Peculiarities of Action of Catecholamines and their Metabolites in the Regulation of Cardiomyocyte Enzymes
DOI:
https://doi.org/10.3889/oamjms.2022.8244Keywords:
Catecholamines, Adrenaline, Mitochondrial and cytosolic enzymes of cardiomyocytesAbstract
BACKGROUND: Myocardial ischemia is accompanied by a significant increase in adrenaline content in the heart. By its nature, sympathetic hyperactivation is accompanied by increased formation of products of enzymatic and nonenzymatic metabolism of adrenaline and its analogs, which can change the use of ATP by cells, change the activity of mitochondrial and cytosolic enzymes, contributing to disruption of bioenergetic adaptation, antioxidant defense system and levels of intercellular modulators such as AMP and adenosine.
AIM: The study objective was to explore the features of adrenaline and its analogs in the regulation of the activity of mitochondrial and cytoplasmic enzymes of cardiomyocytes.
METHODS: The experiment was carried out on 65 3-month-old male Wistar rats weighing 60–190 g. To study the effects of catecholamines and their metabolites in the regulation of mitochondrial and cytoplasmic enzymes activity of cardiomyocytes, experimental rats were put to death by intraperitoneal injection of 10% ketamine in an amount of 0.25 mg/100 g. Activity of mitochondrial succinate dehydrogenase, cytochrome c oxidase, mitochondrial DNP-activated ATPase, adenosine deaminase (AD), AMP deaminase (AMPD), glutathione reductase, and glutathione peroxidase were determined.
RESULTS: Dopamine has the greatest activating effect on cardiac mitochondrial ADH, adrenaline on CHO, and adrenochrome and adrenoxyl on ATPase. Isadrine and dopamine reduce cardiac AMPase activity. An activating effect on cardiac mitochondrial AMPD was found only in norepinephrine.
CONCLUSION: In cardiomyocytes, adrenaline, activates cytosolic enzymes of purine nucleotide metabolism AD and AMPD, as well as increases the level of lipid peroxidation (MDA and DC). This proves that adrenaline acting on adrenoreceptor mechanisms leads the body into a state of oxidative stress. Hormone-mediators of the sympatho-adrenal system adrenaline, dopamine, noradrenaline, isadrine, and catecholamine metabolites (adrenochrome and adrenoxyl), changes the activity of mitochondrial respiratory chain enzymes of cardiomyocytes, also regulate tissue respiration processes, putting mitochondria into the state of “loose” coupling of respiration and phosphorylation.
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Markowitz C. Response of explanted embryonic cardiac tissue to epinephrine and acetylcholine. Am J Physiol. 1931;97(2):271-5. https://doi.org/10.1152/ajplegacy.1931.97.2.271 DOI: https://doi.org/10.1152/ajplegacy.1931.97.2.271
Hsu FY. The effect of adrenaline and acetylcholine on the heart rate of the chick embryo. Chin J Physiol. 1933;7:243-52.
Ignarro LJ, Shideman FE. Appearance and concentrations of catecholamines and their biosynthesis in the embryonic and developing chick. J Pharmacol Exp Ther. 1968;159(1):38-48. PMid:5643949
Ebert SN, Thompson RP. Embryonic epinephrine synthesis in the rat heart before innervation: Association with pacemaking and conduction tissue development. Circ Res. 2001;88(1):117-24. https://doi.org/10.1161/01.res.88.1.117 PMid:11139483 DOI: https://doi.org/10.1161/01.RES.88.1.117
Ebert SN, Rong Q, Boe S, Thompson RP, Grinberg A, Pfeifer K. Targeted insertion of the Cre-recombinase gene at the phenylethanolamine n-methyltransferase locus: A new model for studying the developmental distribution of adrenergic cells. Dev Dyn. 2004;231(4):849-58. https://doi.org/10.1002/dvdy.20188 PMid:15517585 DOI: https://doi.org/10.1002/dvdy.20188
Huang MH, Friend DS, Sunday ME, Singh K, Haley K, Austen KF, et al. An intrinsic adrenergic system in mammalian heart. J Clin Invest. 1996;98(6):1298-303. https://doi.org/10.1172/JCI118916 PMid:8823294 DOI: https://doi.org/10.1172/JCI118916
Tapbergenov SO, Tapbergenov TS. Adreno-Thyroid System. Cell Bioenergy and Stress Adaptation Mechanisms, Semipalatinsk; 1998.
Tapbergenov S, Tapbergenov T. Stress, Adaptation and Adrenal- Thyroid Disfunction Syndrome. Saarbrucken, Germany: Lap Lambert Academic Publishing; 2014. p. 190.
Tapbergenov SO, Tapbergenov TS, Hahn N, Sovetov BS. Functional and metabolic effects of the sympathoadrenal system and stress. Moscow: The Academy of Natural Sciences of Drexel University; 2019. p. 138.
Tapbergenov SO, Tapbergenova SM. Diagnosticheskoe znachenie opredeleniia aktivnosti adenilatdezaminazy syvorotki krovi [Diagnostic value of determining adenylate deaminase activity in the blood]. Lab Delo. 1984;2:104-7.
