References

1. Belikova A.T., Grin V.B., Kozyrev K.M. Funktsional‘no–morfologicheskaya kharakteristika eksperimental‘nogo generalizovannogo amiloidoza nefropaticheskogo tipa [Functional-morphological characteristics of experimental generalized amyloidosis nefrophathia type]. Vestnik novykh meditsinskikh tekhnologii [Bulletin of new medical technologies], 2011, vol. 18(2), pp. 132–133.
2. Berezhnaya N.M., Sepiashvili R.I. Tuchnye kletki i gistamin: fiziologicheskaya rol’ [Mast cells and histamine: physiological role]. Allergologiya i immunologiya [Allergology & Immunology], 2003, vol. 4(4), pp. 29–38.
3. Vasil’ev V.I., Gorodetskii V.R., Radenska-Lopovok S.G., Probatova N.A., Pavlovskaya A.I., Varlamova E.Yu., Sedyshev S.Kh., Logvinenko O.A., Rodionova E.B., Korsakova Yu.O., Gaiduk I.V., Nasonov E.L. Novye pokhody k opredeleniyu organnykh porazhenii pri AL–amiloidoze [New approaches to determining organ damage in AL–amyloidosis]. Nauchno-prakticheskaya revmatologiya [Research and Practice Rheumatology], 2012, vol. 50(1), pp. 83–90.
4. Vermel’ A.E. Amiloidoz: klassifikatsiya, klinicheskaya kharakteristika. Diagnostika i lechenie, [Amyloidosis: classification, clinical characteristics. Diagnosis and treatment]. Klinicheskaya meditsina. [Clinical medicine], 1997, no. 7, pp. 12–17.
5. Galstyan G.R. Vliyanie amilina na funktsiyu V-kletok i regulyatsiyu uglevodnogo obmena [Amelin influence on the function of cells and the regulation of carbohydrate metabolism] Sakharnyi diabet. [Diabetes], 2008, vol. 41(4), pp. 24–25.
6. Gusel’nikova V.V., Pronina A.P., Nazarov P.G., Polevshchikov A.V. Proiskhozhdenie tuchnykh kletok: sovremennoe sostoyanie problemy [The origin of fat cells: modern state of problem] Voprosy morfologii XXI veka: sb. nauch. tr. [Аspects of morphology of the XXI century. Collection of scientific papers]. St. Petersburg, Dean Publ., 2010, issue 2, pp. 108–115.
7. Zakharova E.V. Sistemnyi amiloidoz, diagnoz, differentsial’nyi diagnoz, lechenie [Systemic amyloidosis, diagnosis, differential diagnosis, and treatment]. Lechashchii vrach [Treating doctor], 2004, no. 3. Aviailable at: http://www.lvrach.ru/2004/03/4531161.
8. Ivkova A.N., Gendlin G.E., Nikitin I.G., Pruzhskovskaya M.P. Sistemnyi pervichnyi (idiopaticheskii) amiloidoz [System primary (idiopathic) amyloidosis]. Rossiiskii Meditsinskii Zhurnal [Russian medical journal], 2007, no. 2, pp. 47–49.
9. Kvetnoi I.M., Kvetnaya T.V., Ryadnova I.Yu., Fursov B.B., Ernandes-Yago X., Blesa X.R. Ekspressiya p-amiloida i tau-proteina v tuchnykh kletkakh pri bolezni Al’tsgeimera [The expression of p-amyloid and Tau-protein in fat cells in Alzheimer’s disease]. Arkhiv patologii [Аrchives of pathology], 2003, vol. 65(1), pp. 36–39.
10. Kozlov V.A., Busova O.S. Migratsiya tuchnykh kletok v pochke [Migration of mast cells in the kidney]. Vestnik Chuvashskogo gosudarstvennogo pedagogicheskogo universiteta im. I.Ya. Yakovleva [Bulletin of the Chuvash state University named I. N. Ulyanov], 2010, no. 1, pp. 40–45.
11. Kozlov V.A., Busova O.S. Tuchnokletochnaya populyatsiya pochki i pochechnoi kapsuly [Mast cells population of the kidney and renal capsule]. Moscow, 2009, 104 p.
12. Kozlov V.A., Glazyrina O.S. Vliyanie vodnoi nagruzki i khronicheskogo izbytka medi i tsinka 10PDK na neirotransmitternyi status i populyatsiyu tuchnykh kletok kap-suly pochki [Effect of water stress and chronic excess copper and zinc 10 MPC on neurotransmitter status and population of mast cells capsule of the kidney]. Mikroelementy v meditsine [Тrace elements in medicine], 2008, vol. 9(3-4), pp. 49–56.
