Linked Life Data

12207970

Source:http://linkedlifedata.com/resource/pubmed/id/12207970

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-9-4
pubmed:abstractText
Mutations in the presenilin 1 and 2 genes cause the majority of early onset familial forms of Alzheimer's disease. Here we describe the biochemical and immunohistochemical characterization of calsenilin, a novel calcium binding protein that we have previously shown to interact with presenilins 1 and 2, in mouse brain. The co-immunoprecipitation of endogenous calsenilin and presenilin 1 demonstrates that these proteins are physiologic binding partners. Although calsenilin has been predicted to be a soluble protein, we have found that the majority of it is tightly associated with the cytoplasmic face of intracellular membranes and that it can only be dissociated using harsh treatments such as urea. In addition, we have demonstrated that calsenilin is a developmentally regulated protein that is mainly present in the brain, where it localizes to both the hippocampus and cerebellum. Calsenilin staining co-localized with the somatodendritic marker microtubule-associated protein-2 primarily in the granular cell layer of the cerebellum, indicating that calsenilin expression is primarily neuronal. In primary cultured neurons, calsenilin immunoreactivity was observed in cell bodies as well as in some neuronal processes. Co-localization experiments using specific axonal and dendritic markers indicate that these processes were mainly axonal in nature, although a smaller subset of dendrites also appears to contain calsenilin. In summary, we have established that calsenilin and presenilin 1 can interact at physiologic levels, and that calsenilin is a developmentally regulated protein that is expressed primarily in the cerebellum and hippocampus. Although calsenilin is a soluble protein, it is tightly associated with the membrane. Finally, the expression pattern of calsenilin, which is similar to that of the presenilin(s), suggests that the common locations of these two proteins provide an opportunity for physical interaction in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0306-4522
pubmed:author
pubmed:copyrightInfo
Copyright 2002 IBRO
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12207970-Aging, pubmed-meshheading:12207970-Alzheimer Disease, pubmed-meshheading:12207970-Animals, pubmed-meshheading:12207970-Animals, Newborn, pubmed-meshheading:12207970-Antibody Specificity, pubmed-meshheading:12207970-Brain, pubmed-meshheading:12207970-Calcium-Binding Proteins, pubmed-meshheading:12207970-Cell Compartmentation, pubmed-meshheading:12207970-Cell Membrane, pubmed-meshheading:12207970-Cells, Cultured, pubmed-meshheading:12207970-Fetus, pubmed-meshheading:12207970-Immunohistochemistry, pubmed-meshheading:12207970-Kv Channel-Interacting Proteins, pubmed-meshheading:12207970-Membrane Proteins, pubmed-meshheading:12207970-Mice, pubmed-meshheading:12207970-Microtubule-Associated Proteins, pubmed-meshheading:12207970-Molecular Sequence Data, pubmed-meshheading:12207970-Neurons, pubmed-meshheading:12207970-Presenilin-1, pubmed-meshheading:12207970-Repressor Proteins, pubmed-meshheading:12207970-Sequence Homology, Amino Acid
pubmed:year
2002
pubmed:articleTitle
Biochemical and immunocytochemical characterization of calsenilin in mouse brain.
pubmed:affiliation
Genetics and Aging Unit, Department of Neurology, Massachusetts General Hospital and Harvard Medical School, 114, 16th Street, Charlestown, MA 02129, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't