Amyloidoza serca: utajona przyczyna powikłań sercowo-naczyniowych w praktyce onkologicznej Review article
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Opublikowane:
gru 31, 2014
Słowa kluczowe:
amyloidoza, kardiotoksyczność, rak, transtyretyna
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Abstrakt
Amyloidoza jest rzadką, aczkolwiek znaną przyczyną niewydolności serca, kardiomiopatii, choroby naczyń wieńcowych, dysfunkcji układu przewodzącego serca i uszkodzenia zastawek serca. Choroba często zostaje rozpoznana dopiero w zaawansowanym stadium. Obecnie wyróżniamy kilka typów amyloidozy. Przyczynami amyloidozy serca mogą być: choroba nowotworowa, przewlekły stan zapalny, czynniki genetyczne oraz procesy związane ze starzeniem się organizmu. Nadprodukcja białek amyloidogennych przez komórki guza odgrywa kluczową rolę w patogenezie amyloidozy łańcuchów lekkich. Powikłania sercowo-naczyniowe mogą być indukowane przez odkładające się depozyty nierozpuszczalnych nienatywnych białek bądź też na skutek bezpośredniego toksycznego działania amyloidogennych cząsteczek na kardiomiocyty i komórki śródbłonka naczyniowego. W pracy skupiliśmy się głównie na mechanizmach patofizjologicznych, klasyfikacji i sercowo-naczyniowej manifestacji klinicznej amyloidozy serca.
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Mladosievicova B, Poljak Z, El-Hassoun O, Roziakova L, Carter A. Amyloidoza serca: utajona przyczyna powikłań sercowo-naczyniowych w praktyce onkologicznej. OncoReview [Internet]. 31 grudzień 2014 [cytowane 23 lipiec 2024];4(4(16):137-43. Dostępne na: https://journalsmededu.pl/index.php/OncoReview/article/view/373
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Utwór dostępny jest na licencji Creative Commons Uznanie autorstwa – Użycie niekomercyjne 4.0 Międzynarodowe.
Copyright: © Medical Education sp. z o.o. This is an Open Access article distributed under the terms of the Attribution-NonCommercial 4.0 International (CC BY-NC 4.0). License (https://creativecommons.org/licenses/by-nc/4.0/), allowing third parties to copy and redistribute the material in any medium or format and to remix, transform, and build upon the material, provided the original work is properly cited and states its license.
Address reprint requests to: Medical Education, Marcin Kuźma (marcin.kuzma@mededu.pl)
Bibliografia
1. Guan J, Mishra S, Falk RH et al. Current perspectives on cardiac amyloidosis. Am J Physiol Heart Circ Physiol 2012; 302(3): H544-H552.
2. Poljak Z, El-Hassoun O, Hulín I et al. Cardial amyloidosis in the context of new pathophysiological knowledge. Cardiology Lett 2014; 23(4): 267-274.
3. Yusuf SW, Negi SI, Lenihan DJ. Infiltrative cardiomyopathy and pericardial disease. Semin Oncol 2013; 40(2): 199-209.
4. Gillmore JD, Hawkins PN. Pathophysiology and treatment of systemic amyloidosis. Nat Rev Nephrol 2013; 9(10): 574-586.
5. Pika T, Vymetal J, Latalova P. Amyloidosa a postižení srdce: 186-191. In: Mladosievicova B. et al. Kardioonkologie, 2. ed. Grada Publishing a.s. 2014, Praha.
6. Hemminki K, Li X, Försti A et al. Cancer risk in amyloidosis patients in Sweden with novel findings on non-Hodgkin lymphoma and skin cancer. Ann Oncol 2014; 25(2): 511-518.
7. Sawyer DB, Skinner M. Cardiac amyloidosis: shifting our impressions to hopeful. Curr Heart Fail Rep 2006; 3(2): 64-71.
8. Falk RH. Cardiac amyloidosis: a treatable disease, often overlooked. Circulation 2011; 124(9): 1079-1085.
9. Gertz MA, Dispenzieri A, Sher T. Pathophysiology and treatment of cardiac amyloidosis. Nat Rev Cardiol 2014. http://doi.org/10.1038/nrcardio 2014.165.
