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神经节苷脂/蛋白激酶信号触发细胞骨架肌动蛋白重组。

Ganglioside/protein kinase signals triggering cytoskeletal actin reorganization.

作者信息

Higashi Hideyoshi, Chen Nai Hong

机构信息

Mitsubishi Kagaku Institute of Life Sciences,11-Go Minamioya, Machida, Tokyo 194-8511, Japan.

出版信息

Glycoconj J. 2004;20(1):49-58. doi: 10.1023/B:GLYC.0000016742.88750.1a.

Abstract

Exposure of neuronal cells to nanomolar concentrations of oligosaccharide portions of ganglioside GM2 and GT1b stimulates cAMP-dependent protein kinase (PKA) Ca2+/calmodulin-dependent protein kinase II (CaMKII), respectively, in a few seconds suggesting the presence of glyco-receptor-like molecules on the surface of the cells. Both GM2/PKA (GalNAc/PKA) and GT1b/CaMKII signaling cascades induced cytoskeletal actin reorganization through Cdc42 activation leading to filopodia formation within 2 min. Long-term effects of these glyco-signals were facilitation of dendritic differentiation of primary cultured hippocampal neurons and cerebellar Purkinje neurons indicating physiological roles of the signals in neuronal differentiation and maturation.

摘要

将神经细胞暴露于纳摩尔浓度的神经节苷脂GM2和GT1b的寡糖部分,分别在几秒钟内刺激环磷酸腺苷依赖性蛋白激酶(PKA)和钙/钙调蛋白依赖性蛋白激酶II(CaMKII),这表明细胞表面存在糖受体样分子。GM2/PKA(N-乙酰半乳糖胺/PKA)和GT1b/CaMKII信号级联通过激活Cdc42诱导细胞骨架肌动蛋白重组,从而在2分钟内导致丝状伪足形成。这些糖信号的长期作用是促进原代培养的海马神经元和小脑浦肯野神经元的树突分化,表明这些信号在神经元分化和成熟中具有生理作用。

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