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PMID: 11438517 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Functional differences of tau isoforms containing 3 or 4 C-terminal repeat regions and the influence of oxidative stress.

The Journal of biological chemistry ·Vol. 276 ·No. 36 ·2001-09-07 ·Pages 34288-97

Utton MA, Gibb GM, Burdett ID, Anderton BH, Vandecandelaere A

Abstract

We report functional differences between tau isoforms with 3 or 4 C-terminal repeats and a difference in susceptibility to oxidative conditions, with respect to the regulation of microtubule dynamics in vitro and tau-microtubule binding in cultured cells. In the presence of dithiothreitol in vitro, a 3-repeat tau isoform promotes microtubule nucleation, reduces the tubulin critical concentration for microtubule assembly, and suppresses dynamic instability. Under non-reducing conditions, threshold concentrations of 3-repeat tau and tubulin exist below which this isoform still promotes microtubule nucleation and assembly but fails to reduce the tubulin critical concentration or suppress dynamic instability; above these threshold concentrations, amorphous aggregates of 3-repeat tau and tubulin can be produced at the expense of microtubule formation. A 4-repeat tau isoform is less sensitive to the oxidative potential of the environment, behaving under oxidative conditions similarly to the 3-repeat isoform under reducing conditions. Under conditions of oxidative stress, in Chinese hamster ovary cells stably expressing either 3- or 4-repeat tau, 3-repeat tau disassociates from microtubules more readily than the 4-repeat isoform, and tau-containing high molecular weight aggregates are preferentially observed in lysates from the Chinese hamster ovary cells expressing 3-repeat tau, indicating greater susceptibility of 3-repeat tau to oxidative conditions, compared with 4-repeat tau in vivo.

MeSH Terms
Animals CHO Cells Cell Division Cells, Cultured Cricetinae Dose-Response Relationship, Drug Microscopy, Electron Microscopy, Fluorescence Microtubules/chemistry,metabolism Neurons/metabolism Oxidative Stress Protein Isoforms Protein Structure, Tertiary Recombinant Proteins/metabolism Reducing Agents/pharmacology Swine Time Factors Transfection tau Proteins/chemistry,physiology
Chemicals
Protein Isoforms Recombinant Proteins Reducing Agents tau Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Utton M A
Department of Neuroscience, Institute of Psychiatry, King's College London, De Crespigny Park, London SE5 8AF, United Kingdom. m.utton@iop.kcl.ac.uk
Gibb G M
Burdett I D
Anderton B H
Vandecandelaere A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2001-09-07
Epub
2001-00-03
Pages
34288-97
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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