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Катестатин – перспективный биологический маркер при сердечной недостаточности
Катестатин – перспективный биологический маркер при сердечной недостаточности
Алиева А.М., Теплова Н.В., Резник Е.В., Эттингер О.А., Фараджов Р.А., Хачирова Э.А., Ковтюх И.В., Котикова И.А., Сысоева Д.А., Бигушев И.Р., Никитин И.Г. Катестатин – перспективный биологический маркер при сердечной недостаточности. Consilium Medicum. 2022;24(10):726–731.
DOI: 10.26442/20751753.2022.10.201873
© ООО «КОНСИЛИУМ МЕДИКУМ», 2022 г.
DOI: 10.26442/20751753.2022.10.201873
© ООО «КОНСИЛИУМ МЕДИКУМ», 2022 г.
________________________________________________
Материалы доступны только для специалистов сферы здравоохранения. Авторизуйтесь или зарегистрируйтесь.
Аннотация
Эпидемия сердечной недостаточности (СН) – одна из проблем, с которыми мировая система здравоохранения сталкивается уже не первое десятилетие. СН является многокомпонентным клиническим синдромом, обусловленным нарушением функции сердца и его патологическим ремоделированием. Кроме широко известных натрийуретических пептидов в настоящее время идентифицирован ряд сердечно-сосудистых биологических маркеров, которые дают клиницистам возможность получить дополнительные возможности в диагностировании, классификации, прогнозировании, а также мониторинге эффективности лечения пациентов с СН. С позиции установления симпатической нагрузки у пациентов с СН представляется весьма перспективной оценка концентраций катестатина. Представленные данные нашего литературного обзора свидетельствуют в пользу того, что катестатин, вероятно, является надежным биологическим маркером активности симпатического отдела вегетативной нервной системы, а его повышенные концентрации у больных с СН отражают тяжесть патологического процесса. Однако, несмотря на достоверные результаты исследований, клиническая значимость оценки значений данного маркера как отдельно, так и в рамках многомаркерной модели требует дальнейшего изучения в более крупных проспективных клинических исследованиях.
Ключевые слова: сердечная недостаточность, симпатическая нервная система, катестатин, натрийуретические пептиды, биомаркер
Keywords: heart failure, sympathetic nervous system, catestatin, natriuretic peptides, biomarker
Ключевые слова: сердечная недостаточность, симпатическая нервная система, катестатин, натрийуретические пептиды, биомаркер
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Keywords: heart failure, sympathetic nervous system, catestatin, natriuretic peptides, biomarker
Полный текст
Список литературы
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2. Mohananey D, Mewhort H, Shekhar S, et al. Heart Failure Trial Update-Analysis of Recent Data. J Cardiothorac Vasc Anesth. 2021;35(9):2792-800. DOI:10.1053/j.jvca.2020.09.085
3. Braunwald E. Heart failure. JACC Heart Fail. US National Institutes of Health. 2013;1(1):1-20. DOI:10.1016/j.jchf.2012.10.002
4. Fomin IV. Chronic heart failure in Russian Federation: what do we know and what to do. Russian Journal of Cardiology. 2016;8:7-13 (in Russian).
DOI:10.15829/1560-4071-2016-8-7-13
5. Minatoguchi S. Heart failure and its treatment from the perspective of sympathetic nerve activity. J Cardiol. 2022;79(6):691-7. DOI:10.1016/j.jjcc.2021.11.016
6. Li L, Hu Z, Xiong Y, Yao Y. Device-Based Sympathetic Nerve Regulation for Cardiovascular Diseases. Front Cardiovasc Med. 2021;8:803984. DOI:10.3389/fcvm.2021.803984
7. Swedberg K, Viquerat C, Rouleau JL, et al. Comparison of myocardial catecholamine balance in chronic congestive heart failure and in angina pectoris without failure. Am J Cardiol. 1984;54(7):783‑6. DOI:10.1016/S0002-9149(84)80208-8
8. Viquerat CE, Daly P, Swedberg K, et al. Endogenous catecholamine levels in chronic heart failure. Relation to the severity of hemodynamic abnormalities. Am J Med. 1985;78(3):455-60. DOI:10.1016/0002-9343(85)90338-9
9. Kaye DM, Lambert GW, Lefkovits J, et al. Neurochemical evidence of cardiac sympathetic activation and increased central nervous system norepinephrine turnover in severe congestive heart failure. J Am Coll Cardiol. 1994;23(3):570-8. DOI:10.1016/0735-1097(94)90738-2.
