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首页> 外文期刊>The European Journal of Neuroscience >Large-scale study of phosphoproteins involved in long-term potentiation in the rat dentate gyrus in vivo.
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Large-scale study of phosphoproteins involved in long-term potentiation in the rat dentate gyrus in vivo.

机译：体内长期参与大鼠齿状回长时程增强的磷蛋白的大规模研究。

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The mechanisms underlying the induction of synaptic plasticity and the formation of long-term memory involve activation of cell-signalling cascades and protein modifications such as phosphorylation and dephosphorylation. Based on a protein candidate strategy, studies have identified several protein kinases and their substrates, which show an altered phosphorylation state during the early phases of long-term potentiation (LTP), yet only a limited number of synaptic phosphoproteins are known to be implicated in LTP. To identify new phosphoproteins associated with LTP, we have undertaken a proteomic study of phosphoproteins at different time points following the induction of LTP in the dentate gyrus in vivo (0, 15 and 90 min). For each time point, proteins from the dentate gyrus were separated by two-dimensional gel electrophoresis and stained with Pro-Q Diamond, a fluorescent stain specific for phosphoproteins. Fourteen proteins whose phosphorylation state varied significantly following LTP were identified using matrix-assisted laser desorption ionization/time of flight mass spectrometry and electrospray ionization-Orbitrap tandem mass spectrometry (MS/MS). They are involved in various cellular functions implicated in synaptic plasticity, such as intracellular signalling, axonal growth, exocytosis, protein synthesis and metabolism. Our results highlight new proteins whose phosphorylation or dephosphorylation is associated with LTP induction or maintenance. Further studies focusing on the regulation of specific phosphorylation sites will lead to greater understanding of the individual implications of these proteins in LTP as well as of their molecular interactions.
机译：诱导突触可塑性和长期记忆形成的机制涉及激活细胞信号级联反应和蛋白质修饰，例如磷酸化和去磷酸化。根据蛋白质候选策略，研究已经鉴定出几种蛋白激酶及其底物，这些蛋白激酶在长期增强（LTP）的早期阶段显示出磷酸化状态的改变，但是已知仅涉及有限数量的突触磷蛋白。 LTP。为了鉴定与LTP相关的新的磷蛋白，我们已经在体内齿状回中诱导LTP（0、15和90分钟）之后的不同时间点对磷蛋白进行了蛋白质组学研究。对于每个时间点，通过二维凝胶电泳分离来自齿状回的蛋白质，并用Pro-Q Diamond（对磷蛋白特异的荧光染料）染色。使用基质辅助激光解吸电离/飞行时间质谱和电喷雾电离-Orbitrap串联质谱（MS / MS）鉴定了LTP后磷酸化状态显着变化的14种蛋白质。它们参与与突触可塑性有关的各种细胞功能，例如细胞内信号转导，轴突生长，胞吐作用，蛋白质合成和代谢。我们的结果突出了新蛋白，其磷酸化或去磷酸化与LTP的诱导或维持有关。专注于特定磷酸化位点调控的进一步研究将导致人们进一步了解这些蛋白在LTP中的个体含义及其分子相互作用。

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