THE INFLUENCE OF PROLONGED STRESS ON THE ACTIVITY OF BLOOD ENZYMES IN THE CONDITIONS OF WAR IN UKRAINE

I. I. Tokmenko; G.I. Malyshevska; N. O. Posternak

doi:10.21802/artm.2023.2.26.242

Автор(и)

I. I. Tokmenko Bogomolets National Medical University, Department of Medical Biochemistry and Molecular Biology, Kyiv, Ukraine https://orcid.org/0000-0002-8796-8457
G.I. Malyshevska Bogomolets National Medical University, Department of Medical Biochemistry and Molecular Biology, Kyiv, Ukraine https://orcid.org/0000-0001-9953-8641
N. O. Posternak Bogomolets National Medical University, Department of Medical Biochemistry and Molecular Biology, Kyiv, Ukraine https://orcid.org/0000-0002-4501-5463

DOI:

https://doi.org/10.21802/artm.2023.2.26.242

Ключові слова:

stress, superoxidedismutase, catalase, glutathioneperoxidase, glutathionetransferase

Анотація

The article presents an analysis of scientific works on the effect of long-term stress on blood enzymes. It has been determined that enzymopathies include a wide range of diseases, the cause of which is a malfunction of enzymes. Understanding the mechanisms of the occurrence of such disorders is necessary for the search for new, effective methods of their treatment. In the course of the work, twenty scientific works in English, published in the period 2000-2021, were analyzed, which investigated the mechanisms of human enzyme disorders. It has been established that non-genetic factors, such as injuries or stress, can lead to enzyme malfunctions. Stress factors, such as physical injuries, can affect enzyme dysfunction. One of the ways in which stress affects the functioning of enzymes is a change in their activity in biochemical mechanisms. Mutations in the three-dimensional structure of enzymes are one of the main mechanisms underlying the disruption of enzyme activity under the influence of stress. Since enzymes are large proteins that often have a complex tertiary structure that is important for their functioning, mutations that affect this structure can change their catalytic activity, substrate specificity, and stability, leading to enzymopathies. The stress factor of war is not similar to everyday stress factors, because it exceeds a person's ability to adapt to the action of the stress factor. The results of the research and analysis of research indicate the significant role of stress in disrupting the work of antioxidant blood enzymes. As a result of the analysis of scientific research, it was established that these enzymes include superoxidedismutase, catalase, glutathioneperoxidase, and glutathionetransferase.

Superoxidedismutase is an antioxidant enzyme that plays a crucial role in protecting cells from the harmful effects of reactive oxygen species. ROS are produced during normal cellular metabolism and can also be produced in response to stressful conditions. A decrease in the activity of superoxidedismutase in the erythrocytes of combatants may occur due to epigenetic changes in the regulation of this enzyme, which were caused by long-term stressful conditions.

Catalase is another antioxidant enzyme that plays an important role in protecting cells from oxidative stress. Another possible cause may be a change in the expression of the genes that code for catalase, which leads to a decrease in the level of the enzyme.

Glutathioneperoxidase is an antioxidant enzyme that helps protect cells from oxidative stress by catalyzing the reduction of hydrogen peroxide and organic hydroperoxides to less harmful compounds. Stressful conditions, in particular combat operations, can lead to an increase in the formation of reactive oxygen species and a decrease in antioxidant defense mechanisms, including glutathioneperoxidase.

Glutathionetransferase catalyzes the conjugation of glutathione, a tripeptide consisting of glutamate, cysteine, and glycine, with electrophilic substrates, resulting in the formation of less reactive and more water-soluble products that are suitable for excretion. Prolonged exposure to stress can lead to depletion of glutathione and a decrease in the activity of this enzyme.

The obtained results indicate that wartime conditions can be a significant factor in the development of disorders of these enzymes.

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Посилання

McCrea HJ, De Camilli P. Mutations in phosphoinositide metabolizing enzymes and human disease. Physiology (Bethesda). 2009 Feb; 24:8-16. doi: 10.1152/physiol.00035.2008

Hyry М, Lantto J and Myllyharju J. Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2. J Biol Chem.2009 Nov 6; 284(45):30917-30924. doi: 10.1074/jbc.M109.021238

Naim HY, Roth J, Sterchi EE, Lentze M, Milla P, Schmitz J and Hauri HP. Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme. J Clin Invest. 1988 Aug; 82(2):667-79. doi: 10.1172/JCI113646.

Helmut Sies, Chapter 13 - Oxidative Stress: Eustress and Distress in Redox Homeostasis, Editor(s): George Fink, Stress: Physiology, Biochemistry, and Pathology. 2019; 13:153-163. doi.org/10.1016/B978-0-12-813146-6.00013-8

Reznichenko NYu. Dosvid profilaktychnoho zastosuvannia vitaminnykh zasobiv u dermatovenerolohichnii praktytsi [Experience of prophylactic use of vitamin products in dermatovenerological practice] Zhurnal dermatovenerolohii ta kosmetolohii im. M.O. Torsuieva. 2016; 1-2:53-60. (Ukrainian)

Cai FF, Song YN, Lu YY, Zhang Y, Hu YY and Su SB. Analysis of plasma metabolic profile, characteristics and enzymes in the progression from chronic hepatitis B to hepatocellular carcinoma. Aging (Albany NY). 2020 Jul 23; 12(14):14949-14965. doi: 10.18632/aging.103554.

