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神经轴蛋白,一种大鼠中枢神经系统中新型的假定结构蛋白,在免疫方面与微管相关蛋白5相关。

Neuraxin, a novel putative structural protein of the rat central nervous system that is immunologically related to microtubule-associated protein 5.

作者信息

Rienitz A, Grenningloh G, Hermans-Borgmeyer I, Kirsch J, Littauer U Z, Prior P, Gundelfinger E D, Schmitt B, Betz H

机构信息

ZMBH, Center for Molecular Biology, University of Heidelberg, FRG.

出版信息

EMBO J. 1989 Oct;8(10):2879-88. doi: 10.1002/j.1460-2075.1989.tb08436.x.

Abstract

During screening of a rat spinal cord lambda gt11 cDNA library with poly- and monoclonal antibodies against the postsynaptic glycine receptor a cDNA was isolated which covers an open reading frame encoding a protein of calculated mol. wt 94 kd. Sequence analysis identified a novel type of neuron-specific protein (named neuraxin) which is characterized by an unusual amino acid composition, 12 central heptadecarepeats and putative protein and/or membrane interaction sites. The gene encoding neuraxin appears to be unique in the haploid rat genome and conserved in higher vertebrates. Northern blot and in situ hybridization revealed neuraxin mRNA to be expressed throughout the rodent central nervous system (CNS). In spinal cord, neuraxin transcripts were abundant in motoneurons which also expressed glycine receptor subunit mRNA. A bacterial fusion protein containing approximately 90% of the neuraxin sequence was found to specifically bind tubulin. Polyclonal neuraxin antibodies cross-reacted with microtubule-associated protein 5 (MAP5), and a monoclonal antibody against MAP5 recognized the neuraxin fusion construct. Based on these data we suggest that neuraxin is related to MAP5 and may be implicated in neuronal membrane-microtubule interactions.

摘要

在用抗突触后甘氨酸受体的多克隆和单克隆抗体筛选大鼠脊髓λgt11 cDNA文库的过程中,分离出了一个cDNA,它包含一个开放阅读框,编码一种计算分子量为94kd的蛋白质。序列分析鉴定出一种新型的神经元特异性蛋白质(命名为神经轴蛋白),其特征在于氨基酸组成异常、12个中央十七肽重复序列以及假定的蛋白质和/或膜相互作用位点。编码神经轴蛋白的基因在单倍体大鼠基因组中似乎是独特的,并且在高等脊椎动物中保守。Northern印迹和原位杂交显示神经轴蛋白mRNA在整个啮齿动物中枢神经系统(CNS)中表达。在脊髓中,神经轴蛋白转录本在运动神经元中丰富,这些运动神经元也表达甘氨酸受体亚基mRNA。发现一种包含约90%神经轴蛋白序列的细菌融合蛋白能特异性结合微管蛋白。多克隆神经轴蛋白抗体与微管相关蛋白5(MAP5)发生交叉反应,并且一种针对MAP5的单克隆抗体识别神经轴蛋白融合构建体。基于这些数据,我们认为神经轴蛋白与MAP5相关,并且可能参与神经元膜-微管相互作用。

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