Search results for "Postsynaptic density"

showing 2 items of 12 documents

Low Density Lipoprotein Receptor-related Protein 1 (LRP1) Modulates N-Methyl-d-aspartate (NMDA) Receptor-dependent Intracellular Signaling and NMDA-i…

2013

The lipoprotein receptor LRP1 is essential in neurons of the central nervous system, as was revealed by the analysis of conditional Lrp1-deficient mouse models. The molecular basis of its neuronal functions, however, is still incompletely understood. Here we show by immunocytochemistry, electron microscopy, and postsynaptic density preparation that LRP1 is located postsynaptically. Basal and NMDA-induced phosphorylation of the transcription factor cAMP-response element-binding protein (CREB) as well as NMDA target gene transcription are reduced in LRP1-deficient neurons. In control neurons, NMDA promotes γ-secretase-dependent release of the LRP1 intracellular domain (LRP1-ICD). However, pul…

MaleN-MethylaspartateCell SurvivalBlotting WesternGene ExpressionMice Transgenicmacromolecular substancesAMPA receptorBiologyCREBReceptors N-Methyl-D-AspartateBiochemistryMiceNeurobiologyPostsynaptic potentialAnimalsMolecular BiologyCells CulturedMice KnockoutNeuronsReverse Transcriptase Polymerase Chain Reactionmusculoskeletal neural and ocular physiologyTumor Suppressor ProteinsMembrane ProteinsCell BiologyEmbryo MammalianLRP1Cell biologyProtein SubunitsReceptors LDLnervous systemSynapsesLDL receptorbiology.proteinNMDA receptorFemaleAmyloid Precursor Protein SecretasesSignal transductionDisks Large Homolog 4 ProteinGuanylate KinasesPostsynaptic densityLow Density Lipoprotein Receptor-Related Protein-1Protein BindingSignal TransductionSynaptosomesJournal of Biological Chemistry
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In‐depth protein profiling of the postsynaptic density from mouse hippocampus using data‐independent acquisition proteomics

2014

Located at neuronal terminals, the postsynaptic density (PSD) is a highly complex network of cytoskeletal scaffolding and signaling proteins responsible for the transduction and modulation of glutamatergic signaling between neurons. Using ion-mobility enhanced data-independent label-free LC-MS/MS, we established a reference proteome of crude synaptosomes, synaptic junctions, and PSD derived from mouse hippocampus including TOP3-based absolute quantification values for identified proteins. The final dataset across all fractions comprised 49 491 peptides corresponding to 4558 protein groups. Of these, 2102 protein groups were identified in highly purified PSD in at least two biological replic…

ProteomicsPost-Synaptic DensityProteinsHippocampal formationBiologyProteomicsHippocampusBiochemistryCell biologyMiceTransduction (genetics)Glutamatergicnervous systemProteomeAnimalsData-independent acquisitionCytoskeletonMolecular BiologyPostsynaptic densityPROTEOMICS
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