Амилоидоз легких цепей иммуноглобулинов (AL-амилоидоз)

Автор: Пирогова О.В.

Журнал: Вестник гематологии @bulletin-of-hematology

Рубрика: Обзор литературы

Статья в выпуске: 4 т.19, 2023 года.

Бесплатный доступ

Амилоидозы — это общий термин для группы заболеваний, обусловленных неправильной агрегацией белков и их отложением в органах и тканях в виде нерастворимых белковых фибрилл. Осно- вой амилоида является фибрилла, построенная из скрученных белковых протофиламентов. Системный амилоидоз легких цепей (AL) — одна из форм плазмоклеточных дискразий, характеризующихся гиперпродукцией свободных легких цепей иммуноглобулина клональными плазматическими клетками или В-лимфоцитами. В этом обзоре описывается история открытия, этапов диагностики и изменения подходов к терапии AL-амилоидоза. Выживаемость при AL-амилоидозе зависит от спектра вовлеченных в процесс органов, тяжести их поражения и гематологического ответа на лечение. Фибриллы легких цепей инфильтрируют миокард, препятствуют межклеточному взаимодействию, что приводит к повреждению клеток и внезапной сердечной смерти. Вот почему поражение сердца является основным предиктором исхода заболевания. Современный подход к диагностике и лечению основан на выделении наиболее уязвимой группы больных с IIIb стадией поражения сердца. Основной целью терапии является быстрое и глубокое подавление продукции амилоидогенных легких цепей. Терапия мелфаланом и аутологичная трансплантация гемопоэтических стволовых клеток долгое время считались стандартом лечения AL-амилоидоза, но добавление таргетных препаратов — бортезомиба, даратумумаба и венетоклакса кардинально повысило эффективность лечения.

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AL-амилоидоз, плазматические клетки, бортезомиб, даратумумаб, аутологичная трансплантация гемопоэтических стволовых клеток

Короткий адрес: https://sciup.org/170199873

IDR: 170199873

Список литературы Амилоидоз легких цепей иммуноглобулинов (AL-амилоидоз)

  • Merlini G., Bellotti V. Molecular mechanisms of amyloidosis. // N. Engl. J. Med. – 2003. – Vol. 349. - P. 583–596.
  • Dasari S., Theis J.D., Vrana J.A. et al. Amyloid typing by mass spectrometry in clinical practice: a comprehensive review of 16,175 samples. // Mayo Clin Proc. – 2020. Vol. 95. – P. 1852-1864.
  • Wainewright J. An Anatomical Treatise of the Liver: With the Diseases Incident to It. By a Member of the College of Physicians. – 1722. – P. 29–30.
  • Rokitansky, C. Handbuch der Speciellen Pathologischen Anatomica. – 1842. – P. 311 – 312.
  • Budd G. On diseases of the liver, 1st edn. London: John Churchill. – 1845. – P. 243.
  • Budd G. On diseases of the liver, 3rd edn. London: John Churchill. – 1857. –P. 312–336.
  • Gairdner W. T., Drummond J. On Some Points in the Pathology of the Liver. // Mon J Med Sci. – 1854 – Vol. 9, N 53. – P. 393–399.
  • Schleiden J. M. Scientific botany. First book: chemistry of Plants. - 1842. - P9.
  • Virchow R. Lecture XVII. Amyloid degeneration. Inflammation. // Cellular Pathology as Based Upon Physiological and Pathological Histology. – 1971. – P. 409 – 437.
  • Kyle R. A. Amyloidosis: a convoluted story. // Br J Haematol. – 2001. – Vol. 114, N 3. – P. 529-538.
  • Sipe J. D. Cohen AS. Review: history of the amyloid fibril. // J Struct Biol. – 2000. Vol. 130, N 2-3. – P. 88-98.
  • Wilks S. Cases of lardaceous disease and some allied affections. With remarks. // Guy's Hospital Reports. – 1856. - Vol. 2. – P. 103 – 132.
  • Wilks S. Report on lardaceous disease. // Guy's Hospital Reports. – 1865. Vol. 11. P. 45 – 55.
