‘The awesome power of yeast’ in Alzheimer’s disease research
Sudip Dhakal
+ Author Affiliations
- Author Affiliations
School of Science, RMIT University, Bundoora, Vic. 3083, Australia. Email: sudip.dhakal@rmit.edu.au; dhakal.sudip001@gmail.com
Microbiology Australia 42(3) 130-133 https://doi.org/10.1071/MA21034
Submitted: 6 July 2021 Accepted: 7 August 2021 Published: 6 September 2021
Journal Compilation © The Authors 2021 Open Access CC BY-NC-ND, published (by CSIRO Publishing) on behalf of the ASM
Abstract
The difficulties in performing experimental studies related to diseases of the human brain have fostered a range of disease models from highly expensive and complex animal models to simple, robust, unicellular yeast models. Yeast models have been used in numerous studies to understand Alzheimer’s disease (AD) pathogenesis and to search for drugs targeting AD. Thanks to the conservation of fundamental eukaryotic processes including ageing and the availability of appropriate technological platforms, budding yeast are a simple model eukaryote to assist with understanding human cell biology, offering a platform to study human diseases. This article aims to provide insights from yeast models on the contributions of amyloid beta, a causative agent in AD, and recent research findings on AD chemoprevention.
References
[1] (2021) 2021 Alzheimer’s disease facts and figures. Alzheimers Dement. 17, 327–406.| 2021 Alzheimer’s disease facts and figures.Crossref | GoogleScholarGoogle Scholar | 33756057PubMed |
[2] Abeysinghe, A.A.D.T. et al. (2020) Alzheimer’s disease; a review of the pathophysiological basis and therapeutic interventions. Life Sci. 256, 117996.
| Alzheimer’s disease; a review of the pathophysiological basis and therapeutic interventions.Crossref | GoogleScholarGoogle Scholar |
[3] Schneider, L. (2020) A resurrection of aducanumab for Alzheimer’s disease. Lancet Neurol. 19, 111–112.
| A resurrection of aducanumab for Alzheimer’s disease.Crossref | GoogleScholarGoogle Scholar | 31978357PubMed |
[4] Mahase, E. (2021) FDA approves controversial Alzheimer’s drug despite uncertainty over effectiveness. BMJ 373, 373.
[5] Dhakal, S. and Macreadie, I. (2020) Protein homeostasis networks and the use of yeast to guide interventions in Alzheimer’s disease. Int. J. Mol. Sci. 21, 8014.
| Protein homeostasis networks and the use of yeast to guide interventions in Alzheimer’s disease.Crossref | GoogleScholarGoogle Scholar |
[6] Dhakal, S. et al. (2019) Dietary polyphenols: a multifactorial strategy to target Alzheimer’s disease. Int. J. Mol. Sci. 20, 5090.
| Dietary polyphenols: a multifactorial strategy to target Alzheimer’s disease.Crossref | GoogleScholarGoogle Scholar |
[7] Khurana, V. and Lindquist, S. (2010) Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker’s yeast? Nat. Rev. Neurosci. 11, 436–449.
| Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker’s yeast?Crossref | GoogleScholarGoogle Scholar | 20424620PubMed |
[8] Mcdonald, J.B. et al. (2020) Yeast contributions to Alzheimer’s disease. J. Human Clin. Genet. 2, 1–19.
| Yeast contributions to Alzheimer’s disease.Crossref | GoogleScholarGoogle Scholar |
[9] Seynnaeve, D. et al. (2018) Recent insights on Alzheimer’s disease originating from yeast models. Int. J. Mol. Sci. 19, 1947.
| Recent insights on Alzheimer’s disease originating from yeast models.Crossref | GoogleScholarGoogle Scholar |
[10] Macreadie, I. and Luu, Y.N. (2018) How yeast can inform us about healthy aging. Open J. Soc. Sci. 6, 24–31.
| How yeast can inform us about healthy aging.Crossref | GoogleScholarGoogle Scholar |
[11] San Gil, R. et al. (2017) The heat shock response in neurons and astroglia and its role in neurodegenerative diseases. Mol. Neurodegener. 12, 65.
| The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.Crossref | GoogleScholarGoogle Scholar | 28923065PubMed |
[12] Richter, K. et al. (2010) The heat shock response: life on the verge of death. Mol. Cell 40, 253–266.
| The heat shock response: life on the verge of death.Crossref | GoogleScholarGoogle Scholar | 20965420PubMed |
[13] Torggler, R. et al. (2017) Assays to monitor autophagy in Saccharomyces cerevisiae. Cells 6, 23.
| Assays to monitor autophagy in Saccharomyces cerevisiae.Crossref | GoogleScholarGoogle Scholar |
[14] Vandebroek, T. et al. (2005) Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 44, 11466–11475.
| Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast.Crossref | GoogleScholarGoogle Scholar | 16114883PubMed |
[15] Caine, J. et al. (2007) Alzheimer’s Aβ fused to green fluorescent protein induces growth stress and a heat shock response. FEMS Yeast Res. 7, 1230–1236.
| Alzheimer’s Aβ fused to green fluorescent protein induces growth stress and a heat shock response.Crossref | GoogleScholarGoogle Scholar | 17662055PubMed |
[16] Chen, X. and Petranovic, D. (2015) Amyloid-β peptide-induced cytotoxicity and mitochondrial dysfunction in yeast. FEMS Yeast Res. 15, fov061.
| Amyloid-β peptide-induced cytotoxicity and mitochondrial dysfunction in yeast.Crossref | GoogleScholarGoogle Scholar | 26152713PubMed |
[17] Dhakal, S. et al. (2019) Simvastatin efficiently reduces levels of Alzheimer’s amyloid beta in yeast. Int. J. Mol. Sci. 20, 3531.
| Simvastatin efficiently reduces levels of Alzheimer’s amyloid beta in yeast.Crossref | GoogleScholarGoogle Scholar |
[18] Chen, X. et al. (2020) FMN reduces amyloid-β toxicity in yeast by regulating redox status and cellular metabolism. Nat. Commun. 11, 867.
| FMN reduces amyloid-β toxicity in yeast by regulating redox status and cellular metabolism.Crossref | GoogleScholarGoogle Scholar | 32054832PubMed |
[19] Porzoor, A. et al. (2015) Anti-amyloidogenic properties of some phenolic compounds. Biomolecules 5, 505–527.
| Anti-amyloidogenic properties of some phenolic compounds.Crossref | GoogleScholarGoogle Scholar | 25898401PubMed |
[20] Wolozin, B. et al. (2007) Simvastatin is associated with a reduced incidence of dementia and Parkinson’s disease. BMC Med. 5, 20.
| Simvastatin is associated with a reduced incidence of dementia and Parkinson’s disease.Crossref | GoogleScholarGoogle Scholar | 17640385PubMed |
[21] Carabott, M. et al. (2021) Lipids, statins and susceptibility to SARS-CoV-2 and influenza A viruses. Microbiol. Aust. 42, 87–91.
| Lipids, statins and susceptibility to SARS-CoV-2 and influenza A viruses.Crossref | GoogleScholarGoogle Scholar |
[22] Hottman, D.A. and Li, L. (2014) Protein prenylation and synaptic plasticity: implications for Alzheimer’s disease. Mol. Neurobiol. 50, 177–185.
| Protein prenylation and synaptic plasticity: implications for Alzheimer’s disease.Crossref | GoogleScholarGoogle Scholar | 24390573PubMed |
[23] Luu, Y.N. and Macreadie, I. (2018) Development of convenient system for detecting yeast cell stress, including that of amyloid beta. Int. J. Mol. Sci. 19, 2136.
| Development of convenient system for detecting yeast cell stress, including that of amyloid beta.Crossref | GoogleScholarGoogle Scholar |
[24] Bharadwaj, P.R. et al. (2012) Latrepirdine (dimebon) enhances autophagy and reduces intracellular GFP-Aβ42 levels in yeast. J. Alzheimers Dis. 32, 949–967.
| Latrepirdine (dimebon) enhances autophagy and reduces intracellular GFP-Aβ42 levels in yeast.Crossref | GoogleScholarGoogle Scholar | 22903131PubMed |
[25] McDonald, J.B. et al. (2021) A toxic synergy between aluminium and amyloid beta in yeast. Int. J. Mol. Sci. 22, 1835.
| A toxic synergy between aluminium and amyloid beta in yeast.Crossref | GoogleScholarGoogle Scholar | 33673244PubMed |
[26] Dhakal, S. and Macreadie, I. (2020) Tyramine and amyloid beta 42: a toxic synergy. Biomedicines 8, 145.
| Tyramine and amyloid beta 42: a toxic synergy.Crossref | GoogleScholarGoogle Scholar |
[27] Dhakal, S. and Macreadie, I. (2021) Potential contributions of trace amines in Alzheimer’s disease and therapeutic prospects. Neural Regen. Res. 16, 1394–1396.
| Potential contributions of trace amines in Alzheimer’s disease and therapeutic prospects.Crossref | GoogleScholarGoogle Scholar | 33318424PubMed |
[28] Bell, S.M. et al. (2021) Mitochondrial dysfunction in Alzheimer’s disease: a biomarker of the future? Biomedicines 9, 63.
| Mitochondrial dysfunction in Alzheimer’s disease: a biomarker of the future?Crossref | GoogleScholarGoogle Scholar | 33440662PubMed |
