BIOMARKERS OF OXIDE-CARBONYL STRESS IN RATS WITH GUERIN’S CARCINOMA DURING THE TUMORS PROGRESSION DEPENDING ON SENSITIVITY TO CISPLATIN
DOI:
https://doi.org/10.32471/oncology.2663-7928.t-23-3-2021-g.9805Keywords:
Guérin’s carcinoma, markers, oxidative-carbonyl stress, sensitivity to cisplatin, альбумінAbstract
Aim: to investigate changes in markers of oxidative-carbonyl stress during the progression of Guerin’s carcinoma with different sensitivity to cisplatin and to establish their relation with molecular-structural changes of blood plasma albumin. Object and methods: the work was performed on Wistar rats (females aged 2.5 months and weighing 180–200 g) with transplanted cisplatin-sensitive or -resistant strains of Guerin’s carcinoma. The biological material for the analysis was taken on days 3, 5, 7, 9, 14, 18 and 21 after the implantation. In the research, there were determined prooxidant-antioxidant ratio and catalase activity in the hemolysate, the content of malonic dialdehyde (MDA) in the blood plasma, the content of free SH groups and fructosamine in the albumin molecule and the concentration of aldehyde dinitrophenylhydrazones in the blood plasma albumin fractions. Conformational changes occurring in the plasma albumin molecule were evaluated by absorption and fluorescence spectroscopy. Results: in the dynamics of carcinoma growth, there was detected an increase (compared with the intact control) in the pro-antioxidant ratio which had two peaks that were associated with the onset of active tumor growth on days 5, 18 (sensitive strain) and 9, 21 (cisplatin-resistant strain) after the transplantation. Throughout the experiment, an intensification of lipid peroxidation in the blood plasma of the tumor-bearing rats against gradual decrease in the catalase activity of the hemolysates was observed. The highest values of MDA were registered since day 9 until 21 after the tumor transplantation in the group of rats bearing cisplatin-resistant strain. There was shown a decrease in free sulfhydryl groups alongside with an increase in oxidative modification, glyoxidation end products and polymer cross-linked amyloid-type β-structures in the albumin pool of the rat blood plasma depending on the stage of development and the type of Guerin’s carcinoma strain. Significant changes in the molecular conformation of the albumin of the rat’s blood plasma in accordance with the external microenvironment formed in the blood plasma were observed. Conclusions: the obtained data suggest the presence of progressive oxidative carbonyl stress in rats with Guerin’s carcinoma which can be considered both as a trigger of tumor development and as an acquisition of high malignancy by neoplastic cells. The relation between oxidative carbonyl stress and molecular and structural changes of blood plasma albumin was demonstrated. The results can be used to improve the differential diagnosis of tumors, and the studied indicators can enrich the panel of non-tumor markers of the tumor development and the disease course.
References
Fedorenko ZP, Mykhaylovych YuY, Hulak LO, et al. Cancer in Ukraine, 2019–2020. Bulletin of the National Cancer Registry of Ukraine. Kyiv: National Cancer Institute, 2021; 22. 145 p. (in Ukrainian).
Colombo N, Creutzberg C, Amant F, et al. ESMO-ESGO-ESTRO Consensus сonference on еndometrial сancer: diagnosis, treatment and follow-up. Ann Oncol 2016; 27: 16–41.
Bray F, Ferlay J, Soerjomataram I, et al. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 2018; 68: 394–424.
Fulda S. Evasion of apoptosis as a cellular stress response in cancer. Int J Biochem Cell Biol 2010; 2010:1–6.
Elstrom RL, Bauer DE, Buzzai M, et al. Act stimulates aerobic glycolysis in cancer cells. Cancer Res 2004; 64: 3892–9.
Valko M, Leibfritz D, Moncol J, et al. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 2007; 39 (1): 44–84.