  • Weber H. Mollities ossium, doubtful whether carcinomatous or syphilitic. // Transactions of the Pathological Society of London. – 1867. – Vol. 18. - P. 206 – 210.
  • Hodkinson H.M, Pomerance A. The clinical significance of senile cardiac amyloidosis: a prospective clinico-pathological study. // Q J Med. – 1977. – Vol. 46, N 183. – P. 381 - 387.
  • Bennhold H. Specific staining of amyloid by Congo red. // Münchener Medizinische Wochenschrift. – 1922. - Vol 69. - 1537–1538.
  • Divry P., Florkin M. Sur les propriétés optiques de l'amyloïde. // CR Société de Biologie. – 1927. – Vol. 97. –P. 1808 – 1810.
  • Lubarsch O. Zur Kenntnis ungewöhnlicher Amyloidablagerungen. // Arch. path. Anat. – 1929. - Vol. 271. – P. 867-889.
  • Dahlin D. C.: Primary Amyloidosis, With Report of 6 Cases. // Am. J. Path. – 1949. –Vol. 25. – P. 105 - 124.
  • Magnus-Levy A.: Bence-Jones-Eiweiss und Amyloid. // Ztschr. klin. Med. – 1931. Vol. 116. – P. 510-531.
  • Magnus-Levy A.: Multiple Myelome. VII. Euglobulinämie. Zur Klinik und Pathologie, Amyloidosis. // Z. klin. Med. – 1934. - Vol.126. – P. 62.
  • Magnus-Levy A.: Multiple Myeloma: Etwas vom Eiweisshaushalt der Geschwülste des Knochenmarks, von Nephrosen und vom Amyloid. // Deutsche med. Wchnschr. – 1931. -Vol. 57. – P. 703-706.
  • Magnus-Levy A. Multiple myelome. // Acta Medica Scandinavica. – 1938. – Vol. 95. - P. 217 – 280.
  • Magnus-Levy A. Amyloidosis in multiple myeloma. Progress noted in 50 years of personal observation. // Journal of the Mount Sinai Hospital. – 1952. Vol. 19. - P 8 – 9.
  • Atkinson F. R. B. Multiple Myelomata. // M. Press. – 1937. - Vol.195. - P. 312-317.
  • Apitz K. Die Paraproteinosen (Über die Störung des Eiweisstoffwechsels bei Plasmocytom). // Virchows Archiv für Pathologische Anatomie und Physiologie (B). – 1940. – Vol. 306. – P. 631 – 639.
  • Cohen A.S., Calkins E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. // Nature. - 1959. - Vol. 183. - P. 1202 – 1203.
  • Cohen A.S., Calkins E. The Isolation of Amyloid Fibrils and a Study of the Effect of Collagenase and Hyaluronidase. // J Cell Biol. – 1964. – Vol. 21. – P. 481 - 486.
  • Kyle R.A., Bayrd E.D. Primary systemic amyloidosis and myeloma: discussion of relationship and review of 81 cases. // Archives of Internal Medicine. – 1961. – Vol. 107. P. 344 – 353.
  • Eanes E.D., Glenner G.G. X-ray diffraction studies on amyloid filaments. // Journal of Histochemistry and Cytochemistry. – 1968. – Vol. 16. P. 673 – 677.
  • Glenner G.G., Terry W., Harada, M. et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. // Science. 1971a. – Vol. 172. – P. 1150 – 1151.
  • Glenner G.G., Ein D., Eanes, E.D. et al. Creation of ‘amyloid’ fibrils from Bence Jones protein in vitro. // Science. - 1971b. – Vol. 174. – P 712 –714.
  • Kyle R.A, Bayrd E.D. Amyloidosis: review of 236 cases. // Medicine. – 1975. – Vol. 54. – Vol. 271 – 299.
  • Kyle R.A, Greipp P.R. Amyloidosis (AL): clinical and laboratory features in 229 cases. // Mayo Clin Proc. – 1983. – Vol. 58. – P. 665 - 683.
  • Kyle R.A, Gertz M.A. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. // Semin Hematol. – 1995. – Vol. 32. - P. 45-59.