10. Aggarwal A, Esler MD, Lambert GW, et al. Norepinephrine turnover is increased in suprabulbar subcortical brain regions and is related to whole-body sympathetic activity in human heart failure. Circulation. 2002;105(9):1031-3. DOI:10.1161/hc0902.105724
11. Zucker IH, Schultz HD, Patel KP, et al. Regulation of central angiotensin type 1 receptors and sympathetic outflow in heart failure. Am J Physiol Hear Circ Physiol. 2009;297(5):H1557-66. DOI:10.1152/ajpheart.00073.2009
12. Chidsey CA, Braunwald E, Morrow AG. Catecholamine excretion and cardiac stores of norepinephrine in congestive heart failure. Am J Med. 1965;39(3):442-51.
DOI:10.1016/0002-9343(65)90211-1
13. Katsuumi G, Shimizu I, Yoshida Y, et al. Catecholamine-induced senescence of endothelial cells and bone marrow cells promotes cardiac dysfunction in mice. Int Heart J. 2018;59(4):837-44. DOI:10.1536/ihj.17-313
14. Santos JRU, Brofferio A, Viana B, Pacak K. Catecholamine-Induced Cardiomyopathy in Pheochromocytoma: How to Manage a Rare Complication in a Rare Disease? Horm Metab Res. 2019;51(7):458-69. DOI:10.1055/a-0669-9556
15. Aliyeva AM, Reznik EV, Hasanova ET, et al. Clinical value of blood biomarkers in patients with chronic heart failure. The Russian Archives of Internal Medicine. 2018;8(5):333-45 (in Russian). DOI:10.20514/2226-6704-2018-8-5-333-345
16. Gasparyan AZ, Shlevkov NB, Skvortsov AA. Possibilities of modern biomarkers for assessing the risk of developing ventricular tachyarrhythmias and sudden cardiac death in patients with chronic heart failure. Kardiologiia. 2020;60(4):101-8 (in Russian). DOI:10.18087/cardio.2020.4.n487
17. Alieva AM, Pinchuk TV, Almazova II, et al. Сlinical value of blood biomarker ST2 in patients with chronic heart failure. Consilium Medicum. 2021;23(6):522-6 (in Russian). DOI:10.26442/20751753.2021.6.200606
18. Alieva AM, Almazova II, Pinchuk TV, et al. Fractalkin and cardiovascular disease. Consilium Medicum. 2020;22(5):83-6 (in Russian).
DOI:10.26442/20751753.2020.5.200186
19. Larina VN, Lunev VI. The Value of Biomarkers in the Diagnosis and Prognosis of Heart Failure in Older Age. The Russian Archives of Internal Medicine. 2021;11(2):98-110 (in Russian). DOI:10.20514/2226-6704-2021-11-2-98-110
20. Mahata SK, O’Connor DT, Mahata M, et al. Novel autocrine feedback control of catecholamine release: A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest. 1997;100(6):1623-33. DOI:10.1172/JCI119686
21. Mahata SK, Kiranmayi M, Mahapatra NR. Catestatin: A Master Regulator of Cardiovascular Functions. Curr Med Chem. 2018;25:1352-74. DOI:10.2174/0929867324666170425100416
22. Biswas N, Rodriguez-Flores JL, Courel M, et al. Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides. Endocrinology. 2009;150:3547-57. DOI:10.1210/en.2008-1613
23. Bianco M, Gasparri AM, Colombo B, et al. Chromogranin A Is Preferentially Cleaved into Proangiogenic Peptides in the Bone Marrow of Multiple Myeloma Patients. Cancer Res. 2016;76:1781-91. DOI:10.1158/0008-5472.CAN-15-1637
24. Pasqua T, Angelone T, Spena A, Cerra MC. Biological Roles of the Eclectic Chromogranin-A-derived Peptide Catestatin. Curr Med Chem. 2017;24(31):3356-72. DOI:10.2174/0929867324666170616104759
25. Kraszewski S, Drabik D, Langner M, et al. A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments. Phys Chem Chem Phys. 2015;17(26):17454-60. DOI:10.1039/c4cp02491e
26. Sahu BS, Mohan J, Sahu G, et al. Molecular interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptor. J Cell Sci. 2012;125(Pt. 9):2323-37. DOI:10.1242/jcs.103176. Erratum in: J Cell Sci. 2012;125(Pt. 11):2787. Obbineni, Jagan M [corrected to Mohan, Jagan].
