Change in Membrane Permeability Induced by Amyloid β-Protein Fragment 25 - 35 in Brain Neurons Dissociated from Rats

The Japanese Journal of Pharmacology

Yoshiko Hatakeyama¹  Toshiko Ueha¹  Lumi Chikahisa²  Yasuo Oyama¹  Takuya Kokubun³ 

[1] Laboratory of Cell Signaling (Pharmacology), Faculty of Integrated Arts and Sciences, The University of Tokushima;Taiho Pharmaceutical Co.;Meridian Instruments Far East, Inc.

关键词: Amyloid β-protein;    Brain neuron;    Intracellular Ca2+;    Membrane permeability;    Viability;   

DOI  :  10.1254/jjp.68.77

学科分类：药理学

来源: Nihon Yakuri Gakkai Henshuubu / Japanese Pharmacological Society

【 摘 要 】

References(17)Cited-By(29)Effects of amyloid β-protein fragment 25 - 35, AβP(3P(25 - 35), on the membrane permeability of organic molecules were examined in the brain neurons dissociated from rats by using an argon laser (equipped in flow cytometer and laser microscope) and a combination of two fluorescent dyes, fluo-3-AM and ethidium bromide. AβP(25 - 35) at concentrations of 1 μM or greater induced both leakage of fluo-3 from the neurons and permeation of ethidium across the membrane in a dose-dependent manner, although both dyes are highly impermeant to the intact plasma membrane. Thus, AβP(25 - 35) seems to increase not only membrane permeability of inorganic ions such as Ca2+, Na+ and K+, as previously suggested, but also that of organic molecules. Therefore, the brain neuron membrane is suggested to lose its integrity in the presence of AβP(25 - 35) that leads to neuronal death.

【 授权许可】

Unknown