  • Cohen A.S, Rubinow A., Anderson JJ. et al. Survival of patients with primary (AL) amyloidosis: colchicine-treated cases from 1976 to 1983 compared with cases seen in previous years (1961 to 1973). // Am J Med. – 1987. – Vol. 82. - P. 1182-1190.
  • Kyle R.A, Greipp P.R. Primary systemic amyloidosis: comparison of melphalan and prednisone versus placebo. // Blood. – 1978. - Vol. 52. - P. 818-827
  • Kyle R.A., Gertz M.A., Greipp P.R. et al. A trial of three regimens for primary amyloidosis: colchicine alone, melphalan and prednisone, and melphalan, prednisone and colchicine. // New England Journal of Medicine. – 1997. - Vol. 336. - P. 1202 – 1207.
  • Comenzo R.L, Vosburgh E, Falk R.H. et al. Dose-intensive melphalan with blood stem-cell support for the treatment of AL (amyloid light-chain) amyloidosis: survival and responses in 25 patients. // Blood. – 1998. - Vol. 91, N 10. – P. 3662-3670.
  • Iadanza M.J., Jackson M.P., Eric W Hewitt et al. A new era for understanding amyloid structures and disease. // Nat Rev Mol Cell Biol. – 2018. Vol. 12. – P. 755-773.
  • Sipe J. D., Benson M.D., Buxbaum J.N. et al. Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. // Amyloid. – 2016. – Vol. 23. - P. 209–213.
  • Kourelis T. V., Kyle R.K., Dingli D. et al. Presentation and outcomes of localized immunoglobulin light chain amyloidosis: the Mayo Clinic experience. // Mayo Clin. Proc. – 2017. - Vol. 92. - P. 908–917.
  • Dobson C.M. Protein Folding and Misfolding. // Nature. – 2003. Vol. 426. P. 884–890.
  • Khurana R., Gillespie J.R., Talapatra A. et al. Partially Folded Intermediates as Critical Precursors of Light Chain Amyloid Fibrils and Amorphous Aggregates. // Biochemistry. – 2001. – Vol. 40. – P. 3525 – 3535.
  • Yerbury J. J., Ooi L., Dillin A. et al. Walking the tightrope: proteostasis and neurodegenerative disease. // J. Neurochem. – 2016. – Vol. 137. - P. 489–505.
  • Labbadia J., Morimoto R. I. The biology of proteostasis in aging and disease. // Annu. Rev. Biochem. – 2015. - Vol.84. - P 435–464.
  • Wickner S., Maurizi M.R., Gottesman S. Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins. // Science. – 1999. – Vol. 286. – P. 1888 – 1893.
  • Merlini G., Bellotti V. Molecular Mechanisms of Amyloidosis. // N. Engl. J. Med. – 2003. - Vol. 349. - P. 583 – 596.
  • Merlini G., Stone M. J. Dangerous small B cell clones. // Blood. – 2006. – Vol. 108. – P. 2520 – 2530.
  • Bochtler T., Hegenbart U., Heisset C. et al. Hyperdiploidy is less frequent in AL amyloidosis compared with monoclonal gammopathy of undetermined significance and inversely associated with translocation t(11. - Vol. 14). // Blood. - Vol. 117. – P. 3809 – 3815.
  • Morgan G. J., Kelly J. W. The kinetic stability of a full-length antibody light chain dimer determines whether endoproteolysis can release amyloidogenic variable domains. // J. Mol. Biol. – 2016. – Vol. 428. – P. 4280 – 4297.
  • Blancas-Mejia L. M. et al. Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding. Biophys. // Chem. – 2015. - Vol. 207. – P. 13 – 20.
  • Oberti L. et al. Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity. Sci. Rep. – 2017. – Vol. 7. – P.16809.
  • Westermark G. T., Fandrich M., Lundmark K., Westermark P. Noncerebral amyloidoses: aspects on seeding, cross-seeding, and transmission. // Cold Spring Harb. Perspect. Med. - 2018. - Vol. 8. – P. 024323.
  • Bourne P. C., Ramsland P.A., Shan L. et al. Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties. // Acta Crystallogr Sect D Biol Crystallogr. – 2002. – Vol. 58. – P. 815 – 823.