27. Taupenot L, Mahata SK, Mahata M, et al. Interaction of the catecholamine releaseinhibitory peptide catestatin (human chromogranin A (352372)) with the chromaffin cell surface and Torpedo electroplax: Implications for nicotinic cholinergic antagonism. Regul Pept. 2000;95:9717. DOI:10.1016/S0167-0115(00)00135-X
28. Bozic J, Kumric M, Ticinovic Kurir T, et al. Catestatin as a Biomarker of Cardiovascular Diseases: A Clinical Perspective. Biomedicines. 2021;9(12):1757. DOI:10.3390/biomedicines9121757
29. Angelone T, Quintieri AM, Brar BK, et al. The antihypertensive chromogranin a peptide catestatin acts as a novel endocrine/paracrine modulator of cardiac inotropism and lusitropism. Endocrinology. 2008;149:4780-93. DOI:10.1210/en.2008-0318
30. Zhang YM, Zhang ZY, Wang RX. Protective Mechanisms of Quercetin against Myocardial Ischemia Reperfusion Injury. Front Physiol. 2020;11:956. DOI:10.3389/fphys.2020.00956
31. Mazza R, Gattuso A, Mannarino C, et al. Catestatin (chromogranin A344364) is a novel cardiosuppressive agent: Inhibition of isoproterenol and endothelin signaling in the frog heart. Am J Physiol Heart Circ Physiol. 2008;295:H113-22. DOI:10.1152/ajpheart.00172.2008
32. Gaede AH, Pilowsky PM. Catestatin in rat RVLM is sympathoexcitatory, increases barosensitivity, and attenuates chemosensitivity and the somatosympathetic reflex. Am J Physiol Regul Integr Comp Physiol. 2010;299:R1538-545. DOI:10.1152/ajpregu.00335.2010
33. Gaede AH, Pilowsky PM. Catestatin, a chromogranin A-derived peptide, is sympathoinhibitory and attenuates sympathetic barosensitivity and the chemoreflex in rat CVLM. Am J Physiol Regul Integr Comp Physiol. 2012;302:R365-72. DOI:10.1152/ajpregu.00409.2011
34. Avolio E, Mahata SK, Mantuano E, et al. Antihypertensive and neuroprotective effects of catestatin in spontaneously hypertensive rats: Interaction with GABAergic transmission in amygdala and brainstem. Neuroscience. 2014;270:48-57. DOI:10.1016/j.neuroscience.2014.04.001
35. Gayen JR, Gu Y, OConnor DT, Mahata SK. Global disturbances in autonomic function yield cardiovascular instability and hypertension in the chromogranin a null mouse. Endocrinology. 2009;150:5027-35. DOI:10.1210/en.2009-0429
36. Dev NB, Gayen JR, OConnor DT, Mahata SK. Chromogranin A and the autonomic system: Decomposition of heart rate variability by time and frequency domains, along with non-linear characteristics during chromogranin A ablation, with rescue by its catestatin. Endocrinology. 2010;151:2760-68. DOI:10.1210/en.2009-1110
37. Krüger PG, Mahata SK, Helle KB. Catestatin (CgA344364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides. Regul Pept. 2003;114:29-35. DOI:10.1016/S0167-0115(03)00069-7
38. Fung MM, Salem RM, Mehtani P, et al. Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo. Clin Exp Hypertens. 2010;32:278-87. DOI:10.3109/10641960903265246
39. Zhang D, Shooshtarizadeh P, Laventie BJ, et al. Two chromogranin a-derived peptides induce calcium entry in human neutrophils by calmodulin-regulated calcium independent phospholipase A2. PLoS ONE. 2009;4:e4501. DOI:10.1371/journal.pone.0004501
40. Frodermann V, Nahrendorf M. Neutrophil-macrophage cross-talk in acute myocardial infarction. Eur Heart J. 2017;38:198-200. DOI:10.1093/eurheartj/ehw085