13. Kozlov V.A., Glazyrina O.S., Tolmacheva A.Yu. Vodnaya deprivatsiya vliyaet na ekstraneironal’nyi mediatornyi pul pochek belykh krys i pochechnuyu populyatsiyu tuchnykh kletok [Water deprivation affects extraneuronal mediator pool of the kidneys of white rats and the renal population of mast cells]. Nefrologiya [Nephrology], 2003, vol. 7(2), pp. 76–81.
14. Kozlov V.A., Sapozhnikov S.P., Sheptukhina A.I., Golenkov A.V. Sravnitel’nyi analiz razlichnykh modelei amiloidoza [Comparative analysis of different models of amyloidosis]. Vestnik Rossiiskoi akademii meditsinskikh nauk [Herald of the Russian Academy of Medical Sciences], 2015, no. 1, pp. 5–11.
15. Kondashevskaya M.V. Tuchnye kletki i geparin – klyuchevye zven’ya v adaptivnykh i patologicheskikh protsessakh [Mast cells and heparin – key links in adaptive and pathological processes]. Vestnik Rossiiskoi akademii meditcinskikh nauk [Herald of the Russian Academy of Medical Sciences], 2010, no. 6, pp. 49–54.
16. Murav’ev Yu.V., Alekseeva A.V., Radenska-Lopovok S.G. AA-amiloidoz pri bolezni Stilla, razvivsheisya u vzroslykh [AA-amyloidosis with Still disease developed in adults]. Nauchno-prakticheskaya revmatologiya [Research and Practice Rheumatology], 2011, no. 3, pp. 95–98.
17. Piruzyan L.A, Leksina L.A. Perekhody ot fiziologicheskikh pokazatelei k patofiziologicheskim na primere amiloidoza pri periodicheskoi bolezni, insulinne-zavisimom sakharnom diabete i bolezni Al’tsgeimera [The transitions from physiological to pathophysiological indicators on the example of amyloidosis in periodic disease, non-insulin dependent diabetes mellitus and Alzheimer’s disease]. Fiziologiya cheloveka [Нuman physiology], 2009, vol. 35(1), pp. 107–120.
18. Uspenskaya O., Zakharov V. Patogeneticheskie i neirokhimicheskie osnovy razvitiya bolezni Al’tsgeimera [Pathogenetic and neurochemical bases of development of Alzheimer’s disease]. Vrach [Doctor], 2010, no. 4, pp. 72–74.
19. Shishkin A.N. Amiloidoz [Amyloidoz]. Vrachebnye vedomosti [Medical statements], 2001, vol. 4(18), pp. 33–44.
20. Baglay E.O., Dubikov A.I. Mast cells are key participants in the pathogenesis of immunoinflammatory diseases. Rheumatology Science and Practice, 2015, vol. 53, no. 2, pp. 182–189.
21. Baumruker T., Prische E. Mast cell and their activation – from the molecular mechanisms to clinical relevance. Asp. Immunobiol., 2001. vol. 1, no. 6. pp. 259–263.
22. Beer D.J.,Rocklin R.E. Histamine modulation of lymphocyte biology: membrane receptors, signal transduction, and functions. Crit Rev. Immunol., 1987, vol. 7, no. 1, pp. 55–91.
23. Bohle A., Wehrmann M., Eissele R., von Gise H., Mackensen-Haen S., Muller C. The long-term prognosis of AA and AL renal amyloidosis and the pathogenesis of chronic renal failure in renal amyloidosis. Res. Pract., 1993, vol. 189, no. 3, pp. 316–331.
24. Caughey G.H. New developments in the genetics and activation of mast cell proteases. Immunol., 2002, vol. 38, pp. 1353–1357.
25. Church M.K., Levi-Schaffer F. The human mast cell. Updates on cells and cytokines. Allergy Clin. Immunol., 1997, vol. 99, pp. 155–160.
26. Eklund K.K., Niemi R., Kovanen P.T. Immune functions of serum amyloid A. Rev. Immunol., 2012, vol. 32, no. 4, pp. 335–348.
27. Gafni J., Merker H.J., Shibolet S., Sohar E., Heller H. On the origin of amyloid. Intern. Med., 1966, vol. 65, pp. 1031–1044.