10. Abraham RS, Geyer SM, Price-Troska TL et al. Immunoglobulin light chainvariable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003; 101(10): 3801-3808.
11. Bellotti V, Chiti F. Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr Opin Struct Biol 2008; 18(6): 771-779.
12. Špalek P. Familiárna amyloidná polyneuropatia. Neurol prax 2013; 14(6): 296-300.
13. Quarta CC, Kruger JL, Falk RH. Cardiac amyloidosis. Circulation 2012; 126(12): e178-e182.
14. Falk RH, Dubrey SW. Amyloid heart disease. Prog Cardiovasc Dis 2010; 52(4): 347-361.
15. Dubrey SW, Falk RH. Amyloid heart disease. Br J Hosp Med 2010; 71: 76-82.
16. Banypersad SM, Moon JC, Whelan C et al. Updates in cardiac amyloidosis: a review. J Am Heart Assoc 2012; 1(2): e000364.
17. Steiner I. The prevalence of isolated atrial amyloid. J Pathol 1987; 153(4): 395-398.
18. Goette A, Röcken C. Atrial amyloidosis and atrial fibrillation: a gender-dependent “arrhythmogenic substrate”? Eur Heart J 2004; 25(14): 1185-1186.
19. Fikrle M, Paleček T, Kuchynka P et al. Cardiac amyloidosis: A comprehensive review. Cor et Vasa 2013; 55: e60-e75.
20. Millucci L, Ghezzi L, Bernardini G et al. Prevalence of isolated atrial amyloidosis in young patients affected by congestive heart failure. Scientific World Journal 2012: 29386.
21. Falk RH. AL amyloidosis or multiple myeloma? An important distinction. Br J Haematol 2014; 164(5): 748-9.
22. Dispenzieri A, Kyle RA, Gertz MA et al. Survival in patients with primary systemic amyloidosis and raised serum cardiac troponins. Lancet 2003; 361(9371): 1787-1789.
23. Merlini G, Seldin DC, Gertz MA. Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 2011; 29(14): 1924-1933.
24. Rapezzi C, Merlini G, Quarta CC et al. Systemic cardiac amyloidoses: disease profiles and clinical courses of the 3 main types. Circulation 2009; 120(13): 1203-1212.
25. Palladini G, Campana C, Klersy C et al. Serum n-terminal pro-brain natriuretic peptide is a sensitive marker of myocardial dysfunction in AL amyloidosis. Circulation 2003; 107: 2440-2445.
26. Palladini G, Merlini G. Systemic amyloidoses: what an internist should know. Eur J Intern Med 2013; 24(8): 729-739.
27. Levinson RT, Olatoye OO, Randles EG et al. Role of mutations in the cellular internalization of amyloidogenic light chains into cardiomyocytes. Sci Rep 2013; 3: 1278.
28. Peterson FC, Baden EM, Owen BA et al. A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. Structure 2010; 18: 563-570.
29. Martin DJ, Ramirez-Alvarado M. Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains. Amyloid 2010; 17: 129-136.
30. Biolo A, Ramamurthy S, Connors LH et al. Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: relationship to structural, functional myocardial changes and to light chain amyloid deposition. Circ Heart Fail 2008; 1(4): 249-257.
31. Shi J, Guan J, Jiang B et al. Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38alpha MAPK pathway. Proc Natl Acad Sci USA 2010; 107: 4188-4193.
32. Mishra S, Guan J, Plovie E et al. Human amyloidogenic light chain proteins result in cardiac dysfunction, cell death, and early mortality in zebrafish. Am J Physiol Heart Circ Physiol 2013; 305(1): H95-H103.
33. Guan J, Mishra S, Shi J et al. Stanniocalcin1 is a key mediator of amyloidogenic light chain induced cardiotoxicity. Basic Res Cardiol 2013; 108(5): 378.
