Cited by 388Alzheimer's disease research and treatmentsNeurogenesis and neuroplasticity mechanismsNeuroinflammation and Neurodegeneration Mechanisms

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

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LoPresti, P, Szuchet, S, Papasozomenos, S C, Zinkowski, R P, Binder, L I·1995·Proceedings of the National Academy of Sciences

Abstract

We present evidence that the microtubule-associated protein tau is present in oligodendrocytes (OLGs), the central nervous system cells that make myelin. By showing that tau is distributed in a pattern similar to that of myelin basic protein, our results suggest a possible involvement of tau in some aspect of myelination. Tau protein has been identified in OLGs in situ and in vitro. In interfascicular OLGs, tau localization, revealed by monoclonal antibody Tau-5, was confined to the cell somata. However, in cultured ovine OLGs with an exuberant network of processes, tau was detected in cell somata, cellular processes, and membrane expansions at the tips of these processes. Moreover, in such cultures, tau appeared localized adjacent to or coincident with myelin basic protein in membrane expansions along and at the ends of the cellular processes. The presence of tau mRNA was documented using fluorescence in situ hybridization. The distribution of the tau mRNA was similar to that of the tau protein. Western blot analysis of cultured OLGs showed the presence of many tau isoforms. Together, these results demonstrate that tau is a genuine oligodendrocyte protein and pave the way for determining its functional role in these cells.

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Crossref · 10.1073/pnas.92.22.10369

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Authors
LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I.
Affiliations
  • Molecular Geriatrics Corporation, Lake Bluff, IL 60044, USA.
  • University of Chicago (US)
Venue
Proceedings of the National Academy of Sciences
Published
1995-10-24
Volume
92
Issue
22
Pages
10369-10373
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1991483073
Cited by
388
References
53
Citations by year
2026: 7 · 2025: 12 · 2024: 9 · 2023: 24 · 2022: 19 · 2021: 31 · 2020: 12 · 2019: 18 · 2018: 22 · 2017: 9 · 2016: 8 · 2015: 13 · 2014: 10 · 2013: 11 · 2012: 8
FWCI
3.55
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • University of Pennsylvania
  • National Institutes of Health (5p01ns024575-08, 7r01ag006969-09, 5p50ag008664-09)
  • National Institute on Aging (R01-AG06969, P50-AG08664)
  • National Institute of Neurological Disorders and Stroke (P01-NS-24575)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
tau protein, microtubule-associated proteins, oligodendrocytes, myelination, myelin basic protein, tau isoforms, membrane expansion
MeSH terms
Animals, Brain, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Myelin Basic Protein, Immunohistochemistry, Oligodendroglia, Sheep, Blotting, Western, Microscopy, Immunoelectron, tau Proteins, In Situ Hybridization, Fluorescence, Fluorescent Antibody Technique, Indirect, Rats

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