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The Journal of Neuroscience, January 4, 2012 32(1):381 389 381 Cellular/Molecular Impairment of Catecholamine Systems during Induction of Long-Term Potentiating at Hippocampus CA1 Synapses in HPC-1/Syntax

Since HPC-1/syntax is expressed at both synaptic vesicles and postsynaptic sites, the question was whether HPC-1/syntax inhibition during the early stages of LAP would affect HPC-1-dependent synaptic plasticity by altering the cellular and molecular mechanisms relevant to the maintenance of LAP. We found that HPC-1 inhibited the generation of long-term potentiating (LAP) through induction of the catecholamine neurotransmitter synthesis gene Cyp6a1, which is a member of the cysteine transporters. In addition, HPC-1 inhibited the cellular activity of Cyp6a1 in a variety of hippocampus neuronal cultures and in cultured HPC-1/syntax-activated neurons in vitro, demonstrating that HPC-1 inhibition of the protein synthase and phosphorylation of Cyp6a1 is not confined to specific synapses. These results indicate that HPC-1 is crucial for synapse formation and LAP induction during the early stages of LAP induction and suggest that HPC-1 inhibition is involved in synaptic plasticity at both glutamatergic and Allergic synapses. In the above study, we investigated the involvement of different aspects of synaptic pruning in the maintenance of synaptic plasticity and learning in Drosophila. We found that both the synaptic plasticity and learning in Drosophila involved the induction of a protein called Cyp6a1 within long-term potentiating complexes (TPC). HPC-1 inhibited Cyp6a1 in hippocampus neurons (n = 18) cultured in culture medium and in hippocampus cell lines (N2a-1, A375, A375-B, and HPC-1). Cyp6a1 was a homologous of Cyp5g1 and was synthesized by Cyp6a1-containing BV-2 pyramidal neurons along with other glutamate receptors. To determine whether Cyp6a1 expression or activity was regulated during early stages of LAP, we analyzed synaptic formation in the CA1 area of the hippocampus. We found that long-term, LAP is induced by long-term stimulation at CA1 synapses.

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