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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2000-5-25
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pubmed:abstractText |
Protein phosphatase inhibitor-1 (I-1) has been proposed as a regulatory element in the signal transduction cascade that couples postsynaptic calcium influx to long-term changes in synaptic strength. We have evaluated this model using mice lacking I-1. Recordings made in slices prepared from mutant animals and also in anesthetized mutant animals indicated that long-term potentiation (LTP) is deficient at perforant path-dentate granule cell synapses. In vitro, this deficit was restricted to synapses of the lateral perforant path. LTP at Schaffer collateral-CA1 pyramidal cell synapses remained normal. Thus, protein phosphatase-1-mediated regulation of NMDA receptor-dependent synaptic plasticity involves heterogeneous molecular mechanisms, in both different dendritic subregions and different neuronal subtypes. Examination of the performance of I-1 mutants in spatial learning tests indicated that intact LTP at lateral perforant path-granule cell synapses is either redundant or is not involved in this form of learning.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1529-2401
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pubmed:author |
pubmed-author:AllenP BPB,
pubmed-author:AndersenPP,
pubmed-author:BlissT VTV,
pubmed-author:ChaudhryF AFA,
pubmed-author:ErringtonM LML,
pubmed-author:GreengardPP,
pubmed-author:HvalbyOO,
pubmed-author:JensenVV,
pubmed-author:MorrisR GRG,
pubmed-author:RamsayMM,
pubmed-author:Storm-MathisenJJ
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3537-43
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10804194-Animals,
pubmed-meshheading:10804194-Carrier Proteins,
pubmed-meshheading:10804194-Dentate Gyrus,
pubmed-meshheading:10804194-Excitatory Postsynaptic Potentials,
pubmed-meshheading:10804194-Female,
pubmed-meshheading:10804194-Gene Expression,
pubmed-meshheading:10804194-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10804194-Long-Term Potentiation,
pubmed-meshheading:10804194-Male,
pubmed-meshheading:10804194-Maze Learning,
pubmed-meshheading:10804194-Mice,
pubmed-meshheading:10804194-Mice, Inbred C57BL,
pubmed-meshheading:10804194-Mice, Mutant Strains,
pubmed-meshheading:10804194-Neuronal Plasticity,
pubmed-meshheading:10804194-Perforant Pathway,
pubmed-meshheading:10804194-Phosphoprotein Phosphatases,
pubmed-meshheading:10804194-Phosphoproteins,
pubmed-meshheading:10804194-Protein Phosphatase 1,
pubmed-meshheading:10804194-Pyramidal Cells,
pubmed-meshheading:10804194-RNA-Binding Proteins,
pubmed-meshheading:10804194-Space Perception,
pubmed-meshheading:10804194-Synapses,
pubmed-meshheading:10804194-Water
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pubmed:year |
2000
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pubmed:articleTitle |
Protein phosphatase-1 regulation in the induction of long-term potentiation: heterogeneous molecular mechanisms.
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pubmed:affiliation |
Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, NY 10021, USA. allenp@rickvax.rockefeller.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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