41. Bassino E, Fornero S, Gallo MP, et al. Catestatin exerts direct protective effects on rat cardiomyocytes undergoing ischemia/reperfusion by stimulating PI3K-Akt-GSK3β pathway and preserving mitochondrial membrane potential. PLoS ONE. 2015;10:e0119790. DOI:10.1371/journal.pone.0119790
42. Chu SY, Peng F, Wang J, et al. Catestatin in defense of oxidative-stress-induced apoptosis: A novel mechanism by activating the beta2 adrenergic receptor and PKB/Akt pathway in ischemic-reperfused myocardium. Peptides. 2020;123:170200. DOI:10.1016/j.peptides.2019.170200
43. Zivkovic PM, Matetic A, Tadin Hadjina I, et al. Serum Catestatin Levels and Arterial Stiffness Parameters Are Increased in Patients with Inflammatory Bowel Disease. J Clin Med. 2020;9:628. DOI:10.3390/jcm9030628
44. Penna C, Alloatti G, Gallo MP, et al. Catestatin improves post-ischemic left ventricular function and decreases ischemia/reperfusion injury in heart. Cell Mol Neurobiol. 2010;30:1171-9. DOI:10.1007/s10571-010-9598-5
45. Kumrić M, Tičinović Kurir T, Borovac JA, Božić J. The Role of Natural Killer (NK) Cells in Acute Coronary Syndrome: A Comprehensive Review. Biomolecules. 2020;10:1514. DOI:10.3390/biom10111514
46. Liao F, Zheng Y, Cai J, et al. Catestatin attenuates endoplasmic reticulum induced cell apoptosis by activation type 2 muscarinic acetylcholine receptor in cardiac ischemia/reperfusion. Sci Rep. 2015;5:16590. DOI:10.1038/srep16590
47. Chu SY, Peng F, Wang J, et al. Catestatin in defense of oxidative-stress-induced apoptosis: A novel mechanism by activating the beta2 adrenergic receptor and PKB/Akt pathway in ischemic-reperfused myocardium. Peptides. 2020;123:170200. DOI:10.1016/j.peptides.2019.170200
48. Brar BK, Helgeland E, Mahata SK, et al. Human catestatin peptides differentially regulate infarct size in the ischemic-reperfused rat heart. Regul Pept. 2010;165:63-70. DOI:10.1016/j.regpep.2010.07.153
49. Zhu D, Wang F, Yu H, et al. Catestatin is useful in detecting patients with stage B heart failure. Biomarkers. 2011;16(8):691-7. DOI:10.3109/1354750X.2011.629058
50. Liu L, Ding W, Li R, et al. Plasma levels and diagnostic value of catestatin in patients with heart failure. Peptides. 2013;46:20-5. DOI:10.1016/j.peptides.2013.05.003
51. Borovac JA, Glavas D, Susilovic Grabovac Z, et al. Catestatin in Acutely Decompensated Heart Failure Patients: Insights from the CATSTAT-HF Study. J Clin Med. 2019;8(8):1132. DOI:10.3390/jcm8081132
52. Borovac JA, Glavas D, Susilovic Grabovac Z, et al. Circulating sST2 and catestatin levels in patients with acute worsening of heart failure: a report from the CATSTAT-HF study. ESC Heart Fail. 2020;7(5):2818-28. DOI:10.1002/ehf2.12882
53. Peng F, Chu S, Ding W, et al. The predictive value of plasma catestatin for all-cause and cardiac deaths in chronic heart failure patients. Peptides. 2016;86:112-7. DOI:10.1016/j.peptides.2016.10.007
54. Wołowiec Ł, Rogowicz D, Banach J, et al. Catestatin as a New Prognostic Marker in Stable Patients with Heart Failure with Reduced Ejection Fraction in Two-Year Follow-Up. Dis Markers. 2020;2020:8847211. DOI:10.1155/2020/8847211
55. Ottesen AH, Carlson CR, Louch WE, et al. Glycosylated Chromogranin A in Heart Failure: Implications for Processing and Cardiomyocyte Calcium Homeostasis. Circ Heart Fail. 2017;10(2):e003675. DOI:10.1161/CIRCHEARTFAILURE.116.003675
56. Watanabe T. The Emerging Roles of Chromogranins and Derived Polypeptides in Atherosclerosis, Diabetes, and Coronary Heart Disease. Int J Mol Sci. 2021;22(11):6118. DOI:10.3390/ijms22116118