28. Galli S.J. New concepts about the mast cell. Engl. J. Med., 1993, vol. 328, no. 4. pp. 257–265.
29. Gerz M.A., Kyle R.A. Secondary systemic amyloidosis response and survival in 64 patients. Medicine (Baltimore), 1991, 70, pp. 246–256.
30. Gillmore J.D., Lovat L., Persey M.R., Pepys M.B., Hawkins P.N. Amyloid load and clinical outcome in AA amyloidosis in relation to circulation of serum amyloid protein. Lancet, 2001, 358, pp. 24–29.
31. Gritsman AIu. Effect of histamine and diprazin on the course of experimental amyloidosis in mice. Patol., 1975, vol. 37, no. 7. pp. 50–56.
32. Gruys E., Timmermans H.J.F., van Ederen A.-M. Deposition of amyloid in the liver of hamsters: an enzyme – histochemical and electron-microscopical study. Laboratory Animals, 1979, 13, pp. 1–9.
33. Gueft B., Chidoni J.J. The site of formation and ultrastructure of amyloid. J. Path., 1963, vol. 43, pp. 837–854.
34. Harcha P.A., Vargas A., Yi C., Koulakoff A.A., Giaume C., Saez J.C. Hemichannels Are Required for Amyloid β –Peptide-Induced Degranulation and Are Activated in Brain Mast Cells of APPswe/PS1dE9 Mice. Neurosci., 2015, vol. 35, no 25, pp. 9526–9538. doi: 10.1523/JNEUROSCI. 3686-14.2015.
35. Irani A.M., Schechter N.M., Craig S.S., DeBlois G., Schwart L.B. Two types of human mast cells that have distinct neutral protease compositions. Natl. Acad. Sci. USA, 1986, vol. 83, pp. 4464–4468.
36. Kozlov V.A., Glazirina O.S. Influence of copper and molybdenum on kidney capsules mast cells population. In: Macro and Trace Elements 22. Workshop 2004. 2004. pp. 1128–1133.
37. Kozlov V.A., Glazirina O.S., Kuzmina O.V., Suslikov V.L. Choline and l-dopa influence on biogenic regulators kidney level and kidney mastocytes behavior. In: Macro and Trace Elements 21. Workshop 2002. 2002. pp. 846–855.
38. Kozlov V.A., Glazirina O.S., Kuzmina O.V., Suslikov V.L. Water diures and choline influence on biogenic regulators kidneys level and kidney mastocytes behavior in acute exparement. In: Macro and Trace Elements 21. Workshop 2002. 2002. pp. 831–838.
39. Kuroiwa M., Aoki K., Izumiyama N. Histologikal study of experimental murine AA amyloidosis. Electron. Microsc. (Tokyo), 2003, vol. 52, no. 4. pp. 407–413.
40. Melmon K.L., Rocklin R.E., Rosenkranz R.P. Autacoids as modulators of the inflammatory and immune response. J. Med.,1981, vol. 71, no. 1, pp. 100–106.
41. Merluzzi S., Frossi D., Gri G., Parusso S., Tripodo C., Pucillo C. Mast cells enhance proliferation of B-lymphocytes and drive their differentiation toward Ig A secreting plasma cells. Blood., 2010, vol. 115. pp. 2810–2817. DOI: 10.1182/ blood – 2009-10-250126.
42. Mlac M., Melato M., Marin G. Mast cellsin the islets of Langerhans. A study of their behaviour in connection with diabetes and with insular  Virchows Arch. a Pathol. Ana. Histol., 1975, vol. 365, no. 3, pp. 213–220.
43. Nelson R.B., Siman R., Iqbal M.A., Potter H. Identification of a chymotrypsin-like mast cell protease in rat brain capable of generating the N-terminus of the Alzheimer amyloid beta-protein. Neurochem., 1993, vol. 61, no. 2, pp. 567–577.
44. Niederhoffer N., Levy R., Sick E., Andre P., Coupin G., Lombard Y., Gies J.P. Amyloidbeta peptides trigger CD47-dependent mast cell secretory and phagocytic responses. J. Immunopathol. Pharmacol., 2009, vol. 22, no. 2, pp. 473–483.
45. Niemi К. Baumann, Kovanen P.T., Eklund K., Eklund K.K. Serum amyloid A (SAA) activates human mast cells which leads into degradation of SAA and generation of an amyloidogenic SAA fragment. Biochemica et Biophysica Acta, 2006, vol. 1762, pp. 424–430.
