxiredoxin II 充当 H2O2 激活的磷脂酶 D1 的信号终止子。
DOI：
10.1111/j.1742-4658.2005.04809.x
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Frohman,MichaelA
中科院分区：
文献类型：
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作者：
Xiao,Nianzhou;Du,Guangwei;Frohman,MichaelA
磷脂酶D1（PLD 1）是一种信号转导调节酶，可调节几种细胞内在过程，包括活化NAPDH氧化酶，从而提高细胞内H2 O2。已经报道了几种蛋白质在静息细胞中与PLD 1相互作用。我们试图鉴定在佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA）刺激后与PLD 1相互作用的蛋白质。通过PLD 1亲和下拉和MS鉴定了与过氧化物氧还蛋白II（PrxII）的新型相互作用，PrxII是一种消除细胞H2 O2的酶，H2 O2是PLD 1的已知刺激剂。PMA刺激证实可促进PLD 1和PrxII之间的物理相互作用，并导致PLD 1和PrxII在亚细胞内共定位。通过观察到PrxII的过表达特异性降低了PLD 1对H2 O2刺激的反应，提示了相互作用的功能意义。这些结果表明，PrxII可能通过在涉及产生H2 O2的细胞刺激后被募集到含有活化的PLD 1的位点而对PLD 1具有信号终止作用。
Phospholipase D1 (PLD1) is a signal‐transduction regulated enzyme which regulates several cell intrinsic processes including activation of NAPDH oxidase, which elevates intracellular H2O2. Several proteins have been reported to interact with PLD1 in resting cells. We sought to identify proteins that interact with PLD1 after phorbol 12‐myristate 13‐acetate (PMA) stimulation. A novel interaction with peroxiredoxin II (PrxII), an enzyme that eliminates cellular H2O2, which is a known stimulator of PLD1, was identified by PLD1‐affinity pull‐down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly. Functional significance of the interaction was suggested by the observation that over‐expression of PrxII specifically reduces the response of PLD1 to stimulation by H2O2. These results indicate that PrxII may have a signal‐terminating role for PLD1 by being recruited to sites containing activated PLD1 after cellular stimulation involving production of H2O2.