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Amyloid β protein (Aβ) deposition in dementia with Lewy bodies: predominance of Aβ 42(43) and paucity of Aβ 40 compared with sporadic Alzheimer’s disease
Author(s) -
David Mann,
S. M. P. Brown,
F. Owen,
Baba M,
Takeshi Iwatsubo
Publication year - 1998
Publication title -
neuropathology and applied neurobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.538
H-Index - 95
eISSN - 1365-2990
pISSN - 0305-1846
DOI - 10.1046/j.1365-2990.1998.00112.x
Subject(s) - dementia with lewy bodies , beta (programming language) , deposition (geology) , lewy body , immunohistochemistry , apolipoprotein e , dementia , pathology , alzheimer's disease , gene isoform , amyloid (mycology) , apolipoprotein b , amyloid beta , chemistry , medicine , biology , disease , biochemistry , cholesterol , gene , paleontology , sediment , computer science , programming language
Amyloid β protein (Aβ) deposition was investigated by quantitative immunohistochemistry in 13 cases of dementia with Lewy bodies (DLB) and compared with that in a series of age, gender and ApoE genotype matched cases of Alzheimer’s disease (AD). In DLB the predominant Aβ peptide species deposited was Aβ 42(43) and this was similar in amount to that in AD. By contrast, Aβ 40 deposition was sparse in DLB and was lower than that in AD as was the total Aβ (Aβ 40 +Aβ 42(43) ) deposition. These data reinforce the viewpoint that in all disorders in which Aβ deposition is characteristic, the initial and predominant peptide species deposited is the longer form, Aβ 42(43) . The density of Lewy bodies (LB) in DLB was unrelated to the extent of Aβ deposition, although those cases possessing one or more copies of the apolipoprotein E E4 allele had a higher LB density than those without an E4 allele. This suggests that the apolipoprotein E E4 isoform might facilitate, though not necessarily trigger, the formation of LB in susceptible individuals.