Calpain-mediated degradation of PSD-95 in developing and adult rat brain

被引：62

作者：

Lu, XY ^{[1
]}

Rong, YQ ^{[1
]}

Baudry, M ^{[1
]}

机构：

[1] Univ So Calif, Neurosci Program, Los Angeles, CA 90089 USA

来源：

NEUROSCIENCE LETTERS | 2000年 / 286卷 / 02期

关键词：

PSD-95; calpain; spines; hippocampus; development; synaptic plasticity;

D O I：

10.1016/S0304-3940(00)01101-0

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

PSD-95 is a major postsynaptic density protein that is degraded as a result of synaptic activity. We used four different methods to test the hypothesis that calpain is involved in PSD-95 turnover. Treatment of synaptic membranes with purified calpain resulted in a decrease in immunoreactivity of the native 95 kDa protein and the appearance of two smaller molecular weight species, migrating at 50 and 36 kDa, respectively. Calcium treatment of frozen-thawed brain sections produced an identical digestion pattern, an effect blocked by calpain inhibitors. N-methyl-D-aspartate treatment of organotypic hippocampal cultures produced truncation of PSD-95 and accumulation of the 36 kDa species. Finally, calpain-generated degradation products of PSD95 were prominent in neonatal hippocampus, and disappeared with postnatal development. Our data suggest that PSD-95 is a substrate for calpain, and that calpain-mediated truncation contributes to PSD-95 turnover. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：149 / 153

页数：5

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