57. Алиева А.М., Теплова Н.В., Батов М.А., и др. Пентраксин-3 – перспективный биологический маркер при сердечной недостаточности: литературный обзор. Consilium Medicum. 2022;24(1):53-9. DOI:10.26442/20751753.2022.1.201382
58. Алиева А.М., Пинчук Т.В., Воронкова К.В., и др. Неоптерин – биомаркер хронической сердечной недостаточности (обзор современной литературы). Consilium Medicum. 2021;23(10):756-9. DOI:10.26442/20751753.2021.10.201113
59. Алиева А.М., Алмазова И.И., Пинчук Т.В., и др. Значение копептина в диагностике и прогнозе течения сердечно-сосудистых заболеваний. Клиническая медицина. 2020;98(3):203-9. DOI:10.30629/0023-2149-2020-98-3-203-209
60. Zalewska E, Kmieć P, Sworczak K. Role of Catestatin in the Cardiovascular System and Metabolic Disorders. Front Cardiovasc Med. 2022;9:909480. DOI:10.3389/fcvm.2022.909480
61. Мещеряков Ю.В., Губарева И.В., Губарева Е.Ю., Алексеева А.Ю. Роль катестатина в развитии и декомпенсации сердечной недостаточности: обзор литературы. Российский кардиологический журнал. 2021;26(S3):4492. DOI:10.15829/1560-4071-2021-4492
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16. Гаспарян А.Ж., Шлевков Н.Б., Скворцов А.А. Возможности современных биомаркеров для оценки риска развития желудочковых тахиаритмий и внезапной сердечной смерти у больных хронической сердечной недостаточностью. Кардиология. 2020;60(4):101-8 [Gasparyan AZ, Shlevkov NB, Skvortsov AA. Possibilities of modern biomarkers for assessing the risk of developing ventricular tachyarrhythmias and sudden cardiac death in patients with chronic heart failure]. Kardiologiia. 2020;60(4):101-8 (in Russian)]. DOI:10.18087/cardio.2020.4.n487
17. Алиева А.М., Пинчук Т.В., Алмазова И.И., и др. Клиническое значение определения биомаркера крови ST2 у больных с хронической сердечной недостаточностью. Consilium Medicum. 2021;23(6):522-6 [Alieva AM, Pinchuk TV, Almazova II, et al. Сlinical value of blood biomarker ST2 in patients with chronic heart failure. Consilium Medicum. 2021;23(6):522-6 (in Russian)]. DOI:10.26442/20751753.2021.6.200606
18. Алиева А.М., Алмазова И.И., Пинчук Т.В., и др. Фракталкин и сердечно-сосудистые заболевания. Consilium Medicum. 2020;22(5):83-6 [Alieva AM, Almazova II, Pinchuk TV, et al. Fractalkin and cardiovascular disease. Consilium Medicum. 2020;22(5):83-6 (in Russian)]. DOI:10.26442/20751753.2020.5.200186
19. Ларина В.Н., Лунев В.И. Значение биомаркеров в диагностике и прогнозировании сердечной недостаточности в старшем возрасте. Архивъ внутренней медицины. 2021;11(2):98‑110 [Larina VN, Lunev VI. The Value of Biomarkers in the Diagnosis and Prognosis of Heart Failure in Older Age. The Russian Archives of Internal Medicine. 2021;11(2):98-110 (in Russian)]. DOI:10.20514/2226-6704-2021-11-2-98-110
20. Mahata SK, O’Connor DT, Mahata M, et al. Novel autocrine feedback control of catecholamine release: A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest. 1997;100(6):1623-33. DOI:10.1172/JCI119686
21. Mahata SK, Kiranmayi M, Mahapatra NR. Catestatin: A Master Regulator of Cardiovascular Functions. Curr Med Chem. 2018;25:1352-74. DOI:10.2174/0929867324666170425100416
22. Biswas N, Rodriguez-Flores JL, Courel M, et al. Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides. Endocrinology. 2009;150:3547-57. DOI:10.1210/en.2008-1613
