The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in PubMed. This abstract is what is used to create the fingerprint of the publication. If any grants are referenced by the publication, they will be listed here as well.
Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.
K S Kosik; C L Joachim; D J Selkoe (Profiled Author: Selkoe, Dennis J)
Proceedings of the National Academy of Sciences of the United States of America 1986;83(11):4044-8.Abstract
The detailed protein composition of the paired helical filaments (PHF) that accumulate in human neurons in aging and Alzheimer disease is unknown. However, the identity of certain components has been surmised by using immunocytochemical techniques. Whereas PHF share epitopes with neurofilament proteins and microtubule-associated protein (MAP) 2, we report evidence that the MAP tau (tau) appears to be their major antigenic component. Immunization of rabbits with NaDodSO4-extracted, partially purified PHF (free of normal cytoskeletal elements, including tau) consistently produces antibodies to tau but not, for example, to neurofilaments. Such PHF antibodies label all of the heterogeneous fetal and mature forms of tau from rat and human brain. Absorption of PHF antisera with heat-stable MAPs (rich in tau) results in almost complete loss of staining of neurofibrillary tangles (NFT) in human brain sections. An affinity-purified antibody to tau specifically labels NFT and the neurites of senile plaques in human brain sections as well as NaDodSO4-extracted NFT. tau-Immunoreactive NFT frequently extend into the apical dendrites of pyramidal neurons, suggesting an aberrant intracellular locus for this axonal protein. tau and PHF antibodies label tau proteins identically on electrophoretic transfer blots and stain the gel-excluded protein representing NaDodSO4-insoluble PHF in homogenates of human brain. The progressive accumulation of altered tau protein in neurons in Alzheimer disease may result in instability of microtubules, consequent loss of effective transport of molecules and organelles, and, ultimately, neuronal death.
1 Originating Grant
SELKOE, DENNIS J
1 June 1985 - 30 November 1986
NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
Total Funding: $ 161,851
This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts and related grants with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.
1 May 1985 - 30 September 2000
NATIONAL INSTITUTE ON AGING
Total Funding: $ 2,282,872
2 September 2011 - 30 June 2014
FOGARTY INTERNATIONAL CENTER
Total Funding: $ 70,352
GANDY, SAMUEL E
15 September 2010 - 30 June 2014
NATIONAL CENTER FOR COMPLEMENTARY &ALTERNATIVE MEDICINE
Total Funding: $ 241,601
J G Wood; S S Mirra; N J Pollock; L I BinderProceedings of the National Academy of Sciences of the United States of America 1986;83(11):4040-3.
P Mulvihill; G PerryBrain research 1989;484(1-2):150-6.
D W Dickson; H Ksiezak-Reding; P Davies; S H YenActa neuropathologica 1987;73(3):254-8.
Appears in this Publication
Author of this Publication