Age-associated changes in amyloid-β and formaldehyde concentrations in cerebrospinal fluid of rhesus monkeys

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Abstract

A: Intergroup analyses of Aβ40 concentrations. B: Intergroup analyses of Aβ42 concentrations. C: Intergroup analyses of FA concentrations. D: Correlation between CSF Aβ40 and FA concentrations in young group (R=–0.3385, P=0.2172). E: Correlation between CSF Aβ40 and FA concentrations in middle-aged group (R=0.02914, P=0.8976). F: Correlation between CSF Aβ40 and FA concentrations in aged group (R=–0.5318, P=0.0158). G: Correlation between CSF Aβ42 and FA concentrations in young group (R=–0.379, P=0.1635). H: Correlation between CSF Aβ42 and FA concentrations in middle-aged group (R=0.4296, P=0.046). I: Correlation between CSF Aβ42 and FA concentrations in aged group (R=–0.5344, P=0.0184). Error bars indicate mean± standard deviation (SD). *: P<0.05, **:P<0.01, ***:P<0.001. Aβ: β-amyloid; CSF: Cerebrospinal fluid.

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Methanol and formic acid toxicity: biochemical mechanisms.

Jyrki Liesivuori, and Savolainen (1991)

Metabolism of methanol, methyl ethers, esters and amides give rise to formic acid. This acid is an inhibitor of the mitochondrial cytochrome oxidase causing histotoxic hypoxia. Formic acid is a weaker inhibitor than cyanide and hydrosulphide anions. The body burden of formate in methanol poisoning is high enough to cause acidosis, and other clinical symptoms. Part of the protons can be attributed to formic acid whereas the most significant acid load results from the hypoxic metabolism. The acidosis causes e.g. dilatation of cerebral vessels, facilitation of the entry of calcium ions into cells, loss of lysosomal latency and deranged production of ATP. The latter effect seems to impede parathormone-dependent calcium reabsorption in the kidney tubules. Besides, urinary acidification is affected by formic acid. Its excretion causes continuous recycling of the acid by the tubular cell Cl-/formate exchanger. This sequence of events may partially explain an accumulation of formate in urine. Occupational exposure to vapours of methanol and formic acid can be quantitatively monitored by urinary formic acid determinations. Formic acid toxicity may prove a suitable model for agents causing histotoxic hypoxia.

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Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease.

Nu-Fang Fang, Lan Guo, Doris Chen … (2011)

Amyloid-β (Aβ) peptide-binding alcohol dehydrogenase (ABAD), an enzyme present in neuronal mitochondria, exacerbates Aβ-induced cell stress. The interaction of ABAD with Aβ exacerbates Aβ-induced mitochondrial and neuronal dysfunction. Here, we show that inhibition of the ABAD-Aβ interaction, using a decoy peptide (DP) in vitro and in vivo, protects against aberrant mitochondrial and neuronal function and improves spatial learning/memory. Intraperitoneal administration of ABAD-DP [fused to the transduction of human immunodeficiency virus 1-transactivator (Tat) protein and linked to the mitochondrial targeting sequence (Mito) (TAT-mito-DP) to transgenic APP mice (Tg mAPP)] blocked formation of ABAD-Aβ complex in mitochondria, increased oxygen consumption and enzyme activity associated with the mitochondrial respiratory chain, attenuated mitochondrial oxidative stress, and improved spatial memory. Similar protective effects were observed in Tg mAPP mice overexpressing neuronal ABAD decoy peptide (Tg mAPP/mito-ABAD). Notably, inhibition of the ABAD-Aβ interaction significantly reduced mitochondrial Aβ accumulation. In parallel, the activity of mitochondrial Aβ-degrading enzyme PreP (presequence peptidase) was enhanced in Tg mAPP mitochondria expressing the ABAD decoy peptide. These data indicate that segregating ABAD from Aβ protects mitochondria/neurons from Aβ toxicity; thus, ABAD-Aβ interaction is an important mechanism underlying Aβ-mediated mitochondrial and neuronal perturbation. Inhibitors of ABAD-Aβ interaction may hold promise as targets for the prevention and treatment of Alzheimer's disease.

