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Reduced hippocampal LTP in mice lacking a presynaptic protein: complexin II
Author(s) -
Takahashi Seiichi,
Ujihara Hisamitsu,
Huang GuangZhe,
Yagyu Kenichi,
Sanbo Makoto,
Kaba Hideto,
Yagi Takeshi
Publication year - 1999
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.1460-9568.1999.00652.x
Subject(s) - long term potentiation , neurotransmission , neural facilitation , neuroscience , exocytosis , synaptic vesicle , neurotransmitter , biology , munc 18 , synaptic plasticity , hippocampal formation , snare complex , microbiology and biotechnology , receptor , vesicle , endocrinology , biochemistry , central nervous system , membrane , secretion
The SNAP receptor (SNARE) complex is a core complex specialized for synaptic vesicle exocytosis, and the binding of SNAPs to the complex is an essential step for neurotransmitter release. Complexin I and II have been identified as SNARE‐complex‐associated proteins. Importantly, complexins compete with α‐SNAP for binding to the complex, suggesting that complexins may modulate neurotransmitter release process. To examine this possibility and to understand the physiological function of complexins, we generated complexin II knockout mice. The complexin‐II‐deficient mice (–/–) were viable and fertile, and appeared normal. Electrophysiological recordings in the mutant hippocampus showed that ordinary synaptic transmission and paired‐pulse facilitation, a form of short‐term synaptic plasticity, were normal. However, long‐term potentiation (LTP) in both CA1 and CA3 regions was impaired, suggesting that complexin II may not be essential for synaptic vesicle exocytosis, but it does have a role in the establishment of hippocampal LTP.