23. Bianco M, Gasparri AM, Colombo B, et al. Chromogranin A Is Preferentially Cleaved into Proangiogenic Peptides in the Bone Marrow of Multiple Myeloma Patients. Cancer Res. 2016;76:1781-91. DOI:10.1158/0008-5472.CAN-15-1637
24. Pasqua T, Angelone T, Spena A, Cerra MC. Biological Roles of the Eclectic Chromogranin-A-derived Peptide Catestatin. Curr Med Chem. 2017;24(31):3356-72. DOI:10.2174/0929867324666170616104759
25. Kraszewski S, Drabik D, Langner M, et al. A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments. Phys Chem Chem Phys. 2015;17(26):17454-60. DOI:10.1039/c4cp02491e
26. Sahu BS, Mohan J, Sahu G, et al. Molecular interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptor. J Cell Sci. 2012;125(Pt. 9):2323-37. DOI:10.1242/jcs.103176. Erratum in: J Cell Sci. 2012;125(Pt. 11):2787. Obbineni, Jagan M [corrected to Mohan, Jagan].
27. Taupenot L, Mahata SK, Mahata M, et al. Interaction of the catecholamine releaseinhibitory peptide catestatin (human chromogranin A (352372)) with the chromaffin cell surface and Torpedo electroplax: Implications for nicotinic cholinergic antagonism. Regul Pept. 2000;95:9717. DOI:10.1016/S0167-0115(00)00135-X
28. Bozic J, Kumric M, Ticinovic Kurir T, et al. Catestatin as a Biomarker of Cardiovascular Diseases: A Clinical Perspective. Biomedicines. 2021;9(12):1757. DOI:10.3390/biomedicines9121757
29. Angelone T, Quintieri AM, Brar BK, et al. The antihypertensive chromogranin a peptide catestatin acts as a novel endocrine/paracrine modulator of cardiac inotropism and lusitropism. Endocrinology. 2008;149:4780-93. DOI:10.1210/en.2008-0318
30. Zhang YM, Zhang ZY, Wang RX. Protective Mechanisms of Quercetin against Myocardial Ischemia Reperfusion Injury. Front Physiol. 2020;11:956. DOI:10.3389/fphys.2020.00956
31. Mazza R, Gattuso A, Mannarino C, et al. Catestatin (chromogranin A344364) is a novel cardiosuppressive agent: Inhibition of isoproterenol and endothelin signaling in the frog heart. Am J Physiol Heart Circ Physiol. 2008;295:H113-22. DOI:10.1152/ajpheart.00172.2008
32. Gaede AH, Pilowsky PM. Catestatin in rat RVLM is sympathoexcitatory, increases barosensitivity, and attenuates chemosensitivity and the somatosympathetic reflex. Am J Physiol Regul Integr Comp Physiol. 2010;299:R1538-545. DOI:10.1152/ajpregu.00335.2010
33. Gaede AH, Pilowsky PM. Catestatin, a chromogranin A-derived peptide, is sympathoinhibitory and attenuates sympathetic barosensitivity and the chemoreflex in rat CVLM. Am J Physiol Regul Integr Comp Physiol. 2012;302:R365-72. DOI:10.1152/ajpregu.00409.2011
34. Avolio E, Mahata SK, Mantuano E, et al. Antihypertensive and neuroprotective effects of catestatin in spontaneously hypertensive rats: Interaction with GABAergic transmission in amygdala and brainstem. Neuroscience. 2014;270:48-57. DOI:10.1016/j.neuroscience.2014.04.001
35. Gayen JR, Gu Y, OConnor DT, Mahata SK. Global disturbances in autonomic function yield cardiovascular instability and hypertension in the chromogranin a null mouse. Endocrinology. 2009;150:5027-35. DOI:10.1210/en.2009-0429
36. Dev NB, Gayen JR, OConnor DT, Mahata SK. Chromogranin A and the autonomic system: Decomposition of heart rate variability by time and frequency domains, along with non-linear characteristics during chromogranin A ablation, with rescue by its catestatin. Endocrinology. 2010;151:2760-68. DOI:10.1210/en.2009-1110
