Single article

Ilyina L., Kozlov V., Sapozhnikov S.

Reaction of mast cells in murine liver to experimental amyloidosis

Keywords: mice, red grape wine, liver, prevention, mast cells, fructose, experimental amyloidosis

The article examines the reaction of mast cells (MCs) in murine liver to 1) forming an experimental model of amyloidosis by intraperitoneal introducing an aqueous solution of soy cream substitute TS 9199-004-58706213-10 diluted in proportion of 10 g per 100 ml, 15 times, every second day, in the dose of 0.1 ml per 10 g of murine body mass – 1st group; 2) amyloidogenesis correction by spontaneous consumption of dry red wine supplemented by 5% fructose per os – 2nd group. In mice of the 1st group the percent area (Spercent) of amyloid lesions in Congo-stained histological sections made 17,9±0,1%. The capsule and the parenchyma of mast cells contain α-ortho and β-metachromatic non-degranulating forms in an equal ratio. The proportion of b1 metachromatic MC in the capsule of animals’ liver was 1,8 times higher and in the parenchyma it was 1,5 times higher than in intact animals. In mice of the 2nd group Spercent of amyloid deposition in the liver was less than that in mice of the 1st group and made 2,7±0,13%. In the liver capsule of 2nd group mice, half of all MCs had unsulfated heparin and, unlike the same indicator in the intact group, β2-metachromatic and γ-metachromatic MCs appeared. In the liver parenchyma of 2nd group mice, MCs with immature heparin predominated, β3-metachromatic MCs appeared for the first time in a small amount, the proportion of γ-metachromatic MCs increased. Both in the capsule and in the parenchyma of the liver in group 2 mice, degranulated MCs appeared and the proportion of degranulating forms increased. Thus, the response of MCs to amyloidogenesis is expressed in changing the "maturity" degree of mucopolysaccharides contained in them, and in the amount of forms, including degranulating MCs; red grape dry wine supplemented with 5% of fructose can be a factor in amyloid disease prevention.


