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神经节苷脂对膜酶活性的调节与膜微区中可能存在的神经节苷脂分离之间的关系。

Relationship between the regulation of membrane enzyme activities by gangliosides and a possible ganglioside segregation in membrane microdomains.

作者信息

Sonnino S, Chigorno V, Valsecchi M, Bassi R, Acquotti D, Cantu L, Corti M, Tettamanti G

机构信息

Department of Medical Chemistry and Biochemistry Medical School, University of Milan, Italy.

出版信息

Indian J Biochem Biophys. 1990 Dec;27(6):353-8.

PMID:2102479
Abstract

Laser and neutron scattering experiments showed that in mixed micelles of ganglioside GM2 and GT1b, a membrane mimicking system, the segregation of gangliosides may occur spontaneously. Photolabeling experiments using nitrophenylazide containing ganglioside GM1 proved that gangliosides added to cells in culture enter the cell and bind to its membrane as components of microdomains, which specifically interact with a protein of about 30 kDa. This suggests that ganglioside segregation may be a natural phenomenon. Gangliosides when added to granule cells in culture led to increase in protein phosphorylation, the effect exerted being related to the amount of ganglioside molecules inserted stably into the cell lipid layer and an increase of 0.7% of the cell original ganglioside content promoted an increase of 57% in the incorporation of 32P into cell membrane proteins. From the above results a possible relationship between ganglioside segregation and involvement of ganglioside in enzyme activity control is suggested.

摘要

激光和中子散射实验表明,在神经节苷脂GM2和GT1b的混合胶束(一种膜模拟系统)中,神经节苷脂可能会自发分离。使用含有硝基苯基叠氮化物的神经节苷脂GM1进行的光标记实验证明,添加到培养细胞中的神经节苷脂会进入细胞并作为微区的组成成分与细胞膜结合,这些微区会与一种约30 kDa的蛋白质发生特异性相互作用。这表明神经节苷脂的分离可能是一种自然现象。当将神经节苷脂添加到培养的颗粒细胞中时,会导致蛋白质磷酸化增加,其作用与稳定插入细胞脂质层的神经节苷脂分子数量有关,细胞原始神经节苷脂含量增加0.7%会促使32P掺入细胞膜蛋白的量增加57%。从上述结果可以推测神经节苷脂分离与神经节苷脂参与酶活性控制之间可能存在关联。

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Differential Anatomical Expression of Ganglioside GM1 Species Containing d18:1 or d20:1 Sphingosine Detected by MALDI Imaging Mass Spectrometry in Mature Rat Brain.通过基质辅助激光解吸电离成像质谱法检测成熟大鼠脑中含有d18:1或d20:1鞘氨醇的神经节苷脂GM1种类的差异解剖学表达。
Front Neuroanat. 2015 Dec 1;9:155. doi: 10.3389/fnana.2015.00155. eCollection 2015.