The organization of amyloid-β protein precursor intracellular domain-associated protein-1 in the rat forebrain
| Autor: | Richard J. Weinberg, Bryen A. Jordan, Amanda L. Jacob |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Male
Nuclear Envelope Nerve Tissue Proteins Biology Hippocampal formation Article Rats Sprague-Dawley Amyloid beta-Protein Precursor Postsynaptic potential medicine Neuropil Animals Neurons General Neuroscience Brain Nuclear Proteins Immunogold labelling Immunohistochemistry Cell biology Rats Microscopy Electron medicine.anatomical_structure Synapses Excitatory postsynaptic potential Nuclear Pore Carrier Proteins Neuroscience Nucleus Postsynaptic density Immunostaining Signal Transduction |
| DOI: | 10.17615/8fv6-7a48 |
| Popis: | Sustained activity-dependent synaptic modifications require protein synthesis. Although proteins can be synthesized locally in dendrites, long-term changes also require nuclear signaling. Amyloid-beta protein precursor intracellular domain-associated protein-1 (AIDA-1), an abundant component of the biochemical postsynaptic density fraction, contains a nuclear localization sequence, making it a plausible candidate for synapse-to-nucleus signaling. We used immunohistochemistry to study the regional, cellular, and subcellular distribution of AIDA-1. Immunostaining was prominent in the hippocampus, cerebral cortex, and neostriatum. Along with diffuse staining of neuropil, fluorescence microscopy revealed immunostaining of excitatory synapses throughout the forebrain, and immunoreactive puncta within and directly outside the nucleus. Presynaptic staining was conspicuous in hippocampal mossy fibers. Electron microscopic analysis of material processed for postembedding immunogold revealed AIDA-1 label within postsynaptic densities in both hippocampus and cortex. Together with previous work, these data suggest that AIDA-1 serves as a direct signaling link between synapses and the nucleus in adult rat brain. |
| Databáze: | OpenAIRE |
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