Goroshinskaya IА, Medvedeva DE, Surikova EI, et al. The state of oxidative metabolism in the blood of gastric cancer patients with various tumor histotypes. Modern problems of science and education 2019; 1: http://science-education.ru/ru/article/view?id=28440 (in Rissian).
Muravleva LYe, Sirota VB, Zhumakaeva SS, et al. Oxidative stress in breast cancer. Modern problems of science and education 2019; 1: http://science-education.ru/ru/article/view?id=28590 (in Rissian).
Breusing N, Grune T, Andrisic L, et al. An interlaboratory validation of methods of lipid peroxidation measurement in UVA-treated human plasma samples. Free Radical Research 2010; 44 (10): 1203–15.
Grimsrud PA, Hongwei X, Griffin TJ, Bernlohr DA. Oxidative stress and covalent modification of protein with bioactive aldehydes. J Biol Chem 2008; 283 (32): 21837–41.
Singh R, Barben F, Mori T, Beilin L. Advanced glication end-products: a review. Diabetologia 2001; 44 (2): 129–46.
Baynes JW. From life to death — the struggle between chemistry and biology during aging: the Maillard reaction as an amplifier of genomic damage. Biogerontology 2000; 1 (3): 235–46.
Schalkwijk CG, Stehouwer CDA, Hinsbergh VWM. Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification. Diabetes Metab Res Rev 2004; 20 (5): 369–82.
Mossine VV, Mawhinney TP. 1-Amino-1-deoxy-D-fructose («fructosamine») and its derivatives. Adv Carbohydr Chem Biochem 2010; 64: 291–402.
Cho S-J, Roman G, Yeboah F, et al. The road to advanced glycation end products: a mechanistic perspective. Curr Med Chem 2007; 14 (15): 1653–71.
Krautwald M, Münch G. Advanced glycation end products as biomarkers and gerontotoxins — A basis to explore methylglyoxal-lowering agents for Alzheimer’s disease? Experimental Gerontology 2010; 45 (10): 744–51.
Monnier VM. Intervention against the Maillard reaction in vivo. Arch Biochem Biophys 2003; 419 (1): 1–15.
Shaikh S, Nicholson LF. Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation. J Neurosci Res 2008; 86 (9): 2071–82.
Fuentealba D, Friguet B, Silva E. Advanced Glycation Endproducts Induce Photocrosslinking and Oxidation of Bovine Lens Proteins Through Type‐I Mechanism. Photochem Photobiol 2009; 85 (1): 185–94.
Li W, Gao H, Mu H, et al. Three different active aldehydes induce the production of advanced lipoxidation end products upon incubation with bovine serum albumin. Europ. J of Lipid Scien Techn 2015; 17 (9): 1432–43.
Kuhla B, Luth HJ, Haferburg D, et.al. Methylglyoxal, glyoxal, and their detoxification in Alzheimer’s disease. Ann NY Acad Sci 2005; 1043 (1): 211–16.
Glenn J, Stitt A. The role of advanced glycation end products in retinal ageing and disease. Biochim Biophys Acta 2009; 1790 (10): 1109–16.
Kalousova M, Zima T, Tesar V, et.al. Soluble Receptor for advanced glycation end products in patients with decreased renal function. Mutation Research. Fundamental and Molecular Mechanisms of Mutagenesis 2005; 579 (1–2): 37–46.
Singh VP, Bali A, Singh N, Jaggi AS. Advanced glycation end products and diabetic complications. Korean J Physiol Pharmacol 2014; 18 (1): 14.
Lozinska LM, Semchyshyn GM. Biological aspects of non-enzymatic glycosylation. Ukr biochemistry Journal 2012; 84 (5): 16–37 (in Ukrainian).
Turpaev KT. Signal system Keap1-Nrf2. Regulation mechanism and importance for the protection of cells from the toxic effects of xenobiotics and electrophilic compounds. Biochemistry 2013; 78 (2): 147–66 (in Rissian).
