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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Activation of extracellular signal-regulated kinase ERK after hypo-osmotic stress in renal epithelial A6 cells
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Activation of extracellular signal-regulated kinase ERK after hypo-osmotic stress in renal epithelial A6 cells

机译:低渗应激后肾上皮A6细胞中细胞外信号调节激酶ERK的激活

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摘要

Activation of mitogen-activated protein (MAP) kinases has been reported to occur after a hypo-osmotic cell swelling in various types of cells. In renal epithelial A6 cells, the hypo-osmotic shock induced a rapid increase in the phosphorylation of an extracellular signal-regulated kinase (ERK)-like protein that was maximal 10 min after osmotic stress. Activation of ERK was significantly increased when hypo-osmotic stress was performed in the absence of extracellular Ca2+, a condition that inhibits regulatory volume decrease (RVD). Exposure of cells to PD98059, an inhibitor of the MAP kinase kinase MEK, at a concentration that fully cancelled ERK activation, did not inhibit RVD. On the contrary, RVD was abolished when osmotic shock was induced in the presence of SB203580, an inhibitor of stress-activated protein kinases (SAPKs). These results suggest that different MAP kinases are activated after hypo-osmotic stress in A6 cells. SAPKs would be involved in the control of RVD, while ERK would lead to later events, such as gene expression or energy metabolism. (C) 2004 Elsevier B.V. All rights reserved.
机译:据报道,在各种类型的细胞中低渗细胞膨胀后,发生了促分裂原活化蛋白(MAP)激酶的活化。在肾上皮A6细胞中,低渗性休克诱导细胞外信号调节激酶(ERK)样蛋白的磷酸化迅速增加,这在渗透胁迫后最大10分钟。在不存在细胞外Ca2 +的情况下进行低渗应激时,ERK的激活显着增加,这是抑制调节体积减少(RVD)的条件。以完全抵消ERK激活的浓度将细胞暴露于PD98059(一种MAP激酶激酶MEK的抑制剂)不会抑制RVD。相反,当在压力激活蛋白激酶(SAPKs)抑制剂SB203580的存在下诱导渗透性休克时,RVD消失。这些结果表明在低渗胁迫下,A6细胞中激活了不同的MAP激酶。 SAPKs将参与RVD的控制,而ERK将导致后来的事件,例如基因表达或能量代谢。 (C)2004 Elsevier B.V.保留所有权利。

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