37. Krüger PG, Mahata SK, Helle KB. Catestatin (CgA344364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides. Regul Pept. 2003;114:29-35. DOI:10.1016/S0167-0115(03)00069-7
38. Fung MM, Salem RM, Mehtani P, et al. Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo. Clin Exp Hypertens. 2010;32:278-87. DOI:10.3109/10641960903265246
39. Zhang D, Shooshtarizadeh P, Laventie BJ, et al. Two chromogranin a-derived peptides induce calcium entry in human neutrophils by calmodulin-regulated calcium independent phospholipase A2. PLoS ONE. 2009;4:e4501. DOI:10.1371/journal.pone.0004501
40. Frodermann V, Nahrendorf M. Neutrophil-macrophage cross-talk in acute myocardial infarction. Eur Heart J. 2017;38:198-200. DOI:10.1093/eurheartj/ehw085
41. Bassino E, Fornero S, Gallo MP, et al. Catestatin exerts direct protective effects on rat cardiomyocytes undergoing ischemia/reperfusion by stimulating PI3K-Akt-GSK3β pathway and preserving mitochondrial membrane potential. PLoS ONE. 2015;10:e0119790. DOI:10.1371/journal.pone.0119790
42. Chu SY, Peng F, Wang J, et al. Catestatin in defense of oxidative-stress-induced apoptosis: A novel mechanism by activating the beta2 adrenergic receptor and PKB/Akt pathway in ischemic-reperfused myocardium. Peptides. 2020;123:170200. DOI:10.1016/j.peptides.2019.170200
43. Zivkovic PM, Matetic A, Tadin Hadjina I, et al. Serum Catestatin Levels and Arterial Stiffness Parameters Are Increased in Patients with Inflammatory Bowel Disease. J Clin Med. 2020;9:628. DOI:10.3390/jcm9030628
44. Penna C, Alloatti G, Gallo MP, et al. Catestatin improves post-ischemic left ventricular function and decreases ischemia/reperfusion injury in heart. Cell Mol Neurobiol. 2010;30:1171-9. DOI:10.1007/s10571-010-9598-5
45. Kumrić M, Tičinović Kurir T, Borovac JA, Božić J. The Role of Natural Killer (NK) Cells in Acute Coronary Syndrome: A Comprehensive Review. Biomolecules. 2020;10:1514. DOI:10.3390/biom10111514
46. Liao F, Zheng Y, Cai J, et al. Catestatin attenuates endoplasmic reticulum induced cell apoptosis by activation type 2 muscarinic acetylcholine receptor in cardiac ischemia/reperfusion. Sci Rep. 2015;5:16590. DOI:10.1038/srep16590
47. Chu SY, Peng F, Wang J, et al. Catestatin in defense of oxidative-stress-induced apoptosis: A novel mechanism by activating the beta2 adrenergic receptor and PKB/Akt pathway in ischemic-reperfused myocardium. Peptides. 2020;123:170200. DOI:10.1016/j.peptides.2019.170200
48. Brar BK, Helgeland E, Mahata SK, et al. Human catestatin peptides differentially regulate infarct size in the ischemic-reperfused rat heart. Regul Pept. 2010;165:63-70. DOI:10.1016/j.regpep.2010.07.153
49. Zhu D, Wang F, Yu H, et al. Catestatin is useful in detecting patients with stage B heart failure. Biomarkers. 2011;16(8):691-7. DOI:10.3109/1354750X.2011.629058
50. Liu L, Ding W, Li R, et al. Plasma levels and diagnostic value of catestatin in patients with heart failure. Peptides. 2013;46:20-5. DOI:10.1016/j.peptides.2013.05.003
51. Borovac JA, Glavas D, Susilovic Grabovac Z, et al. Catestatin in Acutely Decompensated Heart Failure Patients: Insights from the CATSTAT-HF Study. J Clin Med. 2019;8(8):1132. DOI:10.3390/jcm8081132
52. Borovac JA, Glavas D, Susilovic Grabovac Z, et al. Circulating sST2 and catestatin levels in patients with acute worsening of heart failure: a report from the CATSTAT-HF study. ESC Heart Fail. 2020;7(5):2818-28. DOI:10.1002/ehf2.12882
