| pubmed-article:7679548 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0002395 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0085103 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0085401 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0205217 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:7679548 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:7679548 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7679548 | pubmed:dateCreated | 1993-3-16 | lld:pubmed |
| pubmed-article:7679548 | pubmed:abstractText | PHF-tau, a modified form of tau in Alzheimer diseased brains, is composed of proteins of molecular weight 68, 64, and 60 kd. The 68-kd PHF-tau has been reported to be encoded by a tau transcript containing both exons 2 and 3. The 64-kd protein contains exon 2, but not exon 3, and the 60-kd protein contains neither exons 2 nor 3. To study the proportion of different tau isoforms in PHF-tau and normal tau, we raised antibodies to exon 2 (E-2) and exon 3 (E-3). By immunoblots, about 74% of the PHF-tau contained exon 2, and 25% contained exon 3; whereas in normal tau, 82 to 90% contained exon 2, and no more than 5% contained exon 3. Enzyme-linked immunosorbent assays demonstrated that PHF-tau was 38% less reactive with E-2 and 79% more reactive with E-3 than normal tau. Alkaline phosphatase treatment increased the E-2 immunoreactivity of PHF-tau by 120% and normal tau by 38%, but it had no effect on E-3 immunoreactivity. The dephosphorylated PHF-tau and normal tau were similar in E-2 immunoreactivities. Phosphatase treatment of Alzheimer's diseased brain sections increased the number of E-2 immunoreactive neuropil threads and senile plaque neurites but had very little effect on the number of immunoreactive neurofibrillary tangles. The results suggest that PHF-tau contains proportionally more isoforms with E-3 than normal tau; that the E-2 epitope is more phosphorylated in PHF-tau than in normal tau; and that the phosphorylated E-2 epitope of PHF-tau is preferentially located in neurites. | lld:pubmed |
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| pubmed-article:7679548 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7679548 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7679548 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:7679548 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7679548 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7679548 | pubmed:issn | 0002-9440 | lld:pubmed |
| pubmed-article:7679548 | pubmed:author | pubmed-author:RaoL MLM | lld:pubmed |
| pubmed-article:7679548 | pubmed:author | pubmed-author:LiuW KWK | lld:pubmed |
| pubmed-article:7679548 | pubmed:author | pubmed-author:DicksonD WDW | lld:pubmed |
| pubmed-article:7679548 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7679548 | pubmed:volume | 142 | lld:pubmed |
| pubmed-article:7679548 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7679548 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7679548 | pubmed:pagination | 387-94 | lld:pubmed |
| pubmed-article:7679548 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7679548 | pubmed:meshHeading | pubmed-meshheading:7679548-... | lld:pubmed |
| pubmed-article:7679548 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7679548 | pubmed:articleTitle | Heterogeneity of tau proteins in Alzheimer's disease. Evidence for increased expression of an isoform and preferential distribution of a phosphorylated isoform in neurites. | lld:pubmed |
| pubmed-article:7679548 | pubmed:affiliation | Department of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461. | lld:pubmed |
| pubmed-article:7679548 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7679548 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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