Localization and Subcellular Distribution ofN-Copine in Mouse Brain
| Autor: | Takashi Nakayama, Goro Kuwajima, Takeshi Yaoi |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
rab3 GTP-Binding Proteins
Gene Expression Hippocampus Nerve Tissue Proteins Kainate receptor Biology Hippocampal formation Biochemistry Mice Synaptotagmins Cellular and Molecular Neuroscience GTP-Binding Proteins Postsynaptic potential Animals Premovement neuronal activity RNA Messenger In Situ Hybridization Brain Chemistry Membrane Glycoproteins Neuronal Plasticity Pyramidal Cells Calcium-Binding Proteins Synaptotagmin I Membrane Proteins Long-term potentiation Immunohistochemistry Olfactory Bulb Cell biology nervous system Dentate Gyrus Synaptic plasticity Calcium Carrier Proteins Neuroscience Subcellular Fractions |
| Zdroj: | Journal of Neurochemistry. 72:373-379 |
| ISSN: | 0022-3042 |
| DOI: | 10.1046/j.1471-4159.1999.0720373.x |
| Popis: | N-Copine is a novel protein with two C2 domains. Its expression is brain specific and up-regulated by neuronal activity such as kainate stimulation and tetanus stimulation evoking hippocampal CA1 long-term potentiation. We examined the localization and subcellular distribution of N-copine in mouse brain. In situ hybridization analysis showed that N-copine mRNA was expressed exclusively in neurons of the hippocampus and in the main and accessory olfactory bulb, where various forms of synaptic plasticity and memory formation are known to occur. In immunohistochemical analyses, N-copine was detected mainly in the cell bodies and dendrites in the neurons, whereas presynaptic proteins such as synaptotagmin I and rab3A were detected in the regions where axons pass through. In fractionation experiments of brain homogenate, N-copine was associated with the membrane fraction in the presence of Ca2+ but not in its absence. As a GST-fusion protein with the second C2 domain of N-copine showed Ca2+ -dependent binding to phosphatidylserine, this domain was considered to be responsible for the Ca2+ -dependent association of N-copine with the membrane. Thus, N-copine may have a role as a Ca2+ sensor in postsynaptic events, in contrast to the known roles of “double C2 domain-containing proteins,” including synaptotagmin I, in presynaptic events. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text