The Positive Side of the Alzheimer’s Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1

Ciccone, Lidia; Shi, Chenghui; Lorenzo, Davide di; Baelen, Anne-Cécile Van; Tonali, Nicolò

doi:10.3390/molecules25102439

Cited by 40 publications

(24 citation statements)

References 243 publications

(328 reference statements)

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“…Interestingly, the human APOE ε4 gene has been reported as a major genetic risk factor for lateonset AD [62]. In AD studies, apo A-I has the capability to prevent the formation of Aβ 42 and reduce Aβ 42 toxicity, and immunohistochemistry revealed the colocalization of apo A-I with Aβ 42 [63].…”

Section: Discussionmentioning

confidence: 99%

Change in the plasma proteome associated with canine cognitive dysfunction syndrome (CCDS) in Thailand

et al. 2021

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Background Canine cognitive dysfunction syndrome (CCDS) is a progressive neurodegenerative disorder found in senior dogs. Due to the lack of biological markers, CCDS is commonly underdiagnosed. The aim of this study was to identify potential plasma biomarkers using proteomics techniques and to increase our understanding of the pathogenic mechanism of the disease. Plasma amyloid beta 42 (Aβ42) has been seen to be a controversial biomarker for CCDS. Proteomics analysis was performed for protein identification and quantification. Results Within CCDS, ageing, and adult dogs, 87 proteins were identified specific to Canis spp. in the plasma samples. Of 87 proteins, 48 and 41 proteins were changed in the ageing and adult groups, respectively. Several distinctly expressed plasma proteins identified in CCDS were involved in complement and coagulation cascades and the apolipoprotein metabolism pathway. Plasma Aβ42 levels considerably overlapped within the CCDS and ageing groups. In the adult group, the Aβ42 level was low compared with that in the other groups. Nevertheless, plasma Aβ42 did not show a correlation with the Canine Cognitive Dysfunction Rating scale (CCDR) score in the CCDS group (p = 0.131, R2 = 0.261). Conclusions Our present findings suggest that plasma Aβ42 does not show potential for use as a diagnostic biomarker in CCDS. The nano-LC-MS/MS data revealed that the predictive underlying mechanism of CCDS was the co-occurrence of inflammation-mediated acute phase response proteins and complement and coagulation cascades that partly functioned by apolipoproteins and lipid metabolism. Some of the differentially expressed proteins may serve as potential predictor biomarkers along with Aβ42 in plasma for improved CCDS diagnosis. Further study in larger population-based cohort study is required in validation to define the correlation between protein expression and the pathogenesis of CCDS.

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Section: Discussionmentioning

confidence: 99%

Change in the plasma proteome associated with canine cognitive dysfunction syndrome (CCDS) in Thailand

et al. 2021

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“…Alternatively, apoA-I could bind APP on the cell surface, avoiding the APP endocytic process, essential for βand γ-secretases activities and resulting in a reduced production of the neurotoxic, insoluble Aβ. The interaction between Aβ and apoA-I with respect to AD pathogenesis has been recently extensively reviewed by Ciccone L. et al [33]. A mechanism implicated in the neuroprotective effect of HDL could be the enhancement of Aβ clearance.…”

Section: Apoa-i and Aβmentioning

confidence: 99%

“…Some intriguing hypothesis on the role of HDL and its associated proteins in brain function and their influence on neurodegeneration, have also been formulated [5,32,33]. This influence could be indirect, due the reported beneficial effects of HDLs on the cardiovascular system, then reflected in the brain [5].…”

Section: Introductionmentioning

confidence: 99%

HDL Proteome and Alzheimer’s Disease: Evidence of a Link

et al. 2020

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Several lines of epidemiological evidence link increased levels of high-density lipoprotein-cholesterol (HDL-C) with lower risk of Alzheimer’s disease (AD). This observed relationship might reflect the beneficial effects of HDL on the cardiovascular system, likely due to the implication of vascular dysregulation in AD development. The atheroprotective properties of this lipoprotein are mostly due to its proteome. In particular, apolipoprotein (Apo) A-I, E, and J and the antioxidant accessory protein paraoxonase 1 (PON1), are the main determinants of the biological function of HDL. Intriguingly, these HDL constituent proteins are also present in the brain, either from in situ expression, or derived from the periphery. Growing preclinical evidence suggests that these HDL proteins may prevent the aberrant changes in the brain that characterize AD pathogenesis. In the present review, we summarize and critically examine the current state of knowledge on the role of these atheroprotective HDL-associated proteins in AD pathogenesis and physiopathology.

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“…The dual properties of TTR as both an amyloidogenic protein and an amyloid inhibitor are not fully elucidated and may appear paradoxical. Anti-amyloidogenic properties of amyloid-forming proteins have, however, previously been reported [ 47 ], and the amyloid-interfering effect could possibly even require similar properties between the target and inhibitor.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of Transthyretin Inhibition of IAPP Amyloid Formation

et al. 2021

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Amyloid-formation by the islet amyloid polypeptide (IAPP), produced by the β-cells in the human pancreas, has been associated with the development of type II diabetes mellitus (T2DM). The human plasma-protein transthyretin (TTR), a well-known amyloid-inhibiting protein, is interestingly also expressed within the IAPP producing β-cells. In the present study, we have characterized the ability of TTR to interfere with IAPP amyloid-formation, both in terms of its intrinsic stability as well as with regard to the effect of TTR-stabilizing drugs. The results show that TTR can prolong the lag-phase as well as impair elongation in the course of IAPP-amyloid formation. We also show that the interfering ability correlates inversely with the thermodynamic stability of TTR, while no such correlation was observed as a function of kinetic stability. Furthermore, we demonstrate that the ability of TTR to interfere is maintained also at the low pH environment within the IAPP-containing granules of the pancreatic β-cells. However, at both neutral and low pH, the addition of TTR-stabilizing drugs partly impaired its efficacy. Taken together, these results expose mechanisms of TTR-mediated inhibition of IAPP amyloid-formation and highlights a potential therapeutic target to prevent the onset of T2DM.

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The Positive Side of the Alzheimer’s Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1

Cited by 40 publications

References 243 publications

Change in the plasma proteome associated with canine cognitive dysfunction syndrome (CCDS) in Thailand

Change in the plasma proteome associated with canine cognitive dysfunction syndrome (CCDS) in Thailand

HDL Proteome and Alzheimer’s Disease: Evidence of a Link

Mechanisms of Transthyretin Inhibition of IAPP Amyloid Formation

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