ISSN 2415-3060 (print), ISSN 2522-4972 (online)
  • 19 of 47
Up
JMBS 2019, 4(1): 141–148
https://doi.org/10.26693/jmbs04.01.141
Clinical Medicine

Condition of Glutationion Chain of the Thiol-Disulphide System in Patients with Chronic Obstructive Pulmonary Disease and Arterial Hypertension

Tyaglaya O. S.
Abstract

Studying the initial role of oxidative stress in the pathogenesis of chronic obstructive pulmonary disease on the background of arterial hypertension gives prospects for adequate pharmacological correction of this comorbid pathology taking into account all pathogenetic aspects. This is due to oxidative stress which is the causative factor in the delicate balance of the thiol-disulfide system, and also triggers the launch of the caspase mechanism of neutrophil apoptosis with progression and mutual burdening of nosologies. The aim of the study was to evaluate the metabolism of a biologically active tripeptide (consisting of γ-glutamic acid residues, cysteine and glycinute) and thiol-disulfide balance in patients with chronic obstructive pulmonary disease and arterial hypertension. Material and methods. During the study we examined 59 patients. They were divided into 3 subgroups: 23 patients were diagnosed with stage II hypertension disease and stage II chronic obstructive pulmonary disease without a clinically significant concomitant pathology, average age 51.72±1.22 (49.33-54.09) years, gender composition: 22 men and 1 woman, smoking status can be compared with patients with chronic obstructive pulmonary disease. The 2nd group comprised 18 patients with hypertension disease of both sexes aged from 33 to 67 years (average age 50.74±1.49 (47.81-53.76), the ratio of men/ women 17/83%), stage II hypertension disease I-III degree, and different cardiovascular risk, without adequate systematic antihypertensive therapy. The 3rd group included 18 patients with chronic obstructive pulmonary disease stage II, the average age was 50.32±0.99 (48.22-52.16) years (gender: 14 men and 4 women), the disease duration was 7.52±1.14. At the same time, 80% were active smokers, the pack-year index was 17.23±2.69, and 23.53% indicated a harmful professional factor (production). The state of the thiol-disulfide system was studied on the content of oxidized and reduced glutathione, SH-groups and the activity of enzymes - glutathione-S-transferase, glutathione reductase and glutathione peroxidase in serum. Results and discussion. Enzymatic activity of glutathione-S-transferase, glutathione reductase and glutathione peroxidase in the group of patients with hypertension was maximum, while it was significantly higher than the corresponding indicators of groups of patients with chronic obstructive pulmonary disease and especially with comorbidity. The ratio of reduced/ oxidized forms of glutathione demonstrates the greatest potential of the thiol-disulfide system in hypertension – 7.97±0.15 u. and low values for comorbidity – 3.81±0.34 u., and the percentage difference between the three groups was statistically significant in each case according to this ratio: arterial hypertension vs. chronic obstructive pulmonary disease – 23.57% (P<0.05), arterial hypertension vs arterial hypertension + chronic obstructive pulmonary disease – 109.19% (P<0.05), chronic obstructive pulmonary disease vs. arterial hypertension + chronic obstructive pulmonary disease – 69.29% (P<0.05). Conclusion. We found that comorbid pathology of chronic obstructive pulmonary disease and arterial hypertension leads to significant changes in the glutathione chain of the thiol-disulfide system due to a decrease in its reduced intermediates (the level of glutathione and reduced thiol groups decreases significantly), an increase in the level of oxidized glutathione and the total amount of oxidized thiols against a background of decreasing enzyme activity glutathione-S-transferase, glutathione reductase and glutathione peroxidase, more significantly than the presence of a single disease in the form of chronic obstructive pulmonary disease or hypertension.

Keywords: thiol-disulfide system, chronic obstructive pulmonary disease, arterial hypertension, glutathione, antioxidant system