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Accumulated hippocampal formaldehyde induces age-dependent memory decline.

J. Zhou, Hongjun Luo, Xiaohui Wang … (2013)

Aging is an important factor in memory decline in aged animals and humans and in Alzheimer's disease and is associated with the impairment of hippocampal long-term potentiation (LTP) and down-regulation of NR1/NR2B expression. Gaseous formaldehyde exposure is known to induce animal memory loss and human cognitive decline; however, it is unclear whether the concentrations of endogenous formaldehyde are elevated in the hippocampus and how excess formaldehyde affects LTP and memory formation during the aging process. In the present study, we report that hippocampal formaldehyde accumulated in memory-deteriorating diseases such as age-related dementia. Spatial memory performance was gradually impaired in normal Sprague-Dawley rats by persistent intraperitoneal injection with formaldehyde. Furthermore, excess formaldehyde treatment suppressed the hippocampal LTP formation by blocking N-methyl-D-aspartate (NMDA) receptor. Chronic excess formaldehyde treatment over a period of 30 days markedly decreased the viability of the hippocampus and down-regulated the expression of the NR1 and NR2B subunits of the NMDA receptor. Our results indicate that excess endogenous formaldehyde is a critical factor in memory loss in age-related memory-deteriorating diseases.

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Author and article information

Contributors

Rong-Qiao He

Xin-Tian Hu

Journal

Journal ID (nlm-ta): Zool Res

Journal ID (iso-abbrev): Zool Res

Journal ID (publisher-id): ZR

Title: Zoological Research

Publisher: Science Press (16 Donghuangchenggen Beijie, Beijing 100717, China )

ISSN (Print): 2095-8137

Publication date (Print): July 2020

Volume: 41

Issue: 4

Pages: 444-448

Affiliations

[1 ] Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China

[2 ] Kunming College of Life Science, University of the Chinese Academy of Sciences, Kunming, Yunnan 650204, China

[3 ] School of Basic Medical Sciences, Dali University, Dali, Yunnan 671000, China

[4 ] CAS Center for Excellence in Brain Science, Chinese Academy of Sciences, Shanghai 200031, China

[5 ] Kunming Primate Research Center and National Research Facility for Phenotypic & Genetic Analysis of Model Animals (Primate Facility), Chinese Academy of Sciences, Kunming, Yunnan 650223, China

[6 ] State Key Laboratory of Brain and Cognitive Science, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China

Author notes

E-mail: xthu@ 123456mail.kiz.ac.cn

xthu@ 123456mail.kiz.ac.cn

#Authors contributed equally to this work

Article

Publisher ID: zr-41-4-444

DOI: 10.24272/j.issn.2095-8137.2020.088

PMC ID: 7340526

PubMed ID: 32543791

SO-VID: 47a428bc-7ee3-4fed-9b2f-3512c708fb9e

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This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

History

Date received : 17 April 2020

Date accepted : 29 May 2020

Funding

This study was supported by the National Key R&D Program of China (2018YFA0801403), Key Realm R&D Program of GuangDong Province (2019B030335001), the Strategic Priority Research Program of the Chinese Academy of Sciences (XDB32060200), the National Natural Science Foundation of China (81941014, 81471312, 81771387, 81460352, 81500983, 31700897, 31700910, 31800901, 31960178, 91732302), the Applied Basic Research Programs of Science and Technology Commission Foundation of Yunnan Province (2017FB109, 2018FB052, 2018FB053, 2019FA007), China Postdoctoral Science Foundation (2018M631105) and CAS “Light of West China” Program

Age-associated changes in amyloid-β and formaldehyde concentrations in cerebrospinal fluid of rhesus monkeys

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Alternative approaches to Alzheimer's Disease

Most cited references 35

Methanol and formic acid toxicity: biochemical mechanisms.

Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease.

Accumulated hippocampal formaldehyde induces age-dependent memory decline.

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