Remodeling of an identified motoneuron during metamorphosis: central and peripheral actions of ecdysteroids during regression of dendrites and motor terminals.

L. M. Knittel, K. Kent
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引用次数: 6

Abstract

During metamorphosis of the moth Manduca sexta, an identified leg motoneuron, the femoral depressor motoneuron (FeDe MN), undergoes reorganization of its central and peripheral processes. This remodeling is under the control of two insect hormones: the ecdysteroids and juvenile hormone (JH). Here, we asked whether peripheral or central actions of the ecdysteroids influenced specific regressive aspects of MN remodeling. We used stable hormonal mimics to manipulate the hormonal environment of either the FeDe muscle or the FeDe MN soma. Our results demonstrate that motor-terminal retraction and dendritic regression can be experimentally uncoupled, indicating that central actions of ecdysteroids trigger dendritic regression whereas peripheral actions trigger terminal retraction. Our results further demonstrate that discrete aspects of motor-terminal retraction can also be experimentally uncoupled, suggesting that they also are regulated differently.
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在变态过程中一个已识别的运动神经元的重塑:在树突和运动终末退化过程中,皮质类固醇的中枢和外周作用。
在Manduca sexta蛾的变态过程中,一个确定的腿部运动神经元,股抑制运动神经元(FeDe MN),经历了其中央和外周过程的重组。这种重塑受两种昆虫激素的控制:表皮甾体激素和幼体激素。在这里,我们询问外周或中枢类固醇的作用是否影响MN重塑的特定退行性方面。我们使用稳定的激素模拟来操纵FeDe肌肉或FeDe MN体细胞的激素环境。我们的研究结果表明,运动-末端缩回和树突退化可以在实验上不耦合,这表明外源性类固醇的中枢作用触发树突退化,而外周作用触发末端缩回。我们的研究结果进一步表明,运动端收缩的离散方面也可以在实验上解耦,这表明它们也受到不同的调节。
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V Fenstermaker, Y Chen, A Ghosh, R Yuste. Regulation of dendritic length and branching by Semaphorin 3A, Journal of Neurobiology (2004) 58(3) 403–412 Synaptic inputs onto spiking local interneurons in crayfish are depressed by nitric oxide. Remodeling of an identified motoneuron during metamorphosis: central and peripheral actions of ecdysteroids during regression of dendrites and motor terminals. Role of Nova-1 in regulating alpha2N, a novel glycine receptor splice variant, in developing spinal cord neurons. Cloning of the cDNA and mRNA expression of CLRP, a complex leucine repeat protein of the Golgi apparatus expressed by specific neurons of the rat brain.
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