46. Okayama J., Kawakami T. Development, migration and survival of mast cells. Immunol Res., 2006, 34, pp. 97–115. doi: 10.1385 / IR : 34:2:97.
47. Olsson N., Siegbahn A., Nilsson G. Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway. Biophys. Res. Commun., 1999, vol.254, no. 1. pp. 143–146.
48. Preciado-Patt L., Herskoviz R., Fridkin M., Lider O. Serum amyloid A binds specific extracellular matrix glycoproteins and induces the adhesion of resting CD4+ T cells. Immunol., 1996, vol. 156, pp. 1189–1195.
49. Reid C., Hebert L., Pozullo G., Gervais F. Splenic macrophage activation and functions in amyloid enhancing factor – induced secondary amyloidosis. Study of phagocytosis, killing, respiratory burst and MHC class II surface expression. Leukocyte Biology, 1993, vol. 53, pp. 651–657.
50. Rocken C., Shakespeare A. Pathology, diagnosis and pathogenesis of AA amyloidosis. Virchows Arch., 2002, vol. 440, no. 2, pp. 111–122.
51. Rodney H., Falk M.D., Raymond L., Comenzo M.D., Martha Skinner M.D. The Systemic Amyloidoses. The New England Journal of Medicine, 1997, vol. 337, no. 13, pp. 898–909.
52. Rodrigues L., Neves M., Sa H., Campos M. Clinical challenges of an oligosecretory plasma cell dyscrasia. BMJ Case Rep., 2013, Feb. 18. doi: 10.1136/bcr-2012-008169.
53. Rokita H., Shirahama T., Cohen A.S., Meck R.L., Benditt E.P., Sipe J.D. Differetial expression of the amyloid SAA 3 gene in the liver and peritoneal macrophages of mice undergoing dissimilar inflammatory episodes. Immunol., 1987, vol. 139, no. 11, pp. 3849–3853.
54. Shibolet S., Merker H.J., Sohar E., Gafni J., Heller H. Cellular proliferation during the development of amyloid – Electron microscopic observation on the kidneys of Leishmania-infected hamster. J. Exp. Path., 1967, vol. 48, pp. 244–249.
55. Shirahama T., Miura K., Ju S.T., Kisilevsky R., Gruys E., Cohen A.S. Amyloid enhancing factor-loaded macrophages in amyloid fibril formation. Lab Invest., 1990, vol. 62, no. 1, pp. 61–68.
56. Sipe J.D., Benson M.D., Buxbaum J.N., Ikeda S., Merlini G., Saraiva M.J.,Westermark P. Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committree of the International Society of amyloidosis. Amyloid., 2012, vol. 19, pp. 167–170.
57. Sipe J.D., Benson M.D., Buxbaum J.N., Ikeda S., Merlini G., Saraiva M.J.,Westermark P. Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid., 2014, vol. 21, no. 4, pp. 221–224. doi: 10.3109/13506129.2014.964858.
58. Skinner M. Protein AA/SAA. Intern. Med., 1992, vol. 232, pp. 513–514.
59. Steel D.M., Whitehead A.S. The major acute phase reactants: C-reactive protein, serum amyloid P component, and serum amyloid A protein.Immunol Today, 1994, 15, pp. 81–88.
60. Stone M.J. Amyloidosis: a final common pathway for protein deposition in tissues. Blood.,1990,  75, pp. 531–545.
61. Tao Du, Ali-Khan Z. Pathogenesis of secondary amyloidosis in an alveolar hydatid cyst-mouse model: histopathology and immuno/enzyme-histohemical analysis of splenic marginal zone cells during amyloidogenesis. Exp. Path., 1990, vol. 71, pp. 313–335.
62. Toth T., Toth-Jakatics R., Jimi S., Takebayashi S. Increased density of interstitial mast cells in amyloid A renal amyloidosis. Modern Pathol., 2000, vol. 13, pp. 1020–1028.
63. Westermark P. Mast cells in the islets of Langerhans ininsular  Virchows Arch. A Pathol. Pathol. Anat., 1971, vol. 354, pp. 17–23.
64. Zhu J., Paul W.E. Heterogeneity and plasticity of T-helper cells. Cell Res., 2010, vol. 20, pp. 4-12. doi: 10.1038/cr.2009.138.
65. Zucker-Franklin D., Franklin E.C. Intracellular Localizacion of Human Amyloid by Fluorescence and Electron Microscopy. J. of Pathology, 1970, vol. 59, no. 1, pp. 23–41.