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肌动蛋白结合蛋白,脑发育蛋白,与神经元分化同步在膜下区域积累。

Actin-binding protein, drebrin, accumulates in submembranous regions in parallel with neuronal differentiation.

作者信息

Asada H, Uyemura K, Shirao T

机构信息

Department of Physiology, School of Medicine, Keio University, Tokyo, Japan.

出版信息

J Neurosci Res. 1994 Jun 1;38(2):149-59. doi: 10.1002/jnr.490380205.

Abstract

Drebrins are developmentally regulated actin-binding proteins. In this study, we analyzed subcellular distribution of drebrin E in neuroblastoma cells (SH-SY5Y) in culture, especially in terms of its relationship to actin filaments. In undifferentiated cells, drebrin E was scattered as flocculus small dots along the stress fibers and also accumulated at adhesion plaques. In parallel with the neuronal differentiation following retinoic acid treatment, drebrin E was accumulated, accompanying filamentous (F) actin, in the submembranous cortical cytoplasm. Similar submembranous localization of drebrins was observed in primary cultured neurons. In the presence of drebrin E F-actin was more stable against cytochalasin D than F-actin lacking drebrin E. These results suggest that drebrin E plays a role in neuronal morphological differentiation by changing its subcellular localization with stabilized F-actin.

摘要

双调蛋白是受发育调控的肌动蛋白结合蛋白。在本研究中,我们分析了双调蛋白E在培养的神经母细胞瘤细胞(SH-SY5Y)中的亚细胞分布,特别是其与肌动蛋白丝的关系。在未分化细胞中,双调蛋白E沿应力纤维呈絮状小点分散分布,并且也聚集在黏着斑处。随着视黄酸处理后神经元的分化,双调蛋白E与丝状(F)肌动蛋白一起在膜下皮质细胞质中积累。在原代培养的神经元中也观察到双调蛋白类似的膜下定位。在存在双调蛋白E的情况下,F-肌动蛋白比缺乏双调蛋白E的F-肌动蛋白对细胞松弛素D更稳定。这些结果表明,双调蛋白E通过改变其亚细胞定位并稳定F-肌动蛋白,在神经元形态分化中发挥作用。

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