Source:http://linkedlifedata.com/resource/pubmed/id/11115852
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
20
|
| pubmed:dateCreated |
2001-1-9
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| pubmed:abstractText |
Mutations in the gene for the microtubule-associated protein tau are associated with frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). In this study we compared the presence of the P301L mutated tau protein from brain material of patients with that of the normal 4-repeat, using polyclonal antibodies specific for the P301L point mutation and its normal counterpart. We determined the relative ratio of mutated versus normal tau protein in the sarkosyl-soluble and -insoluble protein fractions from several brain regions. Although mutated and normal tau proteins are both present in the sarkosyl-insoluble deposits, quantitative analysis showed that the mutated protein is the major component. In the sarkosyl-soluble fraction of frontal and temporal cortex the overall ratio of 3-repeat versus 4-repeat tau isoforms is unchanged but there is a dramatic depletion of mutant tau protein. Furthermore, we observed an increase in tau-immunoreactive cleavage products with the P301L antibody, suggesting that the mutant protein is partly resistant to degradation and this is confirmed by pulse-chase experiments. This is the first direct evidence using patient material that shows a selective aggregation of mutant tau protein resulting in sarkosyl-insoluble deposits and the specific depletion of mutated tau protein in the soluble fraction.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0964-6906
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
12
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| pubmed:volume |
9
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3075-82
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11115852-Aged,
pubmed-meshheading:11115852-Amino Acid Substitution,
pubmed-meshheading:11115852-Animals,
pubmed-meshheading:11115852-Antibodies,
pubmed-meshheading:11115852-COS Cells,
pubmed-meshheading:11115852-Cerebral Cortex,
pubmed-meshheading:11115852-Chromosomes, Human, Pair 17,
pubmed-meshheading:11115852-Dementia,
pubmed-meshheading:11115852-Humans,
pubmed-meshheading:11115852-Immunohistochemistry,
pubmed-meshheading:11115852-Microtubule-Associated Proteins,
pubmed-meshheading:11115852-Middle Aged,
pubmed-meshheading:11115852-PC12 Cells,
pubmed-meshheading:11115852-Parkinsonian Disorders,
pubmed-meshheading:11115852-Point Mutation,
pubmed-meshheading:11115852-Prefrontal Cortex,
pubmed-meshheading:11115852-Rabbits,
pubmed-meshheading:11115852-Rats,
pubmed-meshheading:11115852-tau Proteins
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Mutation-dependent aggregation of tau protein and its selective depletion from the soluble fraction in brain of P301L FTDP-17 patients.
|
| pubmed:affiliation |
Department of Clinical Genetics, Erasmus University, PO Box 1738, 3000 DR Rotterdam, The Netherlands.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|