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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1995-3-2
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pubmed:abstractText |
Microtubule-associated protein tau is abnormally hyperphosphorylated in the brain of patients with Alzheimer's disease, and is the major protein subunit of paired helical filaments. There is also a significant pool of non-paired helical filament abnormally phosphorylated tau in Alzheimer's disease brain. In the present study, the site-specific dephosphorylation of this Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A was studied and compared with that by protein phosphatase-2B. The dephosphorylation was detected by its interaction with several phosphorylation-dependent antibodies to various abnormal phosphorylation sites. Protein phosphatase-2A was able to dephosphorylate the abnormally phosphorylated tau at Ser-46, Ser-199, Ser-202, Ser-396 and Ser-404, but not at Ser-235 (the amino acids are numbered according to the largest isoform of human tau, tau441). Two major types of protein phosphatase-2A, protein phosphatase-2A1 and -2A2, dephosphorylated the abnormally phosphorylated tau at approximately the same rate. After the abnormally phosphorylated tau was dephosphorylated by protein phosphatase-2A, its relative mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis increased. The dephosphorylation of the abnormal tau by protein phosphatase-2A1 and -2A2 was markedly stimulated by Mn2+. These results suggest that tau dephosphorylation is catalysed by protein phosphatase-2A in addition to protein phosphatase-2B. A deficiency of either protein phosphatase-2A or -2B, or both, may be involved in abnormal phosphorylation of tau in Alzheimer's disease.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Polylysine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/tau Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0306-4522
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
765-72
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7838376-Aged,
pubmed-meshheading:7838376-Alzheimer Disease,
pubmed-meshheading:7838376-Animals,
pubmed-meshheading:7838376-Brain,
pubmed-meshheading:7838376-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7838376-Humans,
pubmed-meshheading:7838376-Magnesium,
pubmed-meshheading:7838376-Male,
pubmed-meshheading:7838376-Manganese,
pubmed-meshheading:7838376-Phosphoprotein Phosphatases,
pubmed-meshheading:7838376-Phosphorylation,
pubmed-meshheading:7838376-Polylysine,
pubmed-meshheading:7838376-Protein Phosphatase 2,
pubmed-meshheading:7838376-Rats,
pubmed-meshheading:7838376-Rats, Sprague-Dawley,
pubmed-meshheading:7838376-tau Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A.
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pubmed:affiliation |
New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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