Publication: Intra- and extracellular Aß and PHF in clinically evaluated cases of Alzheimer’s disease
Authors
Fernández-Vizarra, P. ; Fernández, A.P. ; Castro-Blanco, S. ; Serrano, J. ; Bentura, M.L. ; Martínez Murillo, R. ; Martínez, A. ; Rodrigo, J.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Temporal cortical sections from postmortem
brains of individuals without any dementing condition
and with different degrees of severity of Alzheimer’s
disease (AD) evaluated by the Clinical Dementia Rating
scale (CDR 0-CDR 3) were analyzed using
immunohistochemical procedures. To demonstrate the
amyloid-ß-peptide (Aß) deposition and the
neurofibrillary pathology, two monoclonal antibodies
were used, a human CERAD Aß (10D5) antibody raised
against the N-terminal region of the Aß-peptide, and an
antibody raised against paired helical filaments (PHF-1).
The neuron cell bodies and the glial cells were also
recognized by two polyclonal antibodies raised,
respectively, against the protein gene peptide (PGP 9.5)
and glial fibrillary acidic protein (GFAP). Directly
related to severity of AD, progressive deposits of Aßpeptide
were found within cortical pyramidal-like
neurons and forming senile plaques. Ultrastructurally,
Aß-peptide deposits were related to neuronal
intracytoplasmic organelles, such as the ER, the
mitochondria, the Nissl bodies and lipofuscin. We have
also found that the intracellular deposition of the Aß
peptide is a neuropathological finding prior to the
appearance of PHF-immunoreactive structures. We
suggest that the intracellular Aß deposition in cortical
pyramidal neurons is a first neurodegenerative event in
AD development and that it is involved in cell
dysfunction, neuronal death, and plaque formation
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