34. Desai HV, Aronow WS, Peterson SJ et al. Cardiac amyloidosis: approaches to diagnosis and management. Cardiol Rev 2010;18 (1): 1-11.
35. Migrino RQ, Truran S, Gutterman DD et al. Human microvascular dysfunction and apoptotic injury induced by AL amyloidosis light chain proteins. Am J Physiol Heart Circ Physiol 2011; 301(6): H2305-H2312.
36. Halwani O, Delgado DH. Cardiac amyloidosis: an approach to diagnosis and management. Expert Rev Cardiovasc Ther 2010; 8(7): 1007-1013.
37. García-Pavía P, Tomé-Esteban MT, Rapezzi C. Amyloidosis. Also a heart disease. Rev Esp Cardiol (engl. ed.) 2011; 64(9): 797-808.
38. Feng D, Edwards WD, Oh JK et al. Intracardiac thrombosis and embolism in patients with cardiac amyloidosis. Circulation 2007; 116(21): 2420-2426.
39. Feng D, Klarich K, Oh JK. Intracardiac Thrombosis, Embolism and Anticoagulation Therapy in Patients with Cardiac Amyloidosis – Inspiration from a Case Observation. Online: http://cdn.intechopen.com/pdfs-wm/23846.pdf.
40. Dingli D, Utz JP, Gertz MA. Pulmonary hypertension in patients with amyloidosis. Chest 2001; 120: 1735-1738.
2. Poljak Z, El-Hassoun O, Hulín I et al. Cardial amyloidosis in the context of new pathophysiological knowledge. Cardiology Lett 2014; 23(4): 267-274.
3. Yusuf SW, Negi SI, Lenihan DJ. Infiltrative cardiomyopathy and pericardial disease. Semin Oncol 2013; 40(2): 199-209.
4. Gillmore JD, Hawkins PN. Pathophysiology and treatment of systemic amyloidosis. Nat Rev Nephrol 2013; 9(10): 574-586.
5. Pika T, Vymetal J, Latalova P. Amyloidosa a postižení srdce: 186-191. In: Mladosievicova B. et al. Kardioonkologie, 2. ed. Grada Publishing a.s. 2014, Praha.
6. Hemminki K, Li X, Försti A et al. Cancer risk in amyloidosis patients in Sweden with novel findings on non-Hodgkin lymphoma and skin cancer. Ann Oncol 2014; 25(2): 511-518.
7. Sawyer DB, Skinner M. Cardiac amyloidosis: shifting our impressions to hopeful. Curr Heart Fail Rep 2006; 3(2): 64-71.
8. Falk RH. Cardiac amyloidosis: a treatable disease, often overlooked. Circulation 2011; 124(9): 1079-1085.
9. Gertz MA, Dispenzieri A, Sher T. Pathophysiology and treatment of cardiac amyloidosis. Nat Rev Cardiol 2014. http://doi.org/10.1038/nrcardio 2014.165.
10. Abraham RS, Geyer SM, Price-Troska TL et al. Immunoglobulin light chainvariable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003; 101(10): 3801-3808.
11. Bellotti V, Chiti F. Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr Opin Struct Biol 2008; 18(6): 771-779.
12. Špalek P. Familiárna amyloidná polyneuropatia. Neurol prax 2013; 14(6): 296-300.
13. Quarta CC, Kruger JL, Falk RH. Cardiac amyloidosis. Circulation 2012; 126(12): e178-e182.
14. Falk RH, Dubrey SW. Amyloid heart disease. Prog Cardiovasc Dis 2010; 52(4): 347-361.
15. Dubrey SW, Falk RH. Amyloid heart disease. Br J Hosp Med 2010; 71: 76-82.
16. Banypersad SM, Moon JC, Whelan C et al. Updates in cardiac amyloidosis: a review. J Am Heart Assoc 2012; 1(2): e000364.
17. Steiner I. The prevalence of isolated atrial amyloid. J Pathol 1987; 153(4): 395-398.
18. Goette A, Röcken C. Atrial amyloidosis and atrial fibrillation: a gender-dependent “arrhythmogenic substrate”? Eur Heart J 2004; 25(14): 1185-1186.