Çelik İ, Kars A, Guc D, Tekuzman G and Ruacan Ş. Dihydropyrimidine dehydrogenase enzyme deficiency: clinical and genetic assessment of prevalence in Turkish cancer patients. Cancer Invest. 2002; 20(3):333-9. doi: 10.1081/cnv-120001178.

Nater UM, La Marca R, Florin L, Moses A, Langhans W, Koller MM and Ehlert U. Stress-induced changes in human salivary alpha-amylase activity-associations with adrenergic activity. Psychoneuroendocrinology. 2006 Jan; 31(1):49-58. doi: 10.1016/j.psyneuen.2005.05.010.

Hepp M, Werion A, De Greef A, de Ville de Goyet C, de Bournonville M, Behets C and Craps J. Oxidative stress-induced sirtuin1 downregulation correlates to hif-1α, glut-1, and vegf-a upregulation in th1 autoimmune hashimoto’s thyroiditis. Int J Mol Sci. 2021 Apr; 22(8):3806. doi: 10.3390/ijms22083806

Rha AK, Maguire AS and Martin DR. GM1 gangliosidosis: mechanisms and management. Appl Clin Genet. 2021; 14:209-233. doi: 10.2147/TACG.S206076

Luo X, Hu J, Gao X, Fan Y, Sun Y, Gu X and Qiu W. Novel PYGL mutations in Chinese children leading to glycogen storage disease type VI: two case reports. BMC Med Genet. 2020 Apr 8; 21(1):74. doi: 10.1186/s12881-020-01010-4.

Tamashiro KL, Sakai RR, Shively CA, Karatsoreos IN and Reagan LP. Chronic stress, metabolism, and metabolic syndrome. Stress. 2011 Sep; 14(5):468-74. doi: 10.3109/10253890.2011.606341.

Zhang H, Wei M, Sun Q, Yang T, Lu X, Feng X and Fan H. Lycopene ameliorates chronic stress-induced hippocampal injury and subsequent learning and memory dysfunction through inhibiting ROS/JNK signaling pathway in rats. Food and Chemical Toxicology. 2020. Nov; 145:111688. Available from: https://doi.org/10.1016/j.fct.2020.111688

Djordjevic J, Djordjevic A, Adzic M, Niciforovic A and Radojcic MB. Chronic stress differentially affects antioxidant enzymes and modifies the acute stress response in liver of Wistar rats. Physiol Res. 2010; 59(5):729-736. doi: 10.33549/physiolres.931862.

Bayir H, Kagan VE, Clark RS, Janesko-Feldman K, Rafikov R, Huang Z, Zhang X, Vagni V, Billiar TR and Kochanek PM. Neuronal NOS-mediated nitration and inactivation of manganese superoxide dismutase in brain after experimental and human brain injury. J Neurochem. 2007 Apr; 101(1):168-81. doi: 10.1111/j.1471-4159.2006.04353.x.

Miller MW, Lin AP, Wolf EJ and Miller DR. Oxidative stress, inflammation, and neuroprogression in chronic PTSD. Harv Rev Psychiatry. 2018 Mar/Apr; 26(2):57-69. doi: 10.1097/HRP.0000000000000167.

Al Nimer F, Ström M, Lindblom R, Aeinehban S, Bellander BM, Nyengaard JR and Piehl F. Naturally occurring variation in the glutathione-S-transferase 4 gene determines neurodegeneration after traumatic brain injury. Antioxid Redox Signal. 2013 Mar 1; 18(7):784-794.doi: 10.1089/ars.2011.4440

Lohr JB, Palmer BW, Eidt CA, Aailaboyina S, Mausbach BT, Wolkowitz OM and Jeste DV. Is post-traumatic stress disorder associated with premature senescence? A review of the literature. Am J Geriatr Psychiatry. 2015 Jul; 23(7):709-25. doi: 10.1016/j.jagp.2015.04.001.

Anderson RJ. Shell shock: an old injury with new weapons. Mol Interv. 2008 Oct; 8(5):204-18. doi: 10.1124/mi.8.5.2.

Cenacchi G, Papa V, Pegoraro V, Marozzo R, Fanin M and Angelini C. Danon disease: review of natural history and recent advances. Neuropathol Appl Neurobiol. 2020 Jun; 46(4):303-322. doi: 10.1111/nan.12587.

Hajam YA, Rani R, Ganie SY, Sheikh TA, Javaid D, Qadri SS and Reshi MS. Oxidative stress in human pathology and aging: Molecular mechanisms and perspectives. Cells. 2022 Feb 5; 11(3):552. doi: 10.3390/cells11030552.

Kim TD, Lee S and Yoon S. Inflammation in post-traumatic stress disorder (PTSD): a review of potential correlates of PTSD with a neurological perspective. Antioxidants (Basel). 2020 Jan 26; 9(2):107. doi: 10.3390/antiox9020107.

Sheerin CM, Lind MJ, Bountress KE, Marraccini ME, Amstadter AB, Bacanu SA and Nugent NR. Meta-analysis of associations between hypothalamic pituitary adrenal axis genes and risk of posttraumatic stress disorder. J Trauma Stress. 2020 Oct; 33(5):688-698. doi: 10.1002/jts.22484.