Marked decrease of plasma apolipoprotein AI and AII in Japanese patients with late-onset non-familial Alzheimer's disease

Kawano, Motoharu; Kawakami, Masanobu; Otsuka, Masakazu; Yashima, Harumitsu; Yaginuma, Toshio; Ueki, Akira

doi:10.1016/0009-8981(95)06115-t

Cited by 67 publications

(52 citation statements)

References 7 publications

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“…Neither apoA-1 nor apoA-II has an effect on assembly of A13(1-42) into filaments, in contrast to apoE [20]. However, levels of both apolipoproteins were decreased in plasma of late-onset AD patients [9,21]. We showed that these apolipoproteins bound to AI3 with high affinity, with apoE3 having the highest affinity.…”

Section: Introductionmentioning

confidence: 66%

Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies

Shuvaev

Siest

1996

FEBS Letters

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Several apolipoproteins including apoE and apoA-I are known to be associated with amyloid ~peptide, a major component of senile plaques in Alzheimer's disease. In the present study the interaction between three human amphipathic apolipoproteins apoE3, apoA-I and apoA-1I and immobilized amyloid ~i-peptide (1-40) was quantified by plasmon resonance. The interactions were saturable and reversible. The results demonstrated a high affmity of the binding of amphipathic apolipoproteins to amyloid ~peptide. On the other hand, only a small population of synthetic amyloid ~peptide participated in the interaction. The apparent equilibrium dissociation constants /fD were 10 nM for apoE3, 25 nM for apoA-I and 80 nM for apoA-II under physiological conditions. The affinity of the apoE3-amyloid ~-peptide binding was not affected by pH in the range 6.0-8.0 but was significantly increased by high salt concentration. ApoA-I mainly followed similar patterns. A major participation of hydrophobic forces in the binding of apoE3 and apoA-I to amyloid ~-peptide was suggested.

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Section: Introductionmentioning

confidence: 66%

Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies

Shuvaev

Siest

1996

FEBS Letters

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“…There have only been a limited number of studies on the potential role of apoA-I/HDL in AD, and the results from those studies are inconsistent. Some epidemiological studies show a marked decrease of plasma apoA-I levels in human AD patients (22) and a strong correlation between decreased HDL/apoA-I levels and the severity of AD (23). Recently, results from the Honolulu-Asian Aging Study strongly suggest that apoA-I levels, more than HDL cholesterol levels, negatively associate with the risk of AD (24).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, apoA-I polymorphisms have been associated with AD and/or dementia (20,21). Furthermore, epidemiological studies show a marked decrease of plasma apoA-I levels in human AD patients (22) and demonstrate that decreased HDL cholesterol and serum apoA-I concentrations are highly correlated with the severity of AD (23). Recently, results from the Honolulu-Asian Aging Study strongly suggest that apoA-I levels, more than HDL levels, inversely associate with the risk of AD (24).…”

Section: Alzheimer Disease (Ad)mentioning

confidence: 99%

Overexpression of Human Apolipoprotein A-I Preserves Cognitive Function and Attenuates Neuroinflammation and Cerebral Amyloid Angiopathy in a Mouse Model of Alzheimer Disease

Lewis

Cao

et al. 2010

Journal of Biological Chemistry

178

167

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To date there is no effective therapy for Alzheimer disease (AD). High levels of circulating high density lipoprotein (HDL) and its main protein, apolipoprotein A-I (apoA-I), reduce the risk of cardiovascular disease. Clinical studies show that plasma HDL cholesterol and apoA-I levels are low in patients with AD. To investigate if increasing plasma apoA-I/HDL levels ameliorates AD-like memory deficits and amyloid-␤ (A␤) deposition, we generated a line of triple transgenic (Tg) mice overexpressing mutant forms of amyloid-␤ precursor protein (APP) and presenilin 1 (PS1) as well as human apoA-I (AI). Here we show that APP/PS1/AI triple Tg mice have a 2-fold increase of plasma HDL cholesterol levels. When tested in the Morris water maze for spatial orientation abilities, whereas APP/PS1 mice develop age-related learning and memory deficits, APP/PS1/AI mice continue to perform normally during aging. Interestingly, no significant differences were found in the total level and deposition of A␤ in the brains of APP/PS1 and APP/PS1/AI mice, but cerebral amyloid angiopathy was reduced in APP/PS1/AI mice. Also, consistent with the anti-inflammatory properties of apoA-I/HDL, glial activation was reduced in the brain of APP/ PS1/AI mice. In addition, A␤-induced production of proinflammatory chemokines/cytokines was decreased in mouse organotypic hippocampal slice cultures expressing human apoA-I. Therefore, we conclude that overexpression of human apoA-I in the circulation prevents learning and memory deficits in APP/ PS1 mice, partly by attenuating neuroinflammation and cerebral amyloid angiopathy. These findings suggest that elevating plasma apoA-I/HDL levels may be an effective approach to preserve cognitive function in patients with AD.

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“…ApoE has been identified immunohistochemically in many types of amyloid, suggesting that the influence of apoE may be more complicated rather than simply modulating amyloid formation by Aβ. Further, three separate studies have shown that the level of apoA-I in the serum of patients affected with neurodegenerative disease is reduced when compared to unaffected age matched individuals (Kuriyama et al, 1994;Kawano et al, 1995;Merched et al, 2000). Further longitudinal studies on apoA-I levels show that low apoA-I levels are a risk factor for the development of dementia (Saczynski et al, 2007).…”

Section: The Occurrence Of Apolipoproteins As Amyloid In Vivomentioning

confidence: 99%

Apolipoproteins and amyloid fibril formation in atherosclerosis

2011

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Amyloid fibrils arise from the aggregation of misfolded proteins into highly-ordered structures. The accumulation of these fibrils along with some non-fibrillar constituents within amyloid plaques is associated with the pathogenesis of several human degenerative diseases. A number of plasma apolipoproteins, including apolipoprotein (apo) A-I, apoA-II, apoC-II and apoE are implicated in amyloid formation or influence amyloid formation by other proteins. We review present knowledge of amyloid formation by apolipoproteins in disease, with particular focus on atherosclerosis. Further insights into the molecular mechanisms underlying their amyloidogenic propensity are obtained from in vitro studies which describe factors affecting apolipoprotein amyloid fibril formation and interactions. Additionally, we outline the evidence that amyloid fibril formation by apolipoproteins might play a role in the development and progression of atherosclerosis, and highlight possible molecular mechanisms that could contribute to the pathogenesis of this disease.

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Marked decrease of plasma apolipoprotein AI and AII in Japanese patients with late-onset non-familial Alzheimer's disease

Cited by 67 publications

References 7 publications

Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies

Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies

Overexpression of Human Apolipoprotein A-I Preserves Cognitive Function and Attenuates Neuroinflammation and Cerebral Amyloid Angiopathy in a Mouse Model of Alzheimer Disease

Apolipoproteins and amyloid fibril formation in atherosclerosis

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