Alzheimer's disease

Microtubule-associated proteins 2 (MAP 2) are not components of paired helical filaments

M. Rosemblatt, A. Fellous, J. C. Mazie, A. Delacourte, A. Defossez

Resultado de la investigación: Article

11 Citas (Scopus)

Resumen

In Alzheimer's disease, the most characteristic neuropathological changes are the formation of neurofibrillary tangles (NFT) and neuritic plaques (NP) characterized by the presence of bundles of paired helical filaments (PHF) that accumulate in the degenerating neurites and neuronal cell bodies. Although the protein composition of the PHF is ill-defined, a number of microtubule-associated proteins have been implicated in these lesions. Here we report results with an antiserum monospecific for the microtubule-associated protein MAP 2 which does not cross-react with any other microtubular protein. Immunostaining with this antibody of sections from an Alzheimer's brain show a strong reactivity with NFT but no reactivity at the level of the NP. On the other hand, immunostaining of Alzheimer's brain sections with another antibody specific for the microtubule-associated protein τ shows strong staining of PHF on both NFT and NP. These findings confirm the presence of the τ proteins in the PHF and strongly suggest that MAP 2 may not be a main structural component of the PHF. Labelling of NFT with the anti-MAP 2 antiserum suggests a non-specific binding of MAP 2 to the PHF during the process of NFT formation.

Idioma originalEnglish
Páginas (desde-hasta)91-94
Número de páginas4
PublicaciónFEBS Letters
Volumen252
N.º1-2
DOI
EstadoPublished - 1989

Huella dactilar

Microtubule-Associated Proteins
Neurofibrillary Tangles
Alzheimer Disease
Amyloid Plaques
Immune Sera
Brain
Proteins
Antibodies
Neurites
Labeling
Cells
Staining and Labeling
Chemical analysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology
  • Cell Biology
  • Genetics

Citar esto

Rosemblatt, M. ; Fellous, A. ; Mazie, J. C. ; Delacourte, A. ; Defossez, A. / Alzheimer's disease : Microtubule-associated proteins 2 (MAP 2) are not components of paired helical filaments. En: FEBS Letters. 1989 ; Vol. 252, N.º 1-2. pp. 91-94.
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abstract = "In Alzheimer's disease, the most characteristic neuropathological changes are the formation of neurofibrillary tangles (NFT) and neuritic plaques (NP) characterized by the presence of bundles of paired helical filaments (PHF) that accumulate in the degenerating neurites and neuronal cell bodies. Although the protein composition of the PHF is ill-defined, a number of microtubule-associated proteins have been implicated in these lesions. Here we report results with an antiserum monospecific for the microtubule-associated protein MAP 2 which does not cross-react with any other microtubular protein. Immunostaining with this antibody of sections from an Alzheimer's brain show a strong reactivity with NFT but no reactivity at the level of the NP. On the other hand, immunostaining of Alzheimer's brain sections with another antibody specific for the microtubule-associated protein τ shows strong staining of PHF on both NFT and NP. These findings confirm the presence of the τ proteins in the PHF and strongly suggest that MAP 2 may not be a main structural component of the PHF. Labelling of NFT with the anti-MAP 2 antiserum suggests a non-specific binding of MAP 2 to the PHF during the process of NFT formation.",
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Alzheimer's disease : Microtubule-associated proteins 2 (MAP 2) are not components of paired helical filaments. / Rosemblatt, M.; Fellous, A.; Mazie, J. C.; Delacourte, A.; Defossez, A.

En: FEBS Letters, Vol. 252, N.º 1-2, 1989, p. 91-94.

Resultado de la investigación: Article

TY - JOUR

T1 - Alzheimer's disease

T2 - Microtubule-associated proteins 2 (MAP 2) are not components of paired helical filaments

AU - Rosemblatt, M.

AU - Fellous, A.

AU - Mazie, J. C.

AU - Delacourte, A.

AU - Defossez, A.

PY - 1989

Y1 - 1989

N2 - In Alzheimer's disease, the most characteristic neuropathological changes are the formation of neurofibrillary tangles (NFT) and neuritic plaques (NP) characterized by the presence of bundles of paired helical filaments (PHF) that accumulate in the degenerating neurites and neuronal cell bodies. Although the protein composition of the PHF is ill-defined, a number of microtubule-associated proteins have been implicated in these lesions. Here we report results with an antiserum monospecific for the microtubule-associated protein MAP 2 which does not cross-react with any other microtubular protein. Immunostaining with this antibody of sections from an Alzheimer's brain show a strong reactivity with NFT but no reactivity at the level of the NP. On the other hand, immunostaining of Alzheimer's brain sections with another antibody specific for the microtubule-associated protein τ shows strong staining of PHF on both NFT and NP. These findings confirm the presence of the τ proteins in the PHF and strongly suggest that MAP 2 may not be a main structural component of the PHF. Labelling of NFT with the anti-MAP 2 antiserum suggests a non-specific binding of MAP 2 to the PHF during the process of NFT formation.

AB - In Alzheimer's disease, the most characteristic neuropathological changes are the formation of neurofibrillary tangles (NFT) and neuritic plaques (NP) characterized by the presence of bundles of paired helical filaments (PHF) that accumulate in the degenerating neurites and neuronal cell bodies. Although the protein composition of the PHF is ill-defined, a number of microtubule-associated proteins have been implicated in these lesions. Here we report results with an antiserum monospecific for the microtubule-associated protein MAP 2 which does not cross-react with any other microtubular protein. Immunostaining with this antibody of sections from an Alzheimer's brain show a strong reactivity with NFT but no reactivity at the level of the NP. On the other hand, immunostaining of Alzheimer's brain sections with another antibody specific for the microtubule-associated protein τ shows strong staining of PHF on both NFT and NP. These findings confirm the presence of the τ proteins in the PHF and strongly suggest that MAP 2 may not be a main structural component of the PHF. Labelling of NFT with the anti-MAP 2 antiserum suggests a non-specific binding of MAP 2 to the PHF during the process of NFT formation.

KW - Alzheimer's disease

KW - Microtubule-associated protein 2

KW - Neurofibrillary tangle

KW - Paired helical filament

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