  1. Artishevskii A.A., Leontyuk A.S., Sluka B.A. Gistologiya s tekhnikoi gistologicheskikh isledovanii [Histology with the technique of histological studies]. Minsk, Vysshaya shkola Publ., 1999, 236 p.
  2. Baglai E.O., Dubikov A.I. Tuchnye kletki – klyuchevye uchastniki patogeneza immunovos-palitel’nykh zabolevanii [Mast cells are key participants in the pathogenesis of immunosuppressant diseases]. Nauchno-prakticheskaya revmatologiya [Scientific and Practical Rheumatology], 2015, vol. 53, no. 2, pp. 182–189. DOI: http:dx. doi. org/10.14412/ 1995-4484-2015-182-189.
  3. Gordon D.S. Tinktorial’nye parallelituchnykh kletok. Makro-mikrostruktura tkanei v norme, patologii i eksperimente [Tinctorial parallels of mast cells. Macro-microstructure of tissues in norm, pathology and experiment]. Cheboksary, Chuvash State University Publ., 1981, pp. 97–101.
  4. Zapadnyuk I.P., Zapadnyuk V.I., Zakhariya E.A., Zapadnyuk B.V. Laboratornye zhivotnye. Razvedenie, soderzhanie, ispol’zovanie v eksperimente. 3-e izd. pererab. I dop [Laboratory animals. Breeding, content, use in the experiment. 3rd]. Kiev, Vysshaya shkola Publ., 1983, 383 p.
  5. Ilyna L.Yu., Efeykina N.B. Sostoyanie populyatsii tuchnykh kletok pochek belykh myshei pri ehksperimental’nom amiloidoze [The state of mast cells population in mice kidneys in experimental amyloidose]. Acta medica Eurasica, 2018, no. 2, pp. 50–60.
  6. Kozlov V.A., Glazyrina 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 Pedagogical University named after I. Yakovlev], 2010, no. 1(65), pp. 40–46.
  7. Kozlov V.A., Glazyrina O.S. Populyatsiya tuchnykh kletok pochki I pochechnoi kapsuly [Population of mast cells of the kidney and renal capsule]. Moscow, 2009, 104 p.
  8. Kozlov V.A., Sapozhnikov S.P., Mitrasov Yu.N., Avruiskaya A.A., Karyshev P.B., Sheptukhina A.I., Nikolaeva O.V. Amiloid I molekulyarnye motory [Amyloid and molecular motors]. Nauka I innovatsii – 2015: materialy X Mezhdunar. nauch. shkoly [Proc. of Int. Sci. School «Science and Innovations – 2015»]. Yoshkar-Ola, 2015, pp. 197–204.
  9. Kozlov V.A., Sapozhnikov S.P., Karyshev P.B., Sheptukhina A.I., Nikolaeva O.V. Model’ sistemnogo amiloidoza u molodykh myshei [Systemic amyloidosis model on young mice]. Byulleten’ eksperimental’noi biologii I meditsiny [Bulletin of Experimental Biology and Medicine], 2016, vol. 162, no. 10, pp. 523–527.
  10. Lindner D.P., Poberin I.A., Rozkin M.Ya., Efimov V.S. Morfometricheskii analiz populyatsii tuchnykh kletok [Morphometric analysis of the population of mast cells]. Patologii [Arch. Pathology], 1980, no. 6, pp. 60–64.
  11. Piruzyan L.А, Leksina L.А. Perekhody ot fiziologicheskikh pokazatelei k patofiziologicheskim naprimere amiloidoza pri periodicheskoj bolezni, insulinnezavisimom sakharnom diabete I bolezni Аl’tsgeimera [Transitions from physiological to pathophysiological indicators on the example of amyloidosis in periodic disease, insulin-independent diabetes and Alzheimer’s disease]. Fiziologiya cheloveka [Human physiology], 2009, vol. 35 (1), pp. 107–120.
  12. Sapozhnikov S.P., Karyshev P.B., Sheptukhina A.I., Nikolaeva O.V., Avruiskaya A.A., Mitrasov Yu.N., Kozlov V.A. Novye flyuorestsentnye zondy dlya vyyavleniya amiloida [New fluorescent probes for the detection of amyloid]. Sovremennye tekhnologii v meditsine [Modern technologies in medicine], 2017, vol. 9, no. 2, pp. 91–98. DOI: 10. 17691/stm2017.9.2.11.
  13. Fufaeva А.I., Kozlov V.А., Sapozhnikov S.P., Petrova YU.V., Аleksandrova V.Yu. Vliyanie krasnogo vinogradnogo vina i ego sochetaniya s geksozami na formirovanie standartnoi modeli amiloidnoi bolezni [The influence of red grape wine and its combination with hexoses on the formation of the standard model of amyloid disease]. Acta medica Eurasica, 2018, no. 1, pp. 42–51.
  14. Sheptukhina A.I., Nikolaeva O.V., Kozlov V.A., Sapozhnikov S.P. Rol’ etanola v formirovanii eksperimental’nogo amiloidoza amiloidoza [The role of ethanol in the formation of experimental amyloidosis]. Nauchnyi fond «Biolog» [Scientific Foundation «Biologist»], 2015, no. 10(14), pp. 47–50.
  15. Yurina N.A., Radostina A.I. Morfofunktsional’naya geterogennost’ I vzaimodeistvie kletok soedinitel’noi tkani [Morphofunctional heterogeneity and interaction of cells of connective tissue]. Moscow, UDN Publ., 1990, 398 p.
  16. Anekonda T.S. Resveratrol – a boon for treating Alzheimer’s disease? Brain Res. Rev., 2006, vol. 52, no. 2, pp. 316–326.
  17. Bartolini M., Andrisano V. Strategies for the Ingibition of Protein Aggregation in Human Diseases. Bio. Chem., 2010, vol. 11, pp. 1–19.
  18. 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. 9, no 3, pp. 316–331.
  19. Cohen A. S., Skinner M. Diseases of the Liver. 6th Philadelphia, 1988, pp. 1093–1108.
  20. Danilewicz M., Wagrowska-Danilewicz M.Quantitative analysis of interstitial mast cells in AA and AL renal amyloidosis. Res. Pract., 2002, vol. 198, no. 6, pp. 413–419.
  21. Gafni J., Merker H.J., Shibolet S., Sohar E., Heller H. On the origin of amyloid. Intern. Med., 1966, vol. 65, pp. 1031–1044.
  22. Gueft B., Chidoni J.J. The site of formation and ultrastructure of amyloid. J. Path., 1963, vol. 43, pp. 837–854.
  23. 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.
  24. Klunk W.E., Pettegrew J.W., Abraham D.J. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. Histochem. Cytochem., 1989, vol. 37, no. 8, pp. 1273–1281.
  25. Kuroiwa M., Aoki K., Izumiyama N. Histologikal study of experimental murine AA amyloidosis. Electron. Microsc. [Tokyo], 2003, vol. 52, no. 4, pp. 407–413.
  26. Marambaud P., Zhao H., Davies P. Resveratrol promotes clearance of Alzheimer’s disease amyloid-beta peptides. Biol. Chem., 2005, vol. 280, no. 45, pp. 37377–37382.
  27. 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. LeukocyteBiology, 1993, vol. 53, pp. 651–657.
  28. 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.
  29. 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.
  30. Shirahama T., Miura K., Ju S.T., Kisilevsky R., Gruys E., Cohen A.S. Amyloid enhancing factor-loaded macrophages in amyloid fibril formation., 1990, vol. 62, no. 1, pp. 61–68.
  31. So M., Hata Y., Naiki H., Goto Y. Heparin-induced amyloid fibrillation of β2‑microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram. Protein Sci., 2017, vol. 26, no. 5, pp. 1024–1036. DOI: 10.1002/pro.3149.
  32. 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.
  33. Tillement J.-P., Lecanu L., Papadopoulos V. Amyloidosis and Neurodegenerative Diseases: Current Treatments and New Pharmacological Options. Pharmacology, 2010, vol. 85, pp. 1–17. DOI: 10.1159/000259044.
  34. Toth T., Toth-Jakatics R., Jimi S., Takebayashi S. Increased density of interstitial mast cells in amyloid A renal amyloidosis. Pathol., 2000, vol. 13, no. 9, pp. 1020–1028.
  35. Westermark P. Mast cells in the islets of Langerhans ininsular  Virchows Arch. A Pathol. Pathol. Anat., 1971, vol. 354, pp. 17–23.

About authors

Kozlov Vadim A.
Doctor of Biological Sciences, Candidate of Medical Sciences, Professor of the Department of Medical Biology with a course in Microbiology and Virology, Chuvash State University, Russia, Cheboksary (; ORCID:
Sapozhnikov Sergey P.
Doctor of Medical Sciences, Head of the Department of Medical Biology with a course in Microbiology and Virology, Chuvash State University, Russia, Cheboksary (; ORCID:
Ilyina Liliya Yu.
Senior Lecturer, Department of Medical Biology with a course in Microbiology and Virology, Chuvash State University, Russia, Cheboksary (; ORCID:

Article link

Ilyina L., Kozlov V., Sapozhnikov S. Reaction of mast cells in murine liver to experimental amyloidosis [Electronic resource] // Acta medica Eurasica. – 2019. – №1. P. 33-43. – URL: