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首页> 外文期刊>Life sciences >Activation of formyl peptide receptor-like 1 by WKYMVm induces serine phosphorylation of STAT3, which inhibits its tyrosine phosphorylation and nuclear translocation induced by hydrogen peroxide
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Activation of formyl peptide receptor-like 1 by WKYMVm induces serine phosphorylation of STAT3, which inhibits its tyrosine phosphorylation and nuclear translocation induced by hydrogen peroxide

机译：WKYMVm激活甲酰肽受体样1诱导STAT3的丝氨酸磷酸化，从而抑制其酪氨酸磷酸化和过氧化氢诱导的核易位

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摘要

Signal transducer and activator of transcription 3 (STAT3) is an important transcription factor that modulates the expression of several genes. The activation of STAT3 accompanies tyrosine phosphorylation and its translocation to the nucleus. Formyl peptide receptor like 1 (FPRL1) is an important classical chemoattractant receptor. In this study, we observed that the stimulation of FPRL1 by Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm) caused serine phosphorylation but not tyrosine phosphorylation of STAT3 in a pertussis toxin-sensitive manner. Moreover, downstream of FPRL1 stimulation, phospholipase D (PLD) activity was dramatically increased. n-butanol, a well-known phosphatidic acid (PA) acceptor, completely inhibited WKYMVm-induced STAT3 serine phosphorylation. Moreover, the exogenous addition of PA mimicked STAT3 phosphorylation by WKYMVm. We also found that WKYMVm stimulated extracellular signal regulated kinase (ERK), and that ERK activity is required for STAT3 serine phosphorylation. This WKYMVm-induced ERK activation was inhibited by n-butanol, whereas ERK activation was also induced by the addition of exogenous PA. In terms of the functional aspects of the WKYMVm-induced serine phosphorylation of STAT3, we found that hydrogen peroxide-stimulated STAT3 activation was blocked by pretreating WKYMVm. Taken together, we found that WKYMVm stimulated FPRL1, and that this resulted in STAT3 serine phosphorylation via PLD-mediated ERK activation, and that the serine phosphorylation of STAT3 blocked hydrogen peroxide-induced STAT3 activity. (C) 2004 Elsevier Inc. All rights reserved.
机译：信号转导和转录激活因子3（STAT3）是调节几个基因表达的重要转录因子。 STAT3的激活伴随酪氨酸磷酸化及其易位至细胞核。甲酰基肽样受体1（FPRL1）是重要的经典化学引诱剂受体。在这项研究中，我们观察到Trp-Lys-Tyr-Met-Val-D-Met（WKYMVm）刺激FPRL1以百日咳毒素敏感的方式引起STAT3的丝氨酸磷酸化，但不引起酪氨酸磷酸化。此外，在FPRL1刺激的下游，磷脂酶D（PLD）活性显着增加。正丁醇，一种众所周知的磷脂酸（PA）受体，完全抑制WKYMVm诱导的STAT3丝氨酸磷酸化。此外，PA的外源添加模仿WKYMVm的STAT3磷酸化。我们还发现WKYMVm刺激细胞外信号调节激酶（ERK），并且STAT3丝氨酸磷酸化需要ERK活性。 WKYMVm诱导的ERK活化受到正丁醇的抑制，而ERK活化也受到外源PA的诱导。在WKYMVm诱导的STAT3丝氨酸磷酸化的功能方面，我们发现过氧化氢刺激的STAT3激活被WKYMVm预处理所阻断。两者合计，我们发现WKYMVm刺激FPRL1，并通过PLD介导的ERK激活导致STAT3丝氨酸磷酸化，并且STAT3的丝氨酸磷酸化阻止过氧化氢诱导的STAT3活性。 （C）2004 Elsevier Inc.保留所有权利。

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