Glycative Stress and the progression of Alzheimer-type Dementia: From the Perspective of Amyloid-beta Clearance
Main Article Content
Abstract
Glycative stress is a conception of a state that causes an excess of carbohydrate-derived or fatty acid-derived short-chain aldehydes in the body. Short-chain aldehydes, which are highly reactive, undergo a carbonylation process with lysine and arginine residues in proteins and form advanced glycation endproducts (AGEs). When postprandial hyperglycemia occurs, open-ring glucose with exposed aldehyde groups (-CHO) increases and various carbohydrate-derived aldehydes are formed simultaneously (this phenomenon is named “aldehyde sparks”). Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme abundant intracellularly as the keystone of defense against glycative stress and plays a role in metabolizing highly toxic glyceraldehyde, however, under diabetic conditions, the enzyme activity is markedly reduced by forming S-(2-succinyl) cysteine-GAPDH. We also found that a high-fat diet reduced GAPDH activity and increased glyceraldehyde and methylglyoxal. High animal fat diets in particular require caution because they increase preference dependence on animal fat. In the lipid-rich brain, they promotes the formation of lipid-derived AGEs formed by methylglyoxal and acrolein providing evidence of their close association with amyloid cascade, ultimately leading to the onset of Alzheimer-type dementia. Through the process of amylod beta (Aβ) glycation modification and cross-linking, Aβ polymerization is promoted and deposited in the brain. Thus, neurotoxicity is aggravated. Furthermore, Aβ progresses toward being persistent and Aβ clearance is reduced. Tau proteins similarly undergo glycation modification and trigger polymerization. methylglyoxal or acrolein-derived glycated Aβ clearance by primary microglia cultured cells reduced significantly compared to the unglycated Aβ provides evidence of the reduced clearance upon glycation. It was also shown that melatonin, which promotes glycolytic cross-linking degradation, may promote microglial Aβ phagocytosis. We next plan to examine the potential of plant extracts that promote glycation cross-linking degradation to improve Aβ phagocytosis. Advanced Alzheimer-type dementia with a disoriented neural network hardly recovers with treatment. In this review article, we discussed possible future therapeutic strategies for Alzheimer-type dementia by increasing Aβ clearance from the early stage such as the prevention of Aβ-glycation and the promotion of glycated-Aβ degradation, which may be a paradigm shift.
Keywords:
Glycative Stress, Stress, Dementia, Alzheimer-type Dementia, Amyloid-beta Clearance
Article Details
How to Cite
YONEI, Yoshikazu et al.
Glycative Stress and the progression of Alzheimer-type Dementia: From the Perspective of Amyloid-beta Clearance.
Medical Research Archives, [S.l.], v. 10, n. 12, dec. 2022.
ISSN 2375-1924.
Available at: <https://esmed.org/MRA/mra/article/view/3374>. Date accessed: 25 apr. 2024.
doi: https://doi.org/10.18103/mra.v10i12.3374.
Section
Review Articles
The Medical Research Archives grants authors the right to publish and reproduce the unrevised contribution in whole or in part at any time and in any form for any scholarly non-commercial purpose with the condition that all publications of the contribution include a full citation to the journal as published by the Medical Research Archives.
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3. Yonei Y, Yagi M, Takabe W. Stop the "Vicious Cycle" induced by glycative stress. Glycative Stress Res. 2020;7:13-21.
https://doi.org/10.24659/gsr.7.1_13
4. Yonei Y, Yagi M, Takabe W, Kon M. Skin aging: Oxidative stress and glycative stress. Journal of Society Cosmetic Chemists Japan. 2019;53:83-90. (in Japanese) https://www.jstage.jst.go.jp/article/sccj/53/2/53_83/_pdf
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6. Sato K, Zheng Y, Martin-Morales A, Taira T, Yonei Y.Generation of short chain aldehydes and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Glycative Stress Res. 2022;9:129-34.
https://doi.org/10.24659/gsr.9.3_129
7. Nakajima H, Itakura M, Kubo T, Kaneshige A, Harada N, Izawa T, Azuma Y, Kuwamura M, Yamaji R, Takeuchi T. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) aggregation causes mitochondrial dysfunction during oxidative stress-induced cell death. J Biol Chem. 2017;292:4727-42.
8. Nakano T, Goto S, Takaoka Y, Tseng HP, Fujimura T, Kawamoto S, Ono K, Chen CL. A novel moonlight function of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) for immunomodulation. Biofactors. 2018;44: 597 -608.
9. Miwa I, Kito Y, Okuda J. Purification and characterization of triokinase from porcine kidney. Prep Biochem. 1994;24:203-23.
10. Nagai R, Brock JW, Blatnik M, Baatz JE, Bethard J, Walla MD, Thorpe SR, Baynes JW, Frizzell N. Succination of protein thiols during adipocyte maturation: A biomarker of mitochondrial stress. J Biol Chem. 2007;282:34219-28.
11. Frizzell N, Rajesh M, Jepson MJ, Nagai N, Carson JA, Thorpe SR, Baynes JW. Succination of thiol groups in adipose tissue proteins in diabetes: Succination inhibits polymerization and secretion of adiponectin. J Biol Chem. 2009;284: 25772-81.
12. Blatnik M, Thorpe SR, Baynes JW. Succination of proteins by fumarate: mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes. Ann N Y Acad Sci. 2008;1126:272-5.
13. Adam J, Ramracheya R, Chibalina MV, Ternette N, Hamilton A, Tarasov AI, Zhang Q, Rebelato E, Rorsman NJG, Martín-Del-Río R, Lewis A, Özkan G, Do HW, Spégel P, Saitoh K, Kato K, Igarashi K, Kessler BM, Pugh CW, Tamarit-Rodriguez J, Mulder H, Clark A, Frizzell N, Soga T, Ashcroft FM, Silver A, Pollard PJ, Rorsman P. Fumarate hydratase deletion in pancreatic β cells leads to progressive diabetes. Cell Rep. 2017;20:3135-48.
14. Martin-Morales A, Arakawa T, Sato M, Matsumura Y, Mano-Usui F, Ikeda K, Inagaki N, Sato K. Development of a method for quantitation of glyceraldehyde in various body compartments of rodents and humans. J Agric Food Chem. 2021;69:13246-54.
15. Schalkwijk CG, Stehouwer CDA. Methylglyoxal, a highly reactive dicarbonyl compound, in diabetes, its vascular complications, and other age-related diseases. Physiol Rev. 2020;100: 407-61.
16. Masuzaki H, Kozuka C, Yonamine M, Shimabukuro M. Brown rice-specific γ-oryzanol-based novel approach toward lifestyle-related dysfunction of brain and impaired glucose metabolism. Glycative Stress Res. 2017;4:58-66.
https://doi.org/10.24659/gsr.4.1_058
17. Masuzaki H, Kozuka C, Okamoto S, Yonamine M, Tanaka H, Shimabukuro M. Brown rice-specific γ-oryzanol as a promising prophylactic avenue to protect against diabetes mellitus and obesity in humans. J Diabetes Investig. 2019;10:18-25.
18. Schwartz M, Barush K. The resolution of neuro-inflammation in neuro-degeneration: Leukocyte recruitment via the choroid plexus. EMBO J. 2014;33:7-22.
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