  • Oberti L., Rognoni P., Barbiroli A. et al. Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity. // Sci Rep. – 2017. - Vol. 7. - P. 1 – 11.
  • Kazman P., Vielberg M.T., Cendales M.D.P., et al. Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation. // Elife. – 2020. – Vol. 9. - P. 1 – 23.
  • Lavatelli F., Perlman D.H., Spencer B., et al. Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue. // Mol Cell Proteomics. - 2008. – Vol. 7. – P. 1570–1583.
  • Lavatelli F., Mazzini G., Ricagno S, et al. Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis:insights into the timing of proteolysis. // J Biol Chem. – 2020. – Vol. 295. – P. 16572–16584.
  • Buxbaum J.N., Chuba J.V., Hellman G.C., Solomon A, Gallo G.R. Monoclonal immunoglobulin deposition disease: light chain and light and heavy chain deposition diseases and their relation to light chain amyloidosis. Clinical features, immunopathology, and molecular analysis. Ann Intern Med. 1990. - Vol. 112:455–64.
  • Enqvist S, Sletten K, Westermark P. Fibril protein fragmentation pattern in systemic AL-amyloidosis. J Pathol. 2009. - Vol. 219. – P. 473–480.
  • Ferrone F. Analysis of protein aggregation kinetics. // Methods Enzymol. – 1999. Vol. 309. –P. 256–274.
  • Glabe C. G., Kayed, R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. // Neurology. -2006. - Vol.66. – P. 74–78.
  • Ami D., Lavatelli F., Rognoni P. et al. In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study. // Sci. Rep. – 2016. -.P. 29096.
  • Diomede L., Romeo M., Rognoni P. et al. Cardiac light chain amyloidosis: the role of metal ions in oxidative stress and mitochondrial damage. // Antioxid. Redox Signal. 2017. – Vol. 27. – P. 567–582.
  • Marin-Argany M., Lin Y., Misra P. et al. Cell damage in light chain amyloidosis: fibril internalization, toxicity and cell-mediated seeding. // J. Biol. Chem. – 2016. – Vol. 291. - P. 19813–19825.
  • Merlini G., Dispenzieri A., Sanchorawala V. et al. Systemic immunoglobulin light chain amyloidosis. // Nature Reviews Disease Primers. -2018. – Vol. 4. P. 38.
  • Naiki H., Gejyo F. Methods in Enzymology.// Academic Press. -1999.- Vol. - P. 305–318.
  • Nystrom S. N., Westermark G. T. AA-amyloid is cleared by endogenous immunological mechanisms. // Amyloid. -2012. – Vol. 19. – P. 138–145.
  • Pepys M. B. Amyloidosis. // Annu. Rev. – 2006. -Med. Vol. 57. –- P. 223–241.
  • McCausland K.L., White M.K., Guthrie S.D.et al. Light chain (AL) amyloidosis: the journey to diagnosis. // Patient. - 2018. - Vol. 11.- P. 207-216.
  • Muchtar E., Dispenzieri A., Gertz M., Kumar S. et al. Treatment of AL Amyloidosis: Mayo Stratification of Myeloma and Risk- Adapted Therapy (mSMART) Consensus Statement 2020 Update. // Mayo Clin Proc. 2021 Jun. - Vol. 96(6).- P.1546-1577.
  • Gertz M.A., Comenzo R., Falk R.H.et al. Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): a consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis, Tours, France, 18-22 April 2004. Am J Hematol. - 2005. - Vol. 79.- P. 319-328
  • Muchtar E., Gertz M.A., Kyle R.A.et al. A modern primer on light chain amyloidosis in 592 patients with mass spectrometry–verified typing. // Mayo Clin Proc. - 2019. - Vol. 94.- P. 472-483.
  • Kourelis T. V., Dasari S., Theis J. et al. Clarifying immunoglobulin gene usage in systemic and localized immunoglobulin lightchain amyloidosis by mass spectrometry. // Blood. – 2017. - Vol. 129. – P. 299–306.
