Neurotransmitter- and Growth Factor-Induced cAMP Response Element Binding Protein Phosphorylation in Glial Cell Progenitors: Role of Calcium Ions, Protein Kinase C, and Mitogen-Activated Protein Kinase/Ribosomal S6 Kinase Pathway
Neurotransmitter- and Growth Factor-Induced cAMP Response Element Binding Protein Phosphorylation in Glial Cell Progenitors: Role of Calcium Ions, Protein Kinase C, and Mitogen-Activated Protein Kinase/Ribosomal S6 Kinase Pathway
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神经递质和生长因子诱导的 cAMP 响应元件结合蛋白在胶质细胞祖细胞中磷酸化：钙离子、蛋白激酶 C 和丝裂原激活蛋白激酶/核糖体 S6 激酶途径的作用
DOI：
10.1523/jneurosci.17-04-01291.1997
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
V. Gallo
中科院分区：
文献类型：
--
作者：
M. Pende;T. Fisher;P. B. Simpson;J. Russell;J. Blenis;V. Gallo
为了了解细胞外信号如何在神经细胞中产生长期影响，我们分析了神经递质和生长因子诱导皮质少突胶质细胞祖细胞（OP）中转录因子cAMP反应元件结合蛋白（CREB）磷酸化的机制。红藻氨酸激活谷氨酸受体通道，卡巴胆碱刺激G蛋白偶联胆碱能受体，碱性成纤维细胞生长因子（bFGF）刺激酪氨酸激酶受体，迅速导致丝裂原活化蛋白激酶（MAPK）磷酸化和核糖体S6激酶（RSK）激活。红藻氨酸和卡巴胆碱激活MAPK途径需要细胞外钙内流，并伴有蛋白激酶C（PKC）诱导，没有显着增加GTP结合Ras。相反，生长因子刺激的MAPK磷酸化不依赖于细胞外钙离子，并伴有Ras激活。OP细胞的MAPK活性受胞浆钙离子水平的影响，如它们对钙离子螯合剂双（2-氨基苯氧基）乙烷-N，N，N′，N′-四乙酸的敏感性所示。CREB磷酸化的动力学响应于各种激动剂对应于MAPK激活。此外，CREB磷酸化和MAPK活化类似地受到钙离子的影响。MEK抑制剂PD 098059选择性地阻止MAPK通路的激活，强烈地减少了红藻氨酸、卡巴胆碱、bFGF和佛波醇酯TPA对CREB磷酸化的诱导。我们建议，在OP的MAPK/RSK途径介导CREB磷酸化响应钙内流，PKC激活，和生长因子的刺激。
To understand how extracellular signals may produce long-term effects in neural cells, we have analyzed the mechanism by which neurotransmitters and growth factors induce phosphorylation of the transcription factor cAMP response element binding protein (CREB) in cortical oligodendrocyte progenitor (OP) cells. Activation of glutamate receptor channels by kainate, as well as stimulation of G-protein-coupled cholinergic receptors by carbachol and tyrosine kinase receptors by basic fibroblast growth factor (bFGF), rapidly leads to mitogen-activated protein kinase (MAPK) phosphorylation and ribosomal S6 kinase (RSK) activation. Kainate and carbachol activation of the MAPK pathway requires extracellular calcium influx and is accompanied by protein kinase C (PKC) induction, with no significant increase in GTP binding to Ras. Conversely, growth factor-stimulated MAPK phosphorylation is independent of extracellular calcium and is accompanied by Ras activation. Both basal and stimulated MAPK activity in OP cells are influenced by cytoplasmic calcium levels, as shown by their sensitivity to the calcium chelator bis(2-aminophenoxy)ethane-N,N,N′,N′-tetra-acetic acid. The kinetics of CREB phosphorylation in response to the various agonists corresponds to that of MAPK activation. Moreover, CREB phosphorylation and MAPK activation are similarly affected by calcium ions. The MEK inhibitor PD 098059, which selectively prevents activation of the MAPK pathway, strongly reduces induction of CREB phosphorylation by kainate, carbachol, bFGF, and the phorbol ester TPA. We propose that in OPs the MAPK/RSK pathway mediates CREB phosphorylation in response to calcium influx, PKC activation, and growth factor stimulation.
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DOI：
--
发表时间：
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发表时间：
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影响因子：
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期刊：
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
影响因子：
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作者：
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