Linked Life Data

12473071

Source:http://linkedlifedata.com/resource/pubmed/id/12473071

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2002-12-10
pubmed:abstractText
Protein phosphatase (PP2A) 2A is a hetero-trimeric holoenzyme that consists of a core dimer composed of a catalytic subunit that is tightly complexed with the scaffolding subunit PR65/A. This core dimer associates with variable regulatory subunits of the PR55/B, PR61/B', PR72/B" and PR93/PR110/B"' families. As PP2A holoenzymes containing PR55/B have been shown to be involved in the pathogenesis of Alzheimer's disease, we characterized the PR55/B family with particular emphasis on its distribution and expression in the brain. We determined the genomic organization of all members of the PR55/B family and cloned their murine cDNAs. Thereby, two novel splice variants of PR55/Bbeta were identified. In addition, Northern blot analysis revealed multiple transcripts for the different PR55 subunits, suggesting a higher variability within the PR55 family. In situ hybridization analysis revealed that all PR55/B subunits were widely expressed in the brain. PR55/Balpha and Bbeta protein expression varies significantly in areas of the brain affected by neurodegenerative diseases such as the hippocampus or cerebellum. At the cellular level, PR55/Bbeta protein expression was confined to neurons, whereas PR55/Balpha was also expressed in activated astrocytes indicating that the PR55 isoforms confer a different function to the holoenzyme complex. As PP2A dysfunction has been demonstrated to contribute to various human diseases, dissecting the PP2A holoenzyme and its particular function in different cell types will assist in the development of novel therapeutic strategies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0953-816X
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2039-48
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12473071-Alternative Splicing, pubmed-meshheading:12473071-Animals, pubmed-meshheading:12473071-Astrocytes, pubmed-meshheading:12473071-Brain, pubmed-meshheading:12473071-COS Cells, pubmed-meshheading:12473071-DNA, Complementary, pubmed-meshheading:12473071-Gene Expression Regulation, Enzymologic, pubmed-meshheading:12473071-Holoenzymes, pubmed-meshheading:12473071-Immunohistochemistry, pubmed-meshheading:12473071-Macromolecular Substances, pubmed-meshheading:12473071-Mice, pubmed-meshheading:12473071-Molecular Sequence Data, pubmed-meshheading:12473071-Neurodegenerative Diseases, pubmed-meshheading:12473071-Neurons, pubmed-meshheading:12473071-Phosphoprotein Phosphatases, pubmed-meshheading:12473071-Protein Isoforms, pubmed-meshheading:12473071-Protein Phosphatase 2, pubmed-meshheading:12473071-RNA, Messenger, pubmed-meshheading:12473071-Sequence Homology, Amino Acid, pubmed-meshheading:12473071-Sequence Homology, Nucleic Acid, pubmed-meshheading:12473071-tau Proteins
pubmed:year
2002
pubmed:articleTitle
Diversity, developmental regulation and distribution of murine PR55/B subunits of protein phosphatase 2A.
pubmed:affiliation
Friedrich Miescher Institute, Maul beerstrasse 66, 4058 Basel, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't