Linked Life Data

12878699

Source:http://linkedlifedata.com/resource/pubmed/id/12878699

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2003-7-24
pubmed:abstractText
The dystrophin-associated protein complex (DPC), comprising sarcoglycans, dystroglycans, dystrobrevins, and syntrophins, is a component of synapses both in muscle and brain. Dysbindin is a novel component of the DPC, which binds to beta-dystrobrevin and may serve as an adaptor protein that links the DPC to an intracellular signaling cascade. Disruption of the DPC results in muscular dystrophy, and mutations in the human ortholog of dysbindin have been implicated in the pathogenesis of schizophrenia. In both cases, patients also present with neurological symptoms reminiscent of cerebellar problems. In the mouse cerebellum, dysbindin immunoreactivity is expressed at high levels in a subset of mossy fiber synaptic glomeruli in the granular layer. Lower levels of dysbindin immunoreactivity are also detected in Purkinje cell dendrites. In the cerebellar vermis, dysbindin-immunoreactive glomeruli are restricted to an array of parasagittal stripes that bears a consistent relationship to Purkinje cell parasagittal band boundaries as defined by the expression of the respiratory isoenzyme zebrin II/aldolase c. In a mouse model of Duchenne muscular dystrophy, the mdx mutant, in which dystrophin is not expressed, there is a dramatic increase in the number of dysbindin-immunoreactive glomeruli in the posterior cerebellar vermis. Moreover, the topography of the terminal fields is disrupted, replacing the stripes by a homogeneous distribution. Abnormal synaptic organization in the cerebellum may contribute to the neurological problems associated with muscular dystrophy and schizophrenia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
23
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6576-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12878699-Animals, pubmed-meshheading:12878699-Blotting, Western, pubmed-meshheading:12878699-Calcium-Binding Protein, Vitamin D-Dependent, pubmed-meshheading:12878699-Carrier Proteins, pubmed-meshheading:12878699-Cerebellum, pubmed-meshheading:12878699-Choline O-Acetyltransferase, pubmed-meshheading:12878699-Dendrites, pubmed-meshheading:12878699-Disease Models, Animal, pubmed-meshheading:12878699-Dystrophin, pubmed-meshheading:12878699-Female, pubmed-meshheading:12878699-Immunohistochemistry, pubmed-meshheading:12878699-Male, pubmed-meshheading:12878699-Mice, pubmed-meshheading:12878699-Mice, Inbred mdx, pubmed-meshheading:12878699-Muscular Dystrophy, Duchenne, pubmed-meshheading:12878699-Nerve Fibers, pubmed-meshheading:12878699-Nerve Tissue Proteins, pubmed-meshheading:12878699-Nitric Oxide Synthase, pubmed-meshheading:12878699-Nitric Oxide Synthase Type I, pubmed-meshheading:12878699-Purkinje Cells, pubmed-meshheading:12878699-Synapses
pubmed:year
2003
pubmed:articleTitle
Abnormal dysbindin expression in cerebellar mossy fiber synapses in the mdx mouse model of Duchenne muscular dystrophy.
pubmed:affiliation
Department of Cell Biology and Anatomy, and Genes and Development Research Group, Faculty of Medicine, The University of Calgary, Calgary, Alberta T2N 4N1, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't