  • Comenzo R. L., Zhang Y., Martinez C., Osman, K., Herrera G. A. The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig V-L germ line gene use and clonal plasma cell burden. // Blood. - 2001. – Vol. 98. P. 714–720.
  • Perfetti V., Palladini G., Casarini S. et al. The repertoire of lambda light chains causing predominant amyloid heart involvement and identification of a preferentially involved germline gene, IGLV1-44. Blood. – 2012. – Vol. 119. P. 144–150.
  • Quarta C.C., Gonzalez-Lopez E., Gilbertson J.A. et al. Diagnostic sensitivity of abdominal fat aspiration in cardiac amyloidosis. // Eur. Heart J. – 2017. –Vol. 38. – P. 1905–1908.
  • Muchtar E., Dispenzieri A., Lacy M. et al. Overuse of organ biopsies in immunoglobulin light chain amyloidosis (AL): the consequence of failure of early recognition. // Ann. Med. – 2017. – Vol. 49. – P. 545–551.
  • Vrana J. A., Theis J.D., Dasari S. et al. Clinical diagnosis and typing of systemic amyloidosis in subcutaneous fat aspirates by mass spectrometry-based proteomics. // Haematologica. - 2014. – Vol. 99. – P. 1239-1247.
  • Schonland, S. O., Hegenbart U., Bochtler T et al. Immunohistochemistry in the classification of systemic forms of amyloidosis: a systematic investigation of 117 patients. // Blood. 2012. - Vol.119. P. 488–493.
  • Linke R. On typing amyloidosis using immunohistochemistry. Detailled illustrations, review and a note on mass spectrometry. // Prog. Histochem. Cytochem. - 2012. – Vol. 47. P. 61–132.
  • Fernandez de Larrea C., Verga L., Morbini P. et al. A practical approach to the diagnosis of systemic amyloidoses. // Blood. – 2015. - Vol. 125. – P. 2239–2244.
  • Kourelis T.V., Kumar S.K., Go R.S. et al. Immunoglobulin light chain amyloidosis is diagnosed late in patients with preexisting plasma cell dyscrasias. // Am. J. Hematol. – 2014. – Vol. 89. – P.1051–1054.
  • 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. – Vol.107. – P. 2440–2445. This study introduces NT-proBNP as a sensitive marker for the diagnosis and follow-up after therapy of amyloid cardiac dysfunction.
  • Wechalekar A.D., Gillmore J.D., Wassef N. et al. Abnormal N-terminal fragment of brain natriuretic peptide in patients with light chain amyloidosis without cardiac involvement at presentation is a risk factor for development of cardiac amyloidosis. // Haematologica. – 2011. - Vol. 96. –P. 1079–1080.
  • Palladini G., Hegenbart U., Milani P. et al. A staging system for renal outcome and early markers of renal response to chemotherapy in AL amyloidosis. // Blood. – 2014. – Vol. 124. P. 2325–2332.
  • Palladini G., Basset M., Milani P. et al. Biomarker-based screening of organ dysfunction in patients with MGUS allows early diagnosis of AL amyloidosis. // Blood. -2017. –Vol. 130. – P. 1760.
  • Wechalekar A.D., Schonland S.O., Kastritis E. et al. A European collaborative study of treatment outcomes in 346 patients with cardiac stage III AL amyloidosis. // Blood. - 2013. - Vol. 121. – P. 3420–3427.
  • Dispenzieri A., Gertz M.A., Kyle R.A. et al. Serum cardiac troponins and N-terminal pro-brain natriuretic peptide: a staging system for primary systemic amyloidosis. // J. Clin. Oncol. 2004. - Vol. 22. – P. 3751–3757.
  • Kristen A.V., Giannitsis E., Lehrke S. et al. Assessment of disease severity and outcome in patients with systemic light-chain amyloidosis by the high-sensitivity troponin T assay. // Blood. -2010. – Vol. 116. –P. 2455–2461.
  • Palladini G., Barassi A., Klersy C. et al. The combination of high-sensitivity cardiac troponin T (hs-cTnT) at presentation and changes in N-terminal natriuretic peptide type B (NT-proBNP) after chemotherapy best predicts survival in AL amyloidosis. // Blood. -2010. – Vol. 116. – P. 3426–3430.
