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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2005-10-27
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pubmed:abstractText |
Cbln1 is a cerebellum-specific protein of previously unknown function that is structurally related to the C1q and tumor necrosis factor families of proteins. We show that Cbln1 is a glycoprotein secreted from cerebellar granule cells that is essential for three processes in cerebellar Purkinje cells: the matching and maintenance of pre- and postsynaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Notably, the phenotype of cbln1-null mice mimics loss-of-function mutations in the orphan glutamate receptor, GluR delta2, a gene selectively expressed in Purkinje neurons. Therefore, Cbln1 secreted from presynaptic granule cells may be a component of a transneuronal signaling pathway that controls synaptic structure and plasticity.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
Nov
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pubmed:issn |
1097-6256
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pubmed:author |
pubmed-author:BaoDashiD,
pubmed-author:HiraiHirokazuH,
pubmed-author:LiLeyiL,
pubmed-author:MiuraErikoE,
pubmed-author:MiyazakiTaisukeT,
pubmed-author:MorganJames IJI,
pubmed-author:PangZhenZ,
pubmed-author:ParrisJenniferJ,
pubmed-author:RongYongqiY,
pubmed-author:WatanabeMasahikoM,
pubmed-author:YuzakiMichisukeM
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1534-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16234806-Age Factors,
pubmed-meshheading:16234806-Analysis of Variance,
pubmed-meshheading:16234806-Animals,
pubmed-meshheading:16234806-Animals, Newborn,
pubmed-meshheading:16234806-Ataxia,
pubmed-meshheading:16234806-Behavior, Animal,
pubmed-meshheading:16234806-Blotting, Northern,
pubmed-meshheading:16234806-Blotting, Western,
pubmed-meshheading:16234806-Cells, Cultured,
pubmed-meshheading:16234806-Cerebellum,
pubmed-meshheading:16234806-Cloning, Molecular,
pubmed-meshheading:16234806-Dendritic Spines,
pubmed-meshheading:16234806-Dose-Response Relationship, Radiation,
pubmed-meshheading:16234806-Electric Stimulation,
pubmed-meshheading:16234806-Excitatory Postsynaptic Potentials,
pubmed-meshheading:16234806-Gene Expression Regulation,
pubmed-meshheading:16234806-Humans,
pubmed-meshheading:16234806-In Situ Hybridization,
pubmed-meshheading:16234806-Membrane Potentials,
pubmed-meshheading:16234806-Mice,
pubmed-meshheading:16234806-Mice, Inbred ICR,
pubmed-meshheading:16234806-Mice, Transgenic,
pubmed-meshheading:16234806-Microscopy, Electron, Transmission,
pubmed-meshheading:16234806-Motor Activity,
pubmed-meshheading:16234806-Mutagenesis,
pubmed-meshheading:16234806-Nerve Tissue Proteins,
pubmed-meshheading:16234806-Neuronal Plasticity,
pubmed-meshheading:16234806-Neurons,
pubmed-meshheading:16234806-Patch-Clamp Techniques,
pubmed-meshheading:16234806-Protein Precursors,
pubmed-meshheading:16234806-RNA, Messenger,
pubmed-meshheading:16234806-Radioimmunoassay,
pubmed-meshheading:16234806-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:16234806-Synapses,
pubmed-meshheading:16234806-Transfection,
pubmed-meshheading:16234806-Vesicular Glutamate Transport Protein 2
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pubmed:year |
2005
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pubmed:articleTitle |
Cbln1 is essential for synaptic integrity and plasticity in the cerebellum.
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pubmed:affiliation |
Department of Developmental Neurobiology, St. Jude Children's Research Hospital, 332 North Lauderdale Street, MS 323, Memphis, Tennessee 38105-2794, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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