Protein folding vs. COVID-19 and the Mediterranean diet
-
Irena Roterman
and
Leszek Konieczny
Abstract
The experience of the ongoing pandemic gives rise to a variety of questions, touching – among others – upon its biological aspects. Among the most often raised issues is why the situation has deteriorated to such a degree in the Mediterranean basin and the American eastern seaboard. This work identifies possible links between the protein folding process and the aforementioned epidemic. Given the circumstances, it should be regarded as a popular science article.
Research funding: None declared.
Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.
Conflict of interest: The authors declare that they have no conflict of interest.
Ethical approval: The conducted research is not related to either human or animal use.
References
1. Konieczny, L, Roterman, I. The protein is an intelligent micelle. In: Roterman-Konieczna, I, editor. From globular proteins to amyloids. Dordrecht: Elsevier; 2020:241–52 pp.book-chapter.10.1016/B978-0-08-102981-7.00021-XSearch in Google Scholar
2. Ikezoe, Y, Hirota, N, Nakagawa, J, Kitazawa, K. Making water levitate. Nature 1998;393:749–50. https://doi.org/10.1038/31619.Search in Google Scholar
3. Fedorets, AA, Frenkel, M, Shulzinger, E, Dombrovsky, LA, Bormashenko, E, Nosonovsky, M. Self-assembled levitating clusters of water droplets: pattern-formation and stability. Sci Rep 2017;7:1888. https://doi.org/10.1038/s41598-017-02166-5.Search in Google Scholar PubMed PubMed Central
4. Schutzius, TM, Jung, S, Maitra, T, Graeber, G, Köhme, M, Poulikakos, D. Spontaneous droplet trampolining on rigid superhydrophobic surfaces. Nature 2015;527:82–5. https://doi.org/10.1038/nature15738.Search in Google Scholar PubMed
5. Modig, K, Qvist, J, Marshall, CB, Davies, PL, Halle, B. High water mobility on the ice-binding surface of a hyperactive antifreeze protein. Phys Chem Chem Phys 2010;12:10189–97. https://doi.org/10.1039/c002970j.Search in Google Scholar PubMed
6. Banach, M, Konieczny, L, Roterman, I. Why do antifreeze proteins require a solenoid?. Biochimie 2018;144:74–84. https://doi.org/10.1016/j.biochi.2017.10.011.Search in Google Scholar PubMed
7. Wang, M, Kaufmann, RJ. Protein misfolding in the endoplasmic reticulum as a conduit to human disease. Nature 2016;529:326–35. https://doi.org/10.1038/nature17041.Search in Google Scholar PubMed
8. Walter, P, Ron, D. The unfolded protein response: From stress pathway to homeostatic regulation. Science 2011;334:1081–6. https://doi.org/10.1126/science.1209038.Search in Google Scholar PubMed
9. Ding, Q, Dimayuga, E, Markesbery, WR, Keller, JN. Proteasome inhibition increases DNA and RNA oxidation in astrocyte and neuron cultures. J Neurochem 2004;91:1211–8. https://doi.org/10.1111/j.1471-4159.2004.02802.x.Search in Google Scholar PubMed
10. Mimnaugh, EG, Chen, HY, Davie, JR, Celis, JE, Neckers, L. Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response. Biochemistry 1997;36:14418–29. https://doi.org/10.1021/bi970998j.Search in Google Scholar PubMed
11. Halliwell, B. Oxidative stress and neurodegeneration: where are we now?. J Neurochem 2006;97:1634–58. https://doi.org/10.1111/j.1471-4159.2006.03907.x.Search in Google Scholar PubMed
12. Fuertes, G, Villarroya, A, Knecht, E. Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions. Int J Biochem Cell Biol 2003;35:651–64. https://doi.org/10.1016/s1357-2725(02)00382-5.Search in Google Scholar PubMed
13. Torres, C, Lewis, L, Cristofalo, VJ. Proteasome inhibitors shorten replicative life span and induce a senescent-like phenotype of human fibroblasts. J Cell Physiol 2006;207:845–53. https://doi.org/10.1002/jcp.20630.Search in Google Scholar PubMed
14. Martinez-Vicente, M, Sovak, G, Cuervo, AM. Protein degradation and aging. Exp Gerontol 2005;40:622–33. https://doi.org/10.1016/j.exger.2005.07.005.Search in Google Scholar PubMed
15. Johnson, JR, Rajamanoharan, D, McCue, HV, Rankin, K, Barclay, JW. Small heat shock proteins are novel common determinants of alcohol and nicotine sensitivity in Caenorhabditis elegans. Genetics 2016;202:1013–27. https://doi.org/10.1534/genetics.115.185025.Search in Google Scholar PubMed PubMed Central
16. Pignataro, L. Alcohol protects the CNS by activating HSF1 and inducing the heat shock proteins. Neurosci Lett 2019;713:134507. https://doi.org/10.1016/j.neulet.2019.134507.Search in Google Scholar PubMed
17. Guisasola, MC. Role of heat shock proteins in the cardioprotection of regular moderate alcohol consumption. Med Clin (Barc) 2016;146:292–300. https://doi.org/10.1016/j.medcli.2015.12.011.Search in Google Scholar PubMed
18. Yin, SJ, Liao, CS, Chen, CM, Fan, FT, Lee, SC. Genetic polymorphism and activities of human lung alcohol and aldehyde dehydrogenases: Implications for ethanol metabolism and cytotoxicity. Biochem Genet 1992;30:203–15. https://doi.org/10.1007/bf02399709.Search in Google Scholar PubMed
19. Gallina, I, Duxin, JP. A safe fix for alcohol-derived DNA damage. Nature 2020;579:499–500. https://doi.org/10.1038/d41586-020-00462-1.Search in Google Scholar PubMed
20. Rintala, J, Jaatinen, P, Parkkila, S, Sarviharju, M, Kiianmaa, K, Hervonen, A, Niemelä, O. Evidence of acetaldehyde-protein adduct formation in rat brain after lifelong consumption of ethanol. Alcohol Alkohol 2000;35:458–63. https://doi.org/10.1093/alcalc/35.5.458.Search in Google Scholar PubMed
21. Konieczny, L, Roterman, I. The COVID-19 puzzle. Bioinformation 2020;16:418–21.10.6026/97320630016418Search in Google Scholar PubMed PubMed Central
22. Rutkowski, DT, Kaufman, RJ. A trip to the ER: coping with stress. Trends Cell Biol 2004;14:20–8. https://doi.org/10.1016/j.tcb.2003.11.001.Search in Google Scholar PubMed
© 2020 Walter de Gruyter GmbH, Berlin/Boston
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Articles in the same Issue
- Research Articles
- CBIR aided classification using extreme learning machine with probabilistic scaling in MRI brain image
- Feature selection for classification in Steady state visually evoked potentials (SSVEP)-based brain-computer interfaces with genetic algorithm
- Modelling effects of consciousness disorders in brainstem computational model – Preliminary findings
- The use of modern IT solutions for educational purposes on the example of an application enabling to visualize the human eye
- Review
- Technical infrastructure for curriculum mapping in medical education: a narrative review
- Short Communication
- Protein folding vs. COVID-19 and the Mediterranean diet