  • Kumar S., Dispenzieri A., Lacy M.Q. et al. Revised prognostic staging system for light chain amyloidosis incorporating cardiac biomarkers and serum free light chain measurements. J. Clin. Oncol. – 2012. - Vol. 30. – P. 989–995.
  • Palladini G., Milani P., Foli A. Oral melphalan and dexamethasone grants extended survival with minimal toxicity in AL amyloidosis: long-term results of a risk-adapted approach. // Haematologica. – Vol. 99. – P. 743–750.
  • Kastritis E., Gavriatopoulou M., Roussou M. et al. Renal outcomes in patients with AL amyloidosis: prognostic factors, renal response and the impact of therapy. //Am. J. Hematol. – 2017. - Vol. 92. – P. 632–639.
  • Sanchorawala V. Light-chain (AL) amyloidosis: diagnosis and treatment. // Clin J Am Soc Nephrol. - 2006. - Vol. 1.- P.1331–41.
  • Griffin .J.M, Rosenblum H., Maurer M.S. Pathophysiology and therapeutic approaches to cardiac amyloidosis. // Circ Res. – 2021. – Vol.128.- P.1554–75.
  • Garcia-Pavia P. Rapezzi C. Adler Y., et al. Diagnosis and treatment of cardiac amyloidosis: a position statement of the ESC working group on myocardial and pericardial diseases.// Eur Heart J. – 2021. - Vol 42. –P.1554–68.
  • Manolis A.S., Manolis A.A., Manolis T.A., Melita H. Cardiac amyloidosis: An underdiagnosed/underappreciated disease. // Eur J Intern Med. – 2019. – Vol. 67. – P.1–13.
  • Ihne S., Morbach C., Obici L. Amyloidosis in heart failure. // Curr Heart Fail Rep. - 2019. - Vol 16.- P.285–303.
  • Siddiqi O.K., Ruberg F.L. Cardiac amyloidosis: an update on pathophysiology, diagnosis, and treatment. // Trends Cardiovasc Med. – 2018. Vol. 28.- P.10–21.
  • Rubin J., Maurer M. S. Cardiac amyloidosis: overlooked, underappreciated, and treatable. // Annu Rev Med. – 2020. – Vol. 71. - P.203–19.
  • Palladini G., Schonland S.O., Sanchorawala V., et al. Clarification on the definition of complete haematologic response in lightchain (AL) amyloidosis. // Amyloid. 2021. - Vol. 28. - P.1–2.
  • Palladini G., Dispenzieri A., Gertz M.A., et al. New criteria for response to treatment in immunoglobulin light chain amyloidosis based on free light chain measurement and cardiac biomarkers: impact on survival outcomes. // J Clin Oncol. 2012. - Vol. 30, N 36.- P.4541–4549.
  • Manwani R., Cohen O., Sharpley F., et al. A prospective observational study of 915 patients with systemic AL amyloidosis treated with upfront bortezomib. // Blood. 2019. - Vol. 134, N 25. - P. 2271–2280.
  • Sidana S., Dispenzieri A., Murray D.L., et al. Revisiting complete response in light chain amyloidosis. // Leukemia. 2020. - Vol. 34, N 5. - P. 1472–1475.
  • Muchtar E., Gertz M.A., Lacy M.Q., et al. Refining amyloid complete hematological response: quantitative serum free light chains superior to ratio. // Am J Hematol. 2020. - Vol. 95, N 11.- P. 1280–1287.
  • Milani P., Basset M., Nuvolone M., et al. Indicators of profound hematologic response in AL amyloidosis: complete response remains the goal of therapy. // Blood Cancer J. - 2020. - Vol. 10, N 8. - P.90.
  • Kastritis E., Fotiou D., Theodorakakou F., et al. Timing and impact of a deep response in the outcome of patients with systemic light chain (AL) amyloidosis. // Amyloid. 2021. - Vol. 28, N 1. - P.3–11.
  • Пирогова О.В., Кудяшева О.В., Смирнова А.Г. Роль трансплантации аутологичных гемопоэтических стволовых клеток в лечении пациентов с системным AL-амилоидозом. // Клиническая онкогематология. - 2023. – Том. № 16, № 2. - С.128–36.
