Alteration of myo-inositol monophosphatase in Alzheimer's disease brains

被引：18
|
作者：
Shimohama, S
Tanino, H
Sumida, Y
Tsuda, J
Fujimoto, S
机构：
[1] Kyoto Univ, Fac Med, Dept Neurol, Sakyo Ku, Kyoto 606, Japan
[2] Kyoto Pharmaceut Univ, Dept Environm Biochem, Yamashina Ku, Kyoto 607, Japan
来源：
NEUROSCIENCE LETTERS | 1998年 / 245卷 / 03期
关键词：
myo-inositol monophosphatase; myo-inositol; phospholipid metabolism; brain; human; Alzheimer's disease;
D O I：
10.1016/S0304-3940(98)00209-2
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
myo-Inositol monophosphatase (E.C.3.1.3.25) catalyzes the hydrolysis of myo-inositol 1-phosphate in the presence of Mg2+ at a physiologic pH to form free myo-inositol, maintaining a supply that represents the precursor for inositol phospholipid second messenger signaling systems. In the present study the activity and protein level of myo-inositol monophosphatase were investigated in samples from normal human and Alzheimer's disease (AD) postmortem brains. The separation profile on Sephadex G-100 gel filtration chromatography revealed one major form of myo-inositol monophosphatase in crude extracts from both normal human and AD brains. In AD brains myo-inositol monophosphatase activity and its protein level were significantly higher than in control brains. The activity of myo-inositol monophosphatase per enzyme molecule was similar in control and AD brains. These results suggest that myo-inositol monophosphatase is upregulated in AD, probably reflecting compensatory mechanisms concerned with phospholipid metabolism. (C) 1998 Elsevier Science Ireland Ltd.
引用
收藏
页码：159 / 162
页数：4
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