История изучения амилоидоза: от теории Рокитанского до настоящих дней

Рамеев В.В., Лысенко (Козловская) Л.В. История изучения амилоидоза: от теории Рокитанского до настоящих дней. Терапевтический архив. 2024;96(6):635–640. DOI: 10.26442/00403660.2024.06.202732

© ООО «КОНСИЛИУМ МЕДИКУМ», 2024 г.

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Rameev VV, Lysenko (Kozlovskaya) LV. History of the study of amyloidosis: from the Rokitansky’s theory to the present day. Terapevticheskii Arkhiv (Ter. Arkh.). 2024;96(6):635–640. DOI: 10.26442/00403660.2024.06.202732

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Аннотация

В истории изучения амилоидоза преимущественно доминировала концепция дискразии жидкостей – диспротеиноза, которая вылилась в конечном итоге в признание ведущей роли в генезе заболевания амилоидогенности белка-предшественника, выявление и элиминация которого из крови составляют основную диагностическую и терапевтическую задачу в клинике. Данный подход оказался высокоэффективным в отношении наиболее распространенных форм амилоидоза – вторичного и первичного – с аномально высокими концентрациями белков-предшественников в крови. Менее распространены и медленнее прогрессируют наследственные формы амилоидоза, в том числе транстиретинового, которые меньше зависят от амилоидогенности белка-предшественника, а применение, например, стабилизаторов транстиретина или блокада его синтеза при транстиретиновом амилоидозе имеет ограниченную эффективность. Для объяснения патогенеза приведенных форм более приемлема концепция локального макрофагального синтеза амилоида, которая развивается с середины ХХ в. Современные методы протеомного анализа позволяют подтвердить ключевую роль макрофага в амилоидогенезе и необходимость тщательного исследования механизмов макрофагальной аутофагии – главного инструмента поддержания белкового гомеостаза в клетке. Соответственно, не следует ожидать высокой эффективности и от химического растворения амилоида in vivo, потому что активность химической субстанции всегда будет контролироваться макрофагом.

Ключевые слова: амилоидоз, дискразия, K. Рокитанский, сальная болезнь, P. Вирхов, конго красный, макрофаг, аутофагия, протеомный анализ, шапероны, убиквитиновая протеасома

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In the history of amyloidosis studying the concept of liquids dyscrasia has been predominated and finally it is resulted in accepting a serum protein-precursor as a leading amyloidogenic factor in the disease pathogenesis. Consequently basic diagnostic and treatment strategy was aimed to find and eliminate this protein from the blood and this approach evidenced high effectiveness in most frequent AA and AL-amyloidosis characterized with anomaly high levels of precursors in the blood. At the same time there are less frequent and slower progressing inheritant forms of systemic amyloidosis including transthyretin induced, which are less depending on amyloidogenecity of amyloid precursor and because of that, in example, the effectiveness of transthyretin stabilizers or blockers of its synthesis is limited comparing with the precursor elimination in AA or AL. Developed in the middle of XX century a theory of local synthesis by macrophages is more preferable to describe the pathogenesis of these forms. And modern proteome analysis using give rise to confirm the key meaning of macrophage in the amyloidogenesis and proves necessity to know deeply mechanisms of macrophagial autophagia – basic tool of maintaining intracellular protein homeostasis. That is why it is difficult to hope on high effectiveness of chemical amyloid solvents in vivo, which being under macrophages regulation never could realize its chemical activities.

Keywords: amyloidosis, dyscrasia, K. Rokitansky, lardaceous disease, R. Virchow, congo red, macrophage, autophagy, proteomic analysis, chaperones, ubiquitine proteasome

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Список литературы

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14. Cohen DH, Feiner H, Jensson O, Frangione B. Amyloid fibril in hereditary cerebral hemorrhage with amyloidosis (HCHWA) is related to the gastroentero-pancreatic neuroendocrine protein, gamma trace. J Exp Med. 1983;158(2):623-8. DOI:10.1084/jem.158.2.623
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32. Gomes RA, Franco C, Da Costa G, et al. The proteome response to amyloid protein expression in vivo. PLoS One. 2012;7(11):e50123. DOI:10.1371/journal.pone.0050123
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34. Baskakov IV. Thermodynamics and Protein Folding. Amyloid proteins. The beta-sheet conformation and disiease. Weinheim: WILEY-VCH, 2005.