  • Sanchorawala V., Boccadoro M., Gertz M., et al. Guidelines for high dose chemotherapy and stem cell transplantation for systemic AL amyloidosis: EHA-ISA working group guidelines. // Amyloid. - 2022. - Vol. 29, N 1.- P. 1-7.
  • Basset M., Milani P., Nuvolone M., et al. Sequential response-driven bortezomib-based therapy followed by autologous stem cell transplant in AL amyloidosis. // Blood Adv. - 2020. Vol 4. - P. 4175–9.
  • Dispenzieri A., Buadi F., Kumar S.K., et al. Treatment of immunoglobulin light chain amyloidosis: Mayo stratification of myeloma and risk-adapted therapy (mSMART) consensus statement. // Mayo Clin Proc. - 2015. - Vol. 90. - P.1054–81.
  • Wechalekar A.D., Cibeira M.T., Gibbs S.D., et al. Guidelines for non-transplant chemotherapy for treatment of systemic AL amyloidosis: EHA-ISA working group. // Amyloid. - 2022. - Vol. 2022. - P. 1–15.
  • Colvin M. Alkylating agents. // Holland-Frei Cancer Medicine Hamilton. - 2003.
  • Driscoll J.J., Girnius S. Proteasome inhibitors to treat AL amyloidosis. // Exploring New Findings on Amyloidosis. - 2016.
  • Tanaka K. The proteasome: overview of structure and functions. // Proc Jpn Acad Ser B Phys Biol Sci. - 2009. - Vol. 85.- P.12–36.
  • Thibaudeau T.A., Smith D.M. A practical review of proteasome pharmacology. // Pharmacol Rev. - 2019. - Vol. 71. - P.170–97.
  • Oliva L., Orfanelli U., Resnati M., et al. The amyloidogenic light chain is a stressor that sensitizes plasma cells to proteasome inhibitor toxicity. // Blood. - 2017. - Vol. 129. - P.2132–42.
  • Kervoëlen C., Ménoret E., Gomez-Bougie P. et al. Dexamethasone-induced cell death is restricted to specific molecular subgroups of multiple myeloma. // Oncotarget. - 2015. - Vol. 6.- P.26922–34.
  • Bézard M., Oghina S., Vitiello D., et al. Dexamethasone is associated with early deaths in light chain amyloidosis patients with severe cardiac involvement. // PLoS ONE. - 2021. - Vol. 16.- P.e0257189.
  • Le Bras F., Molinier-Frenkel V., Guellich A., et al. Sequential cyclophosphamide-bortezomib-dexamethasone unmasks the harmful cardiac effect of dexamethasone in primary light-chain cardiac amyloidosis. // Eur J Cancer. - 2017. - Vol. 76.- P.183–7.
  • Bazzi T., Kropman K., Benjamin M., Al-Rammahi A. Light chain amyloidosis presenting as a septic shock: a case report and review of literature. // Cureus. - 2022. - Vol. 14.- P.e30263.
  • Kastritis E., Wechalekar A., Schönland S. et al. Challenges in the management of patients with systemic light chain (AL) amyloidosis during the covid-19 pandemic. Br J Haematol. - 2020. - Vol. 190. – P. 346–57.
  • van de Donk N.W.C.J., Richardson P.G., Malavasi F. Cd38 antibodies in multiple myeloma: back to the future. Blood. - 2018. - Vol. 131.-P.13–29.
  • Kastritis E., Palladini G., Minnema M.C. et al. Daratumumab-Based Treatment for Immunoglobulin Light-Chain Amyloidosis. // N Engl J Med. - 2021. - Vol. 385, N 1.- P. 46-58.
  • Kastritis E., Leleu X., Arnulf B.et al. Bortezomib, melphalan, and dexamethasone for light-chain amyloidosis. // J Clin Oncol. - 2020. - Vol. 38.- P. 3252-3260
  • Cibeira M.T., Oriol A., Lahuerta J.J., et al. Phase II trial of lenalidomide, dexamethasone and cyclophosphamide (lendexal) for previously untreated patients with light-chain amyloidosis. // Haematologica. - 2014. - Vol. 99. - P. 117–118.