19. Fikrle M, Paleček T, Kuchynka P et al. Cardiac amyloidosis: A comprehensive review. Cor et Vasa 2013; 55: e60-e75.
20. Millucci L, Ghezzi L, Bernardini G et al. Prevalence of isolated atrial amyloidosis in young patients affected by congestive heart failure. Scientific World Journal 2012: 29386.
21. Falk RH. AL amyloidosis or multiple myeloma? An important distinction. Br J Haematol 2014; 164(5): 748-9.
22. Dispenzieri A, Kyle RA, Gertz MA et al. Survival in patients with primary systemic amyloidosis and raised serum cardiac troponins. Lancet 2003; 361(9371): 1787-1789.
23. Merlini G, Seldin DC, Gertz MA. Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 2011; 29(14): 1924-1933.
24. Rapezzi C, Merlini G, Quarta CC et al. Systemic cardiac amyloidoses: disease profiles and clinical courses of the 3 main types. Circulation 2009; 120(13): 1203-1212.
25. Palladini G, Campana C, Klersy C et al. Serum n-terminal pro-brain natriuretic peptide is a sensitive marker of myocardial dysfunction in AL amyloidosis. Circulation 2003; 107: 2440-2445.
26. Palladini G, Merlini G. Systemic amyloidoses: what an internist should know. Eur J Intern Med 2013; 24(8): 729-739.
27. Levinson RT, Olatoye OO, Randles EG et al. Role of mutations in the cellular internalization of amyloidogenic light chains into cardiomyocytes. Sci Rep 2013; 3: 1278.
28. Peterson FC, Baden EM, Owen BA et al. A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. Structure 2010; 18: 563-570.
29. Martin DJ, Ramirez-Alvarado M. Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains. Amyloid 2010; 17: 129-136.
30. Biolo A, Ramamurthy S, Connors LH et al. Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: relationship to structural, functional myocardial changes and to light chain amyloid deposition. Circ Heart Fail 2008; 1(4): 249-257.
31. Shi J, Guan J, Jiang B et al. Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38alpha MAPK pathway. Proc Natl Acad Sci USA 2010; 107: 4188-4193.
32. Mishra S, Guan J, Plovie E et al. Human amyloidogenic light chain proteins result in cardiac dysfunction, cell death, and early mortality in zebrafish. Am J Physiol Heart Circ Physiol 2013; 305(1): H95-H103.
33. Guan J, Mishra S, Shi J et al. Stanniocalcin1 is a key mediator of amyloidogenic light chain induced cardiotoxicity. Basic Res Cardiol 2013; 108(5): 378.
34. Desai HV, Aronow WS, Peterson SJ et al. Cardiac amyloidosis: approaches to diagnosis and management. Cardiol Rev 2010;18 (1): 1-11.
35. Migrino RQ, Truran S, Gutterman DD et al. Human microvascular dysfunction and apoptotic injury induced by AL amyloidosis light chain proteins. Am J Physiol Heart Circ Physiol 2011; 301(6): H2305-H2312.
36. Halwani O, Delgado DH. Cardiac amyloidosis: an approach to diagnosis and management. Expert Rev Cardiovasc Ther 2010; 8(7): 1007-1013.
37. García-Pavía P, Tomé-Esteban MT, Rapezzi C. Amyloidosis. Also a heart disease. Rev Esp Cardiol (engl. ed.) 2011; 64(9): 797-808.
38. Feng D, Edwards WD, Oh JK et al. Intracardiac thrombosis and embolism in patients with cardiac amyloidosis. Circulation 2007; 116(21): 2420-2426.
39. Feng D, Klarich K, Oh JK. Intracardiac Thrombosis, Embolism and Anticoagulation Therapy in Patients with Cardiac Amyloidosis – Inspiration from a Case Observation. Online: http://cdn.intechopen.com/pdfs-wm/23846.pdf.
40. Dingli D, Utz JP, Gertz MA. Pulmonary hypertension in patients with amyloidosis. Chest 2001; 120: 1735-1738.