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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-8-12
|
| pubmed:abstractText |
The objective of this study was to asses the response of the microtubule-associated protein tau to acute rise in the concentration of free cytoplasmic calcium ([Ca2+]i) in rat cortical neurons and mouse cerebellar granule cells in culture. One-hour exposure to glutamate (100 microM), N-methyl-D-aspartate (100 microM), KCl (50 mM), and ionomycin (5 microM) led to tau protein dephosphorylation as indicated by an appearance of additional faster moving bands on Western immunoblots with a phosphorylation-independent antibody and an increase in the tau-1 immunoreactivity associated with the appearance of an additional faster moving band. Lowering the extracellular concentration of Ca2+ to less than 1 microM fully prevented the drug-induced tau protein dephosphorylation indicating a dependence on Ca2+ influx from the extracellular environment. Administration of okadaic acid (inhibitor of phosphatase 1/2A) simultaneously with the above mentioned drugs decreased the drug-mediated dephosphorylation. Pre-incubation with okadaic acid fully prevented the dephosphorylation. Treatment with cypermethrin (inhibitor of phosphatase 2B) was without effect when administered either alone, simultaneously with the drugs, or pre-incubated. These findings indicate that, independently of the influx pathway, [Ca2+]i elevation leads to dephosphorylation of the microtubule-associated protein tau and implicate phosphatase 1 and/or 2A in the process.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Ionomycin,
http://linkedlifedata.com/resource/pubmed/chemical/N-Methylaspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrethrins,
http://linkedlifedata.com/resource/pubmed/chemical/cypermethrin,
http://linkedlifedata.com/resource/pubmed/chemical/tau Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0006-8993
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
757
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
93-101
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9200503-Analysis of Variance,
pubmed-meshheading:9200503-Animals,
pubmed-meshheading:9200503-Calcium,
pubmed-meshheading:9200503-Cells, Cultured,
pubmed-meshheading:9200503-Cerebellum,
pubmed-meshheading:9200503-Cerebral Cortex,
pubmed-meshheading:9200503-Cytoplasm,
pubmed-meshheading:9200503-Embryo, Mammalian,
pubmed-meshheading:9200503-Glutamic Acid,
pubmed-meshheading:9200503-Ionomycin,
pubmed-meshheading:9200503-Mice,
pubmed-meshheading:9200503-N-Methylaspartate,
pubmed-meshheading:9200503-Neurons,
pubmed-meshheading:9200503-Okadaic Acid,
pubmed-meshheading:9200503-Phosphoprotein Phosphatases,
pubmed-meshheading:9200503-Potassium Chloride,
pubmed-meshheading:9200503-Protein Phosphatase 1,
pubmed-meshheading:9200503-Pyrethrins,
pubmed-meshheading:9200503-Rats,
pubmed-meshheading:9200503-tau Proteins
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Acute rise in the concentration of free cytoplasmic calcium leads to dephosphorylation of the microtubule-associated protein tau.
|
| pubmed:affiliation |
Laboratories for Molecular Neuroscience, Mailman Research Center, McLean Hospital, Belmont, MA 02178, USA. edamec@crcii.mclean.org
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|