  • Moreau P., Jaccard A., Benboubker L., et al. Lenalidomide in combination with melphalan and dexamethasone in patients with newly diagnosed light-chain (AL)-amyloidosis: a multicentre phase I/II dose escalation study. // Amyloid. 2010. - Vol. 17. - P. 87–88.
  • Kastritis E., Dialoupi I., Gavriatopoulou M., et al. Primary treatment of light-chain amyloidosis with bortezomib, lenalidomide, and dexamethasone. // Blood Adv. 2019. - Vol. 3, N 20. - P. 3002–3009.
  • Milani P., Sharpley F., Schonland S.O., et al. Pomalidomide and dexamethasone grant rapid haematologic responses in patients with relapsed and refractory AL amyloidosis: a European retrospective series of 153 patients. // Amyloid. 2020. - Vol. 27, N 4. - P.231–236.
  • Dispenzieri A., Buadi F., Laumann K., et al. Activity of pomalidomide in patients with immunoglobulin light-chain amyloidosis. // Blood. - 2012. - Vol. 119, N 23.- P. 5397–5404.
  • Wechalekar A.D., Schonland S.O., Kastritis E, et al. A European collaborative study of treatment outcomes in 346 patients with cardiac stage III AL amyloidosis. // Blood. - 2013. - Vol. 121, N 17.- P. 3420–3427.
  • Le Bras F., Molinier-Frenkel V., Guellich A., et al. Sequential cyclophosphamide-bortezomib-dexamethasone unmasks the harmful cardiac effect of dexamethasone in primary light-chain cardiac amyloidosis. // Eur J Cancer. - 2017. - Vol. 76. - P.183–187.
  • Kastritis E., Minnema M.C., Dimopoulos M.A., et al. Efficacy and safety of daratumumab monotherapy in newly diagnosed patients with stage 3b light chain amyloidosis: a phase 2 study by the European myeloma network. // Blood. - 2021. - Vol. 138 (Supplement 1). - P. 2730–2730
  • Kimmich C.R., Terzer T., Benner A., et al. Daratumumab for systemic AL amyloidosis: prognostic factors and adverse outcome with nephrotic-range albuminuria. // Blood. - 2020. - Vol. 135, N18. - P. 1517–1530.
  • Sidana S., Larson D.P., Greipp P.T., et al. IgM AL amyloidosis: delineating disease biology and outcomes with clinical, genomic and bone marrow morphological features. // Leukemia. - 2020. - Vol. 34, N5. - P. 1373–1382.
  • Milani P., Schonland S., Merlini G., et al. Treatment of AL amyloidosis with bendamustine: a study of 122 patients. // Blood. - 2018. - Vol. 132, N 18. - P. 1988–1991.
  • Manwani R., Sachchithanantham S., Mahmood S., et al. Treatment of IgM-associated immunoglobulin light-chain amyloidosis with rituximab-bendamustine. // Blood. 2018. - Vol. 132. - P.761–764.
  • Pika T., Hegenbart U., Flodrova P., et al. First report of ibrutinib in IgM-related amyloidosis: few responses, poor tolerability, and short survival. // Blood. - 2018. - Vol. 131. - P. 368–371.
  • Gupta V.A., Ackley J., Kaufman J.L., et al. BCL2 family inhibitors in the biology and treatment of multiple myeloma. // Blood Lymphat Cancer. - 2021. - Vol. 11. - P.11–24.
  • Kumar S.K., Harrison S.J., Cavo M., et al. Venetoclax or placebo in combination with bortezomib and dexamethasone in patients with relapsed or refractory multiple myeloma (BELLINI): a randomised, double-blind, multicentre, phase 3 trial. // Lancet Oncol. - 2020. - Vol. 21(12). - P.1630–1642.
  • Premkumar V.J., Lentzsch S., Pan S., et al. Venetoclax induces deep hematologic remissions in t(11;14) relapsed/refractory AL amyloidosis. // Blood Cancer J. - 2021. - Vol. 11(1). - P.10.
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