Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments

Maria Grazia Spillantini, Michel Goedert, R. Anthony Crowther, Jill R. Murrell, Martin R. Farlow, Bernardino Ghetti

Research output: Contribution to journalArticle

268 Citations (Scopus)

Abstract

Neurofibrillary lesions made of hyperphosphorylated microtubule- associated protein tau constitute not only one of the defining neuropathological features of Alzheimer disease but also are present in a number of other neurodegenerative diseases with dementia. Here we describe a novel autosomal dominant disease named familial 'multiple system tauopathy with presenile dementia,' which is characterized by abundant fibrillary deposits of tau protein in both neurons and glial cells. There are no detectable deposits of β-amyloid. The tau deposits are in the form of twisted filaments that differ in diameter and periodicity from the paired helical filaments of Alzheimer disease. They are stained by both phosphorylation-independent and -dependent anti-tau antibodies. Moreover, tau immunoreactivity coexists with heparan sulfate in affected nerve and glial cells. Tau protein extracted from filaments of familial multiple system tauopathy with presenile dementia shows a minor 72-kDa band and two major bands of 64 and 68 kDa that contain mainly hyperphosphorylated four-repeat tau isoforms of 383 and 412 amino acids.

Original languageEnglish (US)
Pages (from-to)4113-4118
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number8
DOIs
StatePublished - Apr 15 1997

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tau Proteins
Frontotemporal Dementia
Neuroglia
Alzheimer Disease
Neurons
Microtubule-Associated Proteins
Heparitin Sulfate
Amyloid Plaques
Periodicity
Neurodegenerative Diseases
Dementia
Anti-Idiotypic Antibodies
Protein Isoforms
Phosphorylation
Amino Acids

Keywords

  • familial disease
  • microtubule-associated protein tau

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Familial multiple system tauopathy with presenile dementia : A disease with abundant neuronal and glial tau filaments. / Spillantini, Maria Grazia; Goedert, Michel; Crowther, R. Anthony; Murrell, Jill R.; Farlow, Martin R.; Ghetti, Bernardino.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 8, 15.04.1997, p. 4113-4118.

Research output: Contribution to journalArticle

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AB - Neurofibrillary lesions made of hyperphosphorylated microtubule- associated protein tau constitute not only one of the defining neuropathological features of Alzheimer disease but also are present in a number of other neurodegenerative diseases with dementia. Here we describe a novel autosomal dominant disease named familial 'multiple system tauopathy with presenile dementia,' which is characterized by abundant fibrillary deposits of tau protein in both neurons and glial cells. There are no detectable deposits of β-amyloid. The tau deposits are in the form of twisted filaments that differ in diameter and periodicity from the paired helical filaments of Alzheimer disease. They are stained by both phosphorylation-independent and -dependent anti-tau antibodies. Moreover, tau immunoreactivity coexists with heparan sulfate in affected nerve and glial cells. Tau protein extracted from filaments of familial multiple system tauopathy with presenile dementia shows a minor 72-kDa band and two major bands of 64 and 68 kDa that contain mainly hyperphosphorylated four-repeat tau isoforms of 383 and 412 amino acids.

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