Linked Life Data

11739565

Source:http://linkedlifedata.com/resource/pubmed/id/11739565

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2001-12-12
pubmed:abstractText
The ability of neurons to modify synaptic connections based on activity is essential for information processing and storage in the brain. The induction of long-lasting changes in synaptic strength requires new protein synthesis and is often mediated by NMDA-type glutamate receptors (NMDARs). We used a dark-rearing paradigm to examine mRNA translational regulation in the visual cortex after visual experience-induced synaptic plasticity. In this model system, we demonstrate that visual experience induces the translation of mRNA encoding the alpha-subunit of calcium/calmodulin-dependent kinase II in the visual cortex. Furthermore, this increase in translation is NMDAR dependent. One potential source for newly synthesized proteins is the translational activation of dormant cytoplasmic mRNAs. To examine this possibility, we developed a culture-based assay system to study translational regulation in neurons. Cultured hippocampal neurons were transfected with constructs encoding green fluorescent protein (GFP). At 6 hr after transfection, approximately 35% of the transfected neurons (as determined by in situ hybridization) expressed detectable GFP protein. Glutamate stimulation of the cultures at this time induced an increase in the number of neurons expressing GFP protein that was NMDAR dependent. Importantly, the glutamate-induced increase was only detected when the 3'-untranslated region of the GFP constructs contained intact cytoplasmic polyadenylation elements (CPEs). Together, these findings define a molecular mechanism for activity-dependent synaptic plasticity that is mediated by the NMDA receptor and requires the CPE-dependent translation of an identified mRNA.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9541-8
pubmed:dateRevised
2011-9-22
pubmed:meshHeading
pubmed-meshheading:11739565-3' Untranslated Regions, pubmed-meshheading:11739565-Animals, pubmed-meshheading:11739565-Calcium-Calmodulin-Dependent Protein Kinase Type 2, pubmed-meshheading:11739565-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:11739565-Cells, Cultured, pubmed-meshheading:11739565-Darkness, pubmed-meshheading:11739565-Excitatory Amino Acid Agonists, pubmed-meshheading:11739565-Gene Expression Regulation, pubmed-meshheading:11739565-Glutamic Acid, pubmed-meshheading:11739565-Green Fluorescent Proteins, pubmed-meshheading:11739565-Luminescent Proteins, pubmed-meshheading:11739565-Neuronal Plasticity, pubmed-meshheading:11739565-Neurons, pubmed-meshheading:11739565-Photic Stimulation, pubmed-meshheading:11739565-Polyadenylation, pubmed-meshheading:11739565-Protein Biosynthesis, pubmed-meshheading:11739565-RNA, Messenger, pubmed-meshheading:11739565-Rats, pubmed-meshheading:11739565-Rats, Long-Evans, pubmed-meshheading:11739565-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:11739565-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:11739565-Sensory Deprivation, pubmed-meshheading:11739565-Synapses, pubmed-meshheading:11739565-Transfection, pubmed-meshheading:11739565-Visual Cortex
pubmed:year
2001
pubmed:articleTitle
A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons.
pubmed:affiliation
Department of Neuroscience, Brown University, Providence, Rhode Island 02912, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't