Journal of Alzheimers Disease & Parkinsonism
Open Access

Possible Prevention of Alzheimer’s Disease by Aldehyde Dehydrogenase: A Perspective Review

Tetsumori Yamashima^*

Departments of Psychiatry and Behavioral Science and Cell Metabolism and Nutrition, Kanazawa University Graduate School of Medical Science, Japan

Received Date: Mar 19, 2020 / Accepted Date: Jun 04, 2020 / Published Date: Jun 11, 2020

Citation: Yamashima T (2020) Possible Prevention of Alzheimer’s Disease by Aldehyde Dehydrogenase: A Perspective Review. J Alzheimers Dis Parkinsonism 10:489.

Copyright: © 2020 Yamashima T. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Investigating the mechanism of neuronal death in Alzheimer’s disease is difficult, because only a tiny percentage of neurons are degenerating at any time point during the long prodromal period. Epidemiological, genetic, biochemical and animal model studies have attributed excessive aldehyde load as a cause of Alzheimer neuronal death. Focusing on toxic aldehydes will help fill gaps in our knowledge that cannot be explained by the amyloid β or tau hypotheses. Hydroxynonenal is formed by peroxidation of membrane lipids and LDL or during deep-frying of vegetable oils. It carbonylates Hsp70.1, a heat shock protein with the dual functions of a chaperone protein and lysosomal stabilizer. Hydroxynonenal-mediated Hsp70.1 carbonylation followed by calpain-mediated cleavage of carbonylated Hsp70.1, causes lysosomal neuronal death (the ‘calpain-cathepsin hypothesis’). Aldehyde dehydrogenase (ALDH) participates in the removal of not only ethanol-derived acetaldehyde, but also linoleic acid-derived hydroxynonenal. This review describes how scavenging hydroxynonenal by ALDH enzymes prevent Alzheimer’s disease.

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