Proteolysis of cell adhesion molecules by serine proteases: a role in long term potentiation?
Proteolysis of cell adhesion molecules by serine proteases: a role in long term potentiation?
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DOI：
10.1016/s0006-8993(98)00906-8
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发表时间：
1998-11-16
期刊：
影响因子：
2.9
通讯作者：
Lynch, G
中科院分区：
文献类型：
--
作者：
Hoffman, KB;Martinez, J;Lynch, G
组织纤溶酶原激活剂 (tPA) 是一种海马神经元内源性丝氨酸蛋白酶，可识别细胞粘附分子 (CAM) 胞外域中的高度保守序列。当添加到大脑匀浆中时，tPA 产生的 CAM 片段大小与通过短暂的 NMDA 受体刺激在海马切片中产生的片段相似。丝氨酸蛋白酶抑制剂 4-(2-氨基乙基)-苯磺酰氟可阻断 tPA 的作用，在 250 μM 时抑制约 50%。该浓度的抑制剂对突触反应没有明显影响，但导致长期增强作用在 1 小时内衰减回到基线。这些结果表明，由 NMDA 受体引发并由丝氨酸蛋白酶介导的细胞粘附分子的细胞外分解有助于稳定增强的形成。 (C) 1998 年由 Elsevier Science B.V. 出版。保留所有权利。
Tissue plasminogen activator (tPA), a serine protease endogenous to hippocampal neurons, is shown to recognize a highly conserved sequence in the extracellular domain of cell adhesion molecules (CAMs). When added to brain homogenates, tPA generated a CAM fragment similar in size to that produced in hippocampal slices by brief periods of NMDA receptor stimulation. The serine protease inhibitor 4-(2-Aminoethyl)-benzenesulfonyl fluoride blocked the effects of tPA with an approximately 50% suppression at 250 mu M. The inhibitor at this concentration had no evident effect on synaptic responses but caused long term potentiation to decay back to baseline over a 1 h period. These results suggest that extracellular breakdown of cell adhesion molecules initiated by NMDA receptors and mediated by serine proteases contributes to the formation of stable potentiation. (C) 1998 Published by Elsevier Science B.V. All rights reserved.