THE COMPARATIVE ANALYSIS OF AMYLOIDOSIS VARIOUS MODELS

Cover Page

Abstract


Considered natural and experimental amyloidosis models in the existing theories context and known amyloidogenesis mechanisms. Available clinical and experimental observations indicate that the opinion of a fatal incurable amyloidosis wrong. It is shown that there is a significant amount of experimental easily replicable amyloidosis models, which may be used for practicing the treatment methods of this pathology. We offer an amyloidosis models classification: natural (animal models with generic amyloidosis), cell clones, artificial (infectious, protein, etc.). Based on the analysis of amyloidosis existing models concluded — none of the accepted in the scientific the theories community for amyloid building does not combine or explains all known facts about the amyloidogenesismechanisms. It is assumed that there is a proteins group, the beta-sheet structure, which are potentially capable of amyloid conformation building. It is assumed that beta-sheets of these proteins have similar amino acid composition. The condition for the amyloid building conformation is getting too much protein in sufficient quantities in an uncharacteristic place where the ionic strength of the tissue fluid is such that it promotes the amyloid building conformation. It is assumed that an unfortunate amount of ionic strength environment amyloid protein is provided by polysaccharides, tubulins proteins and ionized silicon.

 


V. A. Kozlov

I.N. Ul’yanov Chuvash State University, Cheboksary, Russian Federation

Author for correspondence.
Email: pooh12@yandex.ru

Russian Federation доктор биологических наук, кандидат медицинских наук, профессор кафедры фармакологии, клинической фармакологии и биохимии Чувашского государственного университета им. И.Н. Ульянова Адрес: 428015, Чебоксары, Московский пр-т, д. 45, тел.: +7 (8352) 45-26-73

S. P. Sapozhnikov

I.N. Ul’yanov Chuvash State University, Cheboksary, Russian Federation

Email: pooh12@yandex.ru

Russian Federation доктор медицинских наук, заведующий кафедрой медицинской биологии с курсом микробиологии и вирусологии Чувашского государственного университета им. И.Н. Ульянова
Адрес: 428015, Чебоксары, Московский пр-т, д. 45, тел.: +7 (8352) 45-26-73

A. I. Sheptukhina

I.N. Ul’yanov Chuvash State University, Cheboksary, Russian Federation

Email: pooh12@yandex.ru

Russian Federation студентка 5-го курса медицинского факультета Чувашского государственного университета им. И.Н. Ульянова
Адрес: 428015, Чебоксары, Московский проспект, д. 45, тел.: +7 (8352) 45-26-73

A. V. Golenkov

I.N. Ul’yanov Chuvash State University, Cheboksary, Russian Federation

Email: pooh12@yandex.ru

Russian Federation доктор медицинских наук, профессор, заведующий кафедрой психиатрии, медицинской психологии и неврологии Чувашского государственного университета им. И.Н. Ульянова
Адрес: 428015, Чебоксары, Московский пр-т, д. 45, тел.: +7 (8352) 45-26-73