Vlasova SN, Shabunina EI, Pereslegina IA. Aktivnost’ glutationzavisimykh fermentov éritrotsitov pri khronicheskikh zabolevaniiakh pecheni u deteĭ [The activity of the glutathione-dependent enzymes of erythrocytes in chronic liver diseases in children]. Lab Delo. 1990;8:19-22.
Koroliuk MA, Ivanova LI, Maĭorova IG, Tokarev VE. Labor, Case; 1988.
Mihara M, Uchiyama M. Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Anal Biochem. 1978;86(1):271-8. https://doi.org/10.1016/0003-2697(78)90342-1 PMid:655387 DOI: https://doi.org/10.1016/0003-2697(78)90342-1
Gavrilov VB, Gavrilova AR, Khmara NF. Izmerenie dienovykh kon iugatov v plazme krovi po UF-pogloshcheniiu geptanovykh i izopropanol’nykh ékstraktov [Measurement of diene conjugates in blood plasma using the UV absorption of heptane and isopropanol extracts]. Lab Delo. 1988;2:60-4. PMid:2452294.
Tapbergenov SO, Tapbergenov TS. Biomedicinskaja Himija; 2005. p. 199-205.
Fields LA, Koschinski A, Zaccolo M. Sustained exposure to catecholamines affects cAMP/PKA compartmentalised signalling in adult rat ventricular myocytes. Cell Signal. 2016;28(7):725-32. https://doi.org/10.1016/j.cellsig.2015.10.003 PMid:26475678 DOI: https://doi.org/10.1016/j.cellsig.2015.10.003
Anastacio MM, Kanter EM, Makepeace C, Keith AD, Zhang H, Schuessler RB, et al. Cardioprotective mechanism of diazoxide involves the inhibition of succinate dehydrogenase. Ann Thorac Surg. 2013;95(6):2042-50. https://doi.org/10.1016/j.athoracsur.2013.03.035 PMid:23642436 DOI: https://doi.org/10.1016/j.athoracsur.2013.03.035
Ogunbona OB, Baile MG, Claypool SM. Cardiomyopathy-associated mutation in the ADP/ATP carrier reveals translation-dependent regulation of cytochrome c oxidase activity. Mol Biol Cell. 2018;29(12):1449-64. https://doi.org/10.1091/mbc.E17-12-0700 PMid:29688796 DOI: https://doi.org/10.1091/mbc.E17-12-0700
Zarco-Zavala M, Watanabe R, McMillan DG, et al. The 3×120° rotary mechanism of Paracoccus denitrificans F1-ATPase is different from that of the bacterial and mitochondrial F1-ATPases. Proc Natl Acad Sci USA. 2020;117(47):29647-57. https://doi.org/10.1073/pnas.2003163117 PMid:33168750 DOI: https://doi.org/10.1073/pnas.2003163117
Mailloux RJ, Xuan JY, McBride S, Maharsy W, Thorn S, Holterman CE, et al. Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions. J Biol Chem. 2014;289(21):14812-28. https://doi.org/10.1074/jbc.M114.550574 PMid:24727547 DOI: https://doi.org/10.1074/jbc.M114.550574
Boengler K, Kosiol M, Mayr M, Schulz R, Rohrbach S. Mitochondria and ageing: Role in heart, skeletal muscle and adipose tissue. J Cachexia Sarcopenia Muscle. 2017;8(3):349-69. https://doi.org/10.1002/jcsm.12178 PMid:28432755 DOI: https://doi.org/10.1002/jcsm.12178
Kalsi KK, Yuen AH, Johnson PH, Birks EJ, Yacoub MH, Smolenski RT. AMPD1 C34T mutation selectively affects AMP-deaminase activity in the human heart. Nucleosides Nucleotides Nucleic Acids. 2005;24(4):287-8. https://doi.org/10.1081/NCN-59721 PMid:16021918 DOI: https://doi.org/10.1081/NCN-200059721
Santos A, Pité H, Chaves-Loureiro C, Rocha SM, Taborda-Barata L. Metabolic phenotypes in asthmatic adults: Relationship with inflammatory and clinical phenotypes and prognostic implications. Metabolites. 2021;11(8):534. https://doi.org/10.3390/metabo11080534 PMid:34436475 DOI: https://doi.org/10.3390/metabo11080534
Wikström M, Springett R. Thermodynamic efficiency, reversibility, and degree of coupling in energy conservation by the mitochondrial respiratory chain. Commun Biol. 2020;3(1):451. https://doi.org/10.1038/s42003-020-01192-w PMid:32811895 DOI: https://doi.org/10.1038/s42003-020-01192-w
Tapbergenov SO, Sovetov BS, Tapbergenov AT. Features of influence adenosine, AMP and hyperadrenalinemiya on the immune status, metabolic enzymes of purine nucleotides and the antioxidant defense system. Biomed Khim. 2016;62(6):645-9. https://doi.org/10.18097/PBMC20166206645 PMid:28026807 DOI: https://doi.org/10.18097/PBMC20166206645
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Copyright (c) 2022 Salavat Tapbergenov, Bakytbek Sovetov, Ynkar Kairkhanova, Zhanargul Smailova (Author)
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