53. Peng F, Chu S, Ding W, et al. The predictive value of plasma catestatin for all-cause and cardiac deaths in chronic heart failure patients. Peptides. 2016;86:112-7. DOI:10.1016/j.peptides.2016.10.007
54. Wołowiec Ł, Rogowicz D, Banach J, et al. Catestatin as a New Prognostic Marker in Stable Patients with Heart Failure with Reduced Ejection Fraction in Two-Year Follow-Up. Dis Markers. 2020;2020:8847211. DOI:10.1155/2020/8847211
55. Ottesen AH, Carlson CR, Louch WE, et al. Glycosylated Chromogranin A in Heart Failure: Implications for Processing and Cardiomyocyte Calcium Homeostasis. Circ Heart Fail. 2017;10(2):e003675. DOI:10.1161/CIRCHEARTFAILURE.116.003675
56. Watanabe T. The Emerging Roles of Chromogranins and Derived Polypeptides in Atherosclerosis, Diabetes, and Coronary Heart Disease. Int J Mol Sci. 2021;22(11):6118. DOI:10.3390/ijms22116118
57. Алиева А.М., Теплова Н.В., Батов М.А., и др. Пентраксин-3 – перспективный биологический маркер при сердечной недостаточности: литературный обзор. Consilium Medicum. 2022;24(1):53-9. DOI:10.26442/20751753.2022.1.201382
58. Алиева А.М., Пинчук Т.В., Воронкова К.В., и др. Неоптерин – биомаркер хронической сердечной недостаточности (обзор современной литературы). Consilium Medicum. 2021;23(10):756-9. DOI:10.26442/20751753.2021.10.201113
59. Алиева А.М., Алмазова И.И., Пинчук Т.В., и др. Значение копептина в диагностике и прогнозе течения сердечно-сосудистых заболеваний. Клиническая медицина. 2020;98(3):203-9. DOI:10.30629/0023-2149-2020-98-3-203-209
60. Zalewska E, Kmieć P, Sworczak K. Role of Catestatin in the Cardiovascular System and Metabolic Disorders. Front Cardiovasc Med. 2022;9:909480. DOI:10.3389/fcvm.2022.909480
61. Мещеряков Ю.В., Губарева И.В., Губарева Е.Ю., Алексеева А.Ю. Роль катестатина в развитии и декомпенсации сердечной недостаточности: обзор литературы. Российский кардиологический журнал. 2021;26(S3):4492. DOI:10.15829/1560-4071-2021-4492
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Авторы
А.М. Алиева*1, Н.В. Теплова1, Е.В. Резник1,2, О.А. Эттингер1, Р.А. Фараджов1, Э.А. Хачирова1, И.В. Ковтюх1,3, И.А. Котикова1, Д.А. Сысоева1, И.Р. Бигушев1, И.Г. Никитин1
1 ФГАОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава России, Москва, Россия;
2 ГБУЗ «Городская клиническая больница №31» Департамента здравоохранения города Москвы», Москва, Россия;
3 НКЦ №2 ФГБНУ «Российский научный центр хирургии им. акад. им. Петровского» (ЦКБ РАН), Москва, Россия
*amisha_alieva@mail.ru
1 Pirogov Russian National Research Medical University, Moscow, Russia;
2 City Clinical Hospital No. 31, Moscow, Russia;
3 Scientific Clinical Center No. 2 of Petrovsky Russian Scientific Center of Surgery, Moscow, Russia
*amisha_alieva@mail.ru
1 ФГАОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава России, Москва, Россия;
2 ГБУЗ «Городская клиническая больница №31» Департамента здравоохранения города Москвы», Москва, Россия;
3 НКЦ №2 ФГБНУ «Российский научный центр хирургии им. акад. им. Петровского» (ЦКБ РАН), Москва, Россия
*amisha_alieva@mail.ru
________________________________________________
1 Pirogov Russian National Research Medical University, Moscow, Russia;
2 City Clinical Hospital No. 31, Moscow, Russia;
3 Scientific Clinical Center No. 2 of Petrovsky Russian Scientific Center of Surgery, Moscow, Russia
*amisha_alieva@mail.ru
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