Document Detail


Heterogeneity of tau proteins in Alzheimer's disease. Evidence for increased expression of an isoform and preferential distribution of a phosphorylated isoform in neurites.
MedLine Citation:
PMID:  7679548     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
W K Liu; D W Dickson; S H Yen
Related Documents :
10637228 - D-tacc: a novel centrosomal protein required for normal spindle function in the early d...
9286988 - Identification of the flii and flij components of the caulobacter flagellar type iii pr...
17082178 - Effect of pseudophosphorylation and cross-linking by lipid peroxidation and advanced gl...
10845058 - Microtubule-based transport systems in neurons: the roles of kinesins and dyneins.
19614588 - The evolution of protein domain families.
10602478 - Evidence for interaction between human prune and nm23-h1 ndpkinase.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of pathology     Volume:  142     ISSN:  0002-9440     ISO Abbreviation:  Am. J. Pathol.     Publication Date:  1993 Feb 
Date Detail:
Created Date:  1993-03-16     Completed Date:  1993-03-16     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370502     Medline TA:  Am J Pathol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  387-94     Citation Subset:  AIM; IM    
Affiliation:
Department of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adult
Alzheimer Disease / metabolism*,  pathology
Epitopes
Fetus / metabolism
Humans
Immunohistochemistry
Isomerism
Neurites / metabolism*,  pathology
Neurofibrillary Tangles / pathology
Phosphorylation
Tissue Distribution
tau Proteins / chemistry*,  immunology,  metabolism
Grant Support
ID/Acronym/Agency:
AG01136/AG/NIA NIH HHS; AG04145/AG/NIA NIH HHS; AG06803/AG/NIA NIH HHS
Chemical
Reg. No./Substance:
0/Epitopes; 0/tau Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Low expression of CD20 and CD23 in Epstein-Barr virus-induced B cell tumors in SCID/hu mice.
Next Document:  Expression of keratins 1, 6, 15, 16, and 20 in normal cervical epithelium, squamous metaplasia, cerv...