Abundance of the longer A beta 42 in neocortical and cerebrovascular amyloid beta deposits in Swedish familial Alzheimer's disease and Down's syndrome.

https://arctichealth.org/en/permalink/ahliterature211852
Source
Neuroreport. 1996 May 31;7(8):1377-81
Publication Type
Article
Date
May-31-1996
Author
R N Kalaria
D L Cohen
B D Greenberg
M J Savage
N E Bogdanovic
B. Winblad
L. Lannfelt
A. Adem
Author Affiliation
Department of Neurology, Case Western Reserve University, Cleveland, OH 44106, USA.
Source
Neuroreport. 1996 May 31;7(8):1377-81
Date
May-31-1996
Language
English
Publication Type
Article
Keywords
Adult
Aged
Aged, 80 and over
Alzheimer Disease - genetics - metabolism
Amyloid beta-Peptides - analysis - genetics
Amyloid beta-Protein Precursor - genetics
Cerebral Cortex - chemistry
Cerebrovascular Circulation - physiology
Down Syndrome - genetics - metabolism
Humans
Immunohistochemistry
Middle Aged
Mutation
Nerve Tissue Proteins - analysis - genetics
Periodicity
Sweden
Abstract
Recent studies have demonstrated the deposition of amyloid beta (A beta) protein with carboxyl- and aminoterminal heterogeneity in cortical and cerebrovascular deposits of Alzheimer's disease (AD). Using carboxyl end-terminal specific antibodies to A beta peptides, we examined the immunocytochemical distribution of A beta 40 and A beta 42 species in brain tissue from a Swedish subject with familial AD (FAD) bearing the double mutation at codons 670/671 in the amyloid beta precursor protein (A beta PP), and from subjects with Down's syndrome and sporadic AD. In the Swedish subject, we found profound parenchymal A beta deposits and cerebral amyloid angiopathy in all four cortical lobes and cerebellum. A beta 42 was evident in almost all parenchymal deposits as well as many vascular deposits. Although A beta 40 was present in meningeal and intraparenchymal vessels, deposits containing this shorter peptide reactivity were sparse. Surprisingly, our observations in Swedish FAD showing a remarkable abundance of A beta 42 in both parenchymal and vascular deposits were qualitatively similar to the Down's syndrome and most sporadic AD cases, and to previously published A beta PP717 FAD. While previous transfection studies in different cell cultures indicate substantially increased soluble A beta production and A beta 40 species to be predominant, it would appear that the double A beta PP mutations in Swedish FAD largely result in the deposition of the longer A beta 42 in vivo.
PubMed ID
8856679 View in PubMed
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