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Journal ArticleDOI

Tau as a nucleolar protein in human nonneural cells in vitro and in vivo.

Virginia C. Thurston, +2 more
- 01 Jul 1996 - 
- Vol. 105, Iss: 1, pp 20-30
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TLDR
The Tau-1 monoclonal antibody was localized to the nucleolus of interphase cells and the nucleolar organizing regions (NORs) of acrocentric chromosomes in cultured human cells, contributing to a growing body of evidence defining tau as a multifunctional protein that may be involved in ribosomal biogenesis and/or rRNA transcription in the nucleus of all cells as well as microtubule-stabilizing functions in the neuronal cytoplasm.
Abstract
The Tau-1 monoclonal antibody was localized to the nucleolus of interphase cells and the nucleolar organizing regions (NORs) of acrocentric chromosomes in cultured human cells. Putative nucleolar and NOR tau was found in HeLa cells and lymphoblasts as well as in nontransformed fibroblasts and lymphocytes. To confirm the presence of tau in the nuclei of these nonneural cells, immunoblotting analysis was performed on isolated nuclei from lymphoblasts. Several tau bands were noted on the blot of the nuclear extract suggesting the presence of multiple tau isoforms. Tau-1 immunostaining demonstrated variable staining intensities between individual acrocentric chromosomes in all cells tested. In cultured peripheral lymphocytes, these staining patterns were the same from one chromosome spread to the next within an individual. This consistency of Tau-1 staining and its variability among NORs was reminiscent of staining patterns obtained using the silver-NOR procedure. Comparisons of Tau-1 immunostaining with silver staining of chromosome spreads from human lymphocytes demonstrated that Tau-1 did not immunostain all of the NORs that were silver stained. The intensity of Tau-1 fluorescence in nucleoli was further shown to be increased in phytohemagglutinin-stimulated lymphocytes, indicating an upregulation of nuclear tau when cells reentered the cell cycle. These results contribute to a growing body of evidence defining tau as a multifunctional protein that may be involved in ribosomal biogenesis and/or rRNA transcription in the nucleus of all cells as well as microtubule-stabilizing functions in the neuronal cytoplasm.

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Citations
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Journal ArticleDOI

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders

TL;DR: Tau proteins are the major constituents of intraneuronal and glial fibrillar lesions described in Alzheimer's disease and numerous neurodegenerative disorders referred as 'tauopathies' as discussed by the authors.
Journal ArticleDOI

RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

TL;DR: It is reported that PHF assembly is strongly enhanced by RNA, dependent on the formation of intermolecular disulfide bridges involving Cys322 in the third repeat of tau and includes the dimerization of t Tau as an early intermediate.
Journal ArticleDOI

Tau interacts with src-family non-receptor tyrosine kinases

TL;DR: The data suggest that tau is involved in signal transduction pathways, and an interaction between tau and fyn may serve as a mechanism by which extracellular signals influence the spatial distribution of microtubules.
Journal ArticleDOI

Tau and tauopathies

TL;DR: According to currently emerging cell biological concepts, tau might play a role in the regulation of neuronal plasticity in a wide array of neuronal networks and in addition, it might be involved in regulating genome stability.
Journal ArticleDOI

Nuclear Tau, a Key Player in Neuronal DNA Protection

TL;DR: It is demonstrated that acute oxidative stress and mild heat stress induce the accumulation of dephosphorylated Tau in neuronal nuclei and a novel role for nuclear Tau as a key player in early stress response is highlighted.
References
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Journal ArticleDOI

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TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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TL;DR: A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets that results in quantitative transfer of ribosomal proteins from gels containing urea.
Journal ArticleDOI

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

TL;DR: It is suggested that tau in Alzheimer brain is an abnormally phosphorylated protein component of PHF, the two major locations of paired-helical filaments in Alzheimer disease brain.
Journal ArticleDOI

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

TL;DR: Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.
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