Full text: PDF (Ukr) 231K

References
  1. Goodrich LE, Roy S, Alp EE, Zhao J, Hu MY, Lehnert N. Electronic structure and biologically relevant reactivity of low-spin {FeNO}8 porphyrin model complexes: new insight from a bis-picket fence porphyrin. Inorg Chem. 2013 Jul; 52(13): 7766-80. https://www.ncbi.nlm.nih.gov/pubmed/23746143. https://doi.org/10.1021/ic400977h
  2. Muravleva LYe. Okislitel'naya modifikatsiya belkov: problemy i perspektivy issledovaniya [Oxidative Modification of Proteins: Problems and Prospects of Research]. Fundamental'nyye issledovaniya. 2010; 1: 74-7. [Russian]
  3. Gorbacheva SV, Belenichev IF. Antioksidantnaya modulyatsiya neyroapoptoza v usloviyakh disbalansa tiol-disul'fidnoy sistemy i nakopleniya okislennykh promezhutochnykh soyedineniy in vitro [Antioxidant modulation of neuroapoptosis under conditions of imbalance of the thiol-disulfide system and the accumulation of oxidized intermediates in vitro]. Vísnik problem bíologíí̈ í meditsini. 2015; 3(1): 124-8. [Russian]
  4. Popov SS. Aktivnost' glutationovoy antioksidantnoy sistemy pri gipertireoze i pri deystvii melatonina [Activity of the glutathione antioxidant system in hyperthyroidism and under the action of melatonin]. Problemy endokrinologii. 2008; 3: 47-50. [Russian]
  5. Kulinskiy VI, Kolesnichenko LS. Sistema glutationa I. Sintez, transport glutationtransferazy, glutationperoksidazy [Glutathione system I. Synthesis, transport of glutathione transferase, glutathione peroxidase]. Biokhimiya. 2009; 55(3): 225-40. [Russian]
  6. Dave BN, Paradkar NM. Total superoxide dismutase, Cu/Zn superoxide dismutase and glutathione peroxidase in untreated hyperthyroidism and hypothyroidism. JK Science. 2009; 11(1): 6-10.
  7. Gorbacheva HA. Narusheniye tioldisul'fidnogo ravnovesiya u bol'nykh s ostrymi vospalitel'nymi zabolevaniyami organov dykhaniya [Violation of thiol-disulfide balance in patients with acute inflammatory diseases of the respiratory system]. Sbornik trudov desyatoy nauchno-prakticheskoy konferentsii «Aktual'nyye voprosy vnutrennikh bolezney». SPb; 2009. р. 66-7. [Russian]
  8. Ago Т, Sadoshima J. Thioredoxin 1 as a negative regulation of cardiac hypertrophy. Antioxid and Redox Signal. 2007; 9(8): 679-87. https://doi.org/10.1089/ars.2007.1529
  9. Funato Y, Miki Н. Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation. Antioxid and Redox Signal. 2007; 9(8): 1035-57. https://www.ncbi.nlm.nih.gov/pubmed/17567240. https://doi.org/10.1089/ars.2007.1550
  10. Mirza S, Clay RD, Koslow MA, Scanlon PD. COPD Guidelines: A Review of the 2018 GOLD Report. Mayo Clin Proc. 2018; 93(10): 1488-502. https://doi.org/10.1016/j.mayocp.2018.05.026
  11. Williams B, Mancia G, Spiering W, Agabiti Rosei E, Azizi M, Burnier M, et al. 2018 ESC/ESH Guidelines for the management of arterial hypertension. Eur Heart J. 2018; 39(33): 3021-104. https://www.ncbi.nlm.nih.gov/pubmed/30165516. https://doi.org/10.1093/eurheartj/ehy339
  12. Halliwell B. Free radical in Biology and Medicine. Oxpord: Clarendon Press; 1995. 345 p.
  13. Danilova LA. Spravochnik po laboratornym metodam issledovaniya [Handbook of laboratory research methods]. SPb: Piter; 2003. 736 p. [Russian]
  14. Moin VM. Prostoy i spetsificheskiy metod opredeleniya aktivnosti glutationperoksidazy v eritrotsitakh [A simple and specific method for determining the activity of glutathione peroxidase in erythrocytes] Lab delo. 1986; 12: 124-6. [Russian]
  15. Goldberg DM. Methods of Enzymatic Analysis. Weinheim: Verlag Chemie. 1983; 5 (3): 258-65.
  16. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov; 193(1): 265-75. https://www.ncbi.nlm.nih.gov/pubmed/14907713
  17. Xie J, Yang XY, Shi JD, Deng XQ, Long W. A new inflammation marker of chronic obstructive pulmonary disease. World J Emerg Med. 2010; 3: 190-5. https://www.ncbi.nlm.nih.gov/pubmed/25214966. https://www.ncbi.nlm.nih.gov/pmc/articles/4129679
  18. Mehta SL, Kumari S, Mendelev N, Li PA. Selenium preserves mitochondrial function, stimulates mitochondrial biogenesis, and reduces infarct volume after focal cerebral ischemia. BMC Neurosci. 2012 Jul; 9(13): 79. https://www.ncbi.nlm.nih.gov/pubmed/22776356. https://www.ncbi.nlm.nih.gov/pmc/articles/3411431. https://doi.org/10.1186/1471-2202-13-79
  19. Malli F, Papaioannou AI, Gourgoulianis KI. The role of leptin in the respiratory system: an overview. Respiratory research. 2010; 11(1): 152. https://www.ncbi.nlm.nih.gov/pubmed/21040518. https://www.ncbi.nlm.nih.gov/pmc/articles/2988727. https://doi.org/10.1186/1465-9921-11-152
  20. Ivanova YV. Vliyaniye razlichnykh skhem lecheniya na uroven' provospalitel'nogo tsitokina TNF-al'fa v indutsirovannoy mokrote pri obostrenii HOBL u lits, perenesshikh tuberkulez legkikh [Effect of various treatment regimens on the level of proinflammatory cytokine TNF-alpha in induced sputum during exacerbation of COPD in people who have had pulmonary tuberculosis]. Bukovinskiy meditsinskiy vestnik. 2013; 1(65): 38-41. [Russian]