Nishizawa Y, Koyama H. Endogenous secretory receptor for advanced glycation endproducts and cardiovascular disease in end-stage renal disease. J Ren Nutr 2008; 18 (1): 76–82.
Sofyina ZP, Syrkina AB, Goldina A, Kleina A. Experimental evaluation of anticancer drugs in the USSR and the USA. Moscow: Medicine, 1980. 296 p. (in Rissian).
Serkiz II, Druzhina NA, Khrienko AP, et al. Chemiluminescence of blood under radiation exposure. Kyiv: Naukova Dumka, 1989. 176 p. (in Russian).
Druzhyna MO, Makovetska LI, Glavin OA, et al. The freeradical processes in peripheral blood of patients with benign breast disease. Oncology 2018; 78 (4): 250–4 (in Ukrainian).
Korolyuk MA, Ivanova LI, Mayorova IG. Method for determining the activity of catalase. Laboratory work 1988; 1: 16–9 (in Russian).
Stal’naya ID, Garishvili TG. Method for determination of malondialdehyde using thiobarbituric acid. In: Modern methods n biochemistry. Orekhovich VN (ed). Moscow: Meditsina, 1997: 66–8 (in Russian).
Haynes R, Osuga DT, Feeney RE. Modification of amino groups in inhibitors of proteolytic enzymes. Biochemistry 1967; 6 (2): 541–7.
Levine RL, Garland D, Oliver CN, et al. Determination of carbonyl content in oxidatively modified proteins. Meth Enzymol 1990; 186: 464–78.
Dubinina EE, Burmistrov SO, Khodov DA, Porotov IG. Oxidative modification of human blood serum proteins, a method for its determination. Questions of medicinal chemistry 1995; 41 (1): 24–6 (in Russian).
Johnson RN, Mercalf PA, Baker JR. Fructosamine: a new approach to the estimation of serum glycosyl protein. Clin Chem Acta 1982; 137: 87–9.
Alok R, Sidra I, Brijesh KM, et al. Optical screening of glycationinduced structural alterations in serum proteins of diabetes patients using spectroscopic techniques. IJNTR 2016; 5: 44–8.
Lakin GF. Biometry. Moscow: Vyschaya Shkola, 1990. 352 p. (in Russian)
Dubinina EE, Pustygina AV. Oxidative modification of proteins, its role in pathological conditions. Ukrbiochem journal 2008; 80 (6): 5–18
Hauck AK, Bernlohr DA. Oxidative stress and lipotoxicity. J Lipid Res 2016; 57 (11): 1976–86.
Plowman JE, Deb-Choudhury S, Grosvenor AJ, Dyer JM. Protein oxidation: Identification and utilisation of molecular markers to differentiate singlet oxygen and hydroxyl radical-mediated oxidative pathways. Photochem Photobiol Sci 2013; 12 (11): 1960–7.
Gubsky YuI, et al. Toxicological consequences of oxidative modification of proteins in various pathological conditions. Modern problems of toxicology 2005; 8 (3): 20–7 (in Russian)
Turell L, Radi R, Alvarez B. The thiol pool in human plasma: the central contribution of albumin to redox processes. Free Radic Biol Med 2013; 65: 244–53.
Dubinina EE. Oxygen metabolism products in the functional cell activity (life and death, creation and destruction). Physiological and clinical and biochemical aspects. SPb: Publishing house «Medical Press», 2006. 400 p. (in Russian)
Feeney MB, Schwneich C. Tyrosine modifications in aging. Antioxid Redox Signal 2012; 7 (1): 1571–9.
Kay P, Wagner JR, Gagnon H, et al. Modification of peptide and protein cysteine thiol groups by conjugation with a degradation product of ascorbate. Chem Res Toxicol 2013; 26 (9): 1333–9.
Kurian GA, Rajagopal R, Vedantham S, Rajesh M. The role of oxidative stress in myocardial ischemia and reperfusion injury nd remodeling: revisited. Oxid Med Cell Longev 2016; 2016: 1656450.