________________________________________________

1. Cohen AS, Calkins E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature. 1959;183(4669):1202-3. DOI:10.1038/1831202a0
2. Kyle RA. Amyloidosis: a convoluted story. Br J Haematol. 2001;114(3):529-38. DOI:10.1046/j.1365-2141.2001.02999.x
3. Nienhuis HL, Bijzet J, Hazenberg BP. The Prevalence and Management of Systemic Amyloidosis in Western Countries. Kidney Dis (Basel). 2016;2(1):10-9. DOI:10.1159/000444206
4. Abu Ali Ibn Sina. Kanon vrachebnoi nauki. Tashkent: Fan, 1981 (in Russian).
5. Schwartz P. Amyloidosis, expression and cause of presenile and senile mental and physical regression. A revision of the amyloid problem (author's transl). Zentralbl Allg Pathol. 1975;119(6):533-48 (in German).
6. Amyloidosis. Proceedings of the symposium on amyloidosis, University of Groningen, the Netherlands, September 24–28, 1967. Amsterdam: Excepta Medica Foundation, 1968.
7. Vinogradova O.M. Pervichnyi i geneticheskie varianty amiloidoza. Moscow: Meditsina, 1980 (in Russian).
8. Pras M, Zucker-Franklin D, Rimon A, Franklin EC. Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations. J Exp Med. 1969;130(4):777-96. DOI:10.1084/jem.130.4.777
9. Glenner GG, Terry W, Harada M, et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971;172(3988):1150-1. DOI:10.1126/science.172.3988.1150
10. Glenner GG, Ein D, Eanes ED, et al. Creation of "amyloid" fibrils from Bence Jones proteins in vitro. Science. 1971;174(4010):712-4. DOI:10.1126/science.174.4010.712
11. Benditt EP, Eriksen N, Hermodson MA, Ericsson LH. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971;19(2):169-73. DOI:10.1016/0014-5793(71)80506-9
12. Sletten K, Westermark P, Natvig JB. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J Exp Med. 1976;143(4):993-8. DOI:10.1084/jem.143.4.993
13. Costa PP, Figueira AS, Bravo FR. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A. 1978;75(9):4499-503. DOI:10.1073/pnas.75.9.4499
14. Cohen DH, Feiner H, Jensson O, Frangione B. Amyloid fibril in hereditary cerebral hemorrhage with amyloidosis (HCHWA) is related to the gastroentero-pancreatic neuroendocrine protein, gamma trace. J Exp Med. 1983;158(2):623-8. DOI:10.1084/jem.158.2.623
15. Nichols WC, Dwulet FE, Liepnieks J, Benson MD. Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. Biochem Biophys Res Commun. 1988;156(2):762-8. DOI:10.1016/s0006-291x(88)80909-4
16. Benson MD, Liepnieks JJ, Yazaki M, et al. A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene. Genomics. 2001;72(3):272-7. DOI:10.1006/geno.2000.6499
17. Benson MD, Liepnieks J, Uemichi T, et al. Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain. Nat Genet. 1993;3(3):252-5. DOI:10.1038/ng0393-252
18. Maury CP, Baumann M. Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): relation of the amyloid protein to variant gelsolin. Biochim Biophys Acta. 1990;1096(1):84-6. DOI:10.1016/0925-4439(90)90016-i
19. Pepys MB, Hawkins PN, Booth DR, et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993;362(6420):553-7. DOI:10.1038/362553a0
20. Gejyo F, Yamada T, Odani S, et al. A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun. 1985;129(3):701-6. DOI:10.1016/0006-291x(85)91948-5
21. Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984;120(3):885-90. DOI:10.1016/s0006-291x(84)80190-4
22. Masters CL, Gajdusek DC, Gibbs CJ Jr. The familial occurrence of Creutzfeldt-Jakob disease and Alzheimer's disease. Brain. 1981;104(3):535-58. DOI:10.1093/brain/104.3.535
23. Levin M, Pras M, Franklin EC. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973;138(2):373-80. DOI:10.1084/jem.138.2.373
24. Husby G, Natvig JB. A serum component related to nonimmunoglobulin amyloid protein AS, a possible precursor of the fibrils. J Clin Invest. 1974;53(4):1054-61. DOI:10.1172/JCI107642
25. Sipe JD, Benson MD, Buxbaum JN, et al. Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. Amyloid. 2016;23(4):209-13. DOI:10.1080/13506129.2016.1257986
26. Picken MM. Proteomics and mass spectrometry in the diagnosis of renal amyloidosis. Clin Kidney J. 2015;8(6):665-72. DOI:10.1093/ckj/sfv087
27. Rameev VV, Kozlovskaya LV, Rameeva AS, et al. The analysis of secondary AA-amyloidosis current etiology and its influence on the approaches for diagnosis and treatment. Terapevticheskii Arkhiv (Ter. Arkh.). 2021;93(6):672-8 (in Russian). DOI:10.26442/00403660.2021.06.200851
28. Rameeva AS, Rameev VV, Bobkova IN, et al. Leading factors of progression in patients with cardiac amyloidosis. Rational Pharmacotherapy in Cardiology. 2022;18(2):143-52 (in Russian). DOI:10.20996/1819-6446-2022-04-02
29. Teilum G. Origin of amyloidosis from PAS-positive reticuloendothelial cells in situ and basic factor in pathogenesis. Amyloidosis. Amsterdam. 1968.
30. Serov VV, Shamov IA. Amiloidoz. Moscow: Meditsina, 1977 (in Russian).
31. Kluve-Beckerman B, Liepnieks JJ, Wang L, Benson MD. A cell culture system for the study of amyloid pathogenesis. Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A. Am J Pathol. 1999;155(1):123-33. DOI:10.1016/S0002-9440(10)65107-3
32. Gomes RA, Franco C, Da Costa G, et al. The proteome response to amyloid protein expression in vivo. PLoS One. 2012;7(11):e50123. DOI:10.1371/journal.pone.0050123
33. Chen B, Retzlaff M, Roos T, Frydman J. Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol. 2011;3(8):a004374. DOI:10.1101/cshperspect.a004374
34. Baskakov IV. Thermodynamics and Protein Folding. Amyloid proteins. The beta-sheet conformation and disiease. Weinheim: WILEY-VCH, 2005.

Авторы

В.В. Рамеев*, Л.В. Лысенко (Козловская)

ФГАОУ ВО «Первый Московский государственный медицинский университет им. И.М. Сеченова» Минздрава России (Сеченовский Университет), Москва, Россия
*vvrameev@mail.ru

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Vilen V. Rameev*, Lidia V. Lysenko (Kozlovskaya)

Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia
*vvrameev@mail.ru

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