  1. Kozlovskaya L.V., Rameev V.V., Sarkisova I.A. Amyloidosis in the elderly. Klinicheskaya meditsina: Nauchno-prakticheskii zhurnal = Clinical Medicine: Scientific and practical journal. 2005; 83 (6): 12–20.
  2. Chiu K., So K.-F., Chuen-Chung Chang R. Progressive Neurode-generation of Retina in Alzheimer’s disease – Are β-Amyloid Peptide and Tau New Pathological Factors in Glaucoma? Glaucoma. Basic and Clinical Aspects. 2013. Rumelt Sh. (ed.). http://www. intechopen.com/books/glaucoma-basic-and-clinical-aspects/ progressive-neurodegeneration-of-retina-in-alzheimer-s-disease-are-amyloid-peptide-and-tau-new-patho (available: 27.01.2015)
  3. Kitazawa M., Green K.N., Caccamo A., La Ferla F.M. Genetically augmenting Abeta42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice. Am. J. Pathol. 2006; 168 (6): 1986–1997.
  4. Vattemi G., Nogalska A., King Engel W., D’Agostino C., Checler F., Askanas V. Amyloid-beta 42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol. 2009; 117 (5): 569–574.
  5. Gomperts S.N., Rentz D.M., Moran E., Becker J.A., Locascio J.J., Klunk W.E., Mathis C.A., Elmaleh D.R., Shoup T., Fischman A.J., Hyman B.T., Growdon J.H., Johnson K.A. Imaging amyloid deposition in Lewy body diseases. Neurology. 2008; 71 (12): 903–910.
  6. Irvine G.B., El-Agnaf O.M., Shankar G.M., Walsh D.M. Protein aggregation in the brain: the molecular basis for Alzheimer’s and Parkinson’s diseases. Mol. Med. 200 8; 14: 451–464.
  7. Head E., Lott I.T. Down syndrome and beta-amyloid deposition. Curr. Opin. Neurol. 2004; 17 (2): 95–100.
  8. Luheshi L.V., Dobson C.M. Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett. 2009; 583: 2581–2586.
  9. Nakazato M., Matsukura S. New Type of Amyloidosis b) Islet Amyloid Polypeptide (IAPP/Amylin) in Non-Insulin-Dependent Diabetes Mellitus. Internal Medicine. 1993; 32 (12): 928–929.
  10. Gendlin G.E. Renal amyloidosis. Lechashchii vrach = Attending physician. 2000; 2: 8–10.
  11. Brin V.B., Gabueva A.A., Kozyrev K.M. Effect of succinic acid and sulphide mineral water "Redant-4" separately and in combination on the functional-structural condition of the kidneys in the simulation of generalized amyloidosis neuropathic type. Kubanskii nauchnyi meditsinskii vestnik = Kuban research medical bulletin. 2010; 7 (121): 33–37.
  12. Kisieva Z.A., Brin V.B., Kozyrev K.M. Influence mildronata and Acyzol on the basic processes of urine formation and excretion of electrolytes in Syrian golden hamsters with experimental model of amyloid nephropathy. Sovremennye problemy nauki i obrazovaniya = Modern problems of science and education. 2014; (2): 9. Available at: http://www.science-education.ru/pdf/2014/2/656.pdf (accessed: 27.01.2015).
  13. Sjakste N., Baumane L., Boucher J.L., Dzintare M.,Meirena D., SjaksteJ., LauberteL., Kalvinsh I. Effects of gamma-butyrobetaine and mildronate on oxide production in lipopolysaccaride-treated rats. Basic Clin. Pharmacol. Toxicol. 2004; 94 (1): 46–50.
  14. Forloni G., Angeretti N., Smiroldo S. Neuroprotective activity of acetyl-L-carnitine: studies in vitro. J. Neurosci. Res. 1994; 37 (1): 92–96.
  15. Jang M.H., Piao X.L, Kim H.Y., Cho E.J., Baek S.H., Kwon S.W., Park J.H. Resveratrol oligomers from Vitisamurensis attenuate beta-amyloid-induced oxidative stress in PC12 cells. Biol. Pharm. Bull. 2007; 30: 1130–1134.
  16. Savaskan E., Olivieri G., Meier F., Seifritz E., Wirz-Justice A., Muller-Spahn F. Red wine ingredient resveratrol protects from beta-amyloid neurotoxicity. Gerontology. 2003; 49: 380–383.
  17. Kozlov V.A., Golenkov A.V., Sapozhnikov S.P. Effects of dry red wine and other alcoholic beverages on the development and course of Alzheimer's disease: the obvious, questionable and unknown. Psikhicheskoe zdorov'e = Mental health. 2014; 6 (97): C. 81–88.
  18. Baza znanii po biologii cheloveka (Knowledge Base of Human Biology). Available at: http://humbio.ru/humbio/immunology/x003ee6f.htm (accessed: 27.01.2015).
  19. Alam S., Suzuki H., Tsukahara T. Alternative splicing regulation of APP exon 7 by RBFox proteins. Neurochem. Int. 2014; pii: S0197-0186(14)00184-3. doi: 10.1016/j.neuint.2014.08.001.
  20. Goate A., Chartier-Harlin M.C., Mullan M., Brown G., Crawford F., Fidani L., Giuffra L., Haynes A., Irving N., James L., Mant R., Newton P., Rooke K., Rogues P., Talbot C., Pericak-Vance M., Roses A., Williamson R., Rossor M., Owen M., Hardy J. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer’s disease. Nature. 1991; 349: 704–706.
  21. Tanzi R., Gusella J., Watkins P., Bruns G.A., St George-Hyslop P., Van Keuren M.L., Patterson D., Pagan S., Kurnit D.M., Neve R.L. Amyloid beta-protein gene: cDNA, mRNA distribution and genetic linkage near the Alzheimer locus. Science. 1987; 235: 880–884.
  22. Ando Y., Nakamura M., Araki S. Transthyretin-related family-alamyloidotic polyneuropathy. Arch. Neurol.2005; 62: 1057–1062.
  23. Zhang C., Khandelwal P.J., Chakraborty R., Cuellar T.L., Sarangi S., Patel S.A., Cosentino C.P., O’Connor M., Lee J.C.,Tanzi R.E., Saunders A.J. An AICD-based functional screen to identify APP metabolism regulators. Mol. Neurodegener. 2007; 2 (15): 19 p. (page number not for citation purposes). doi: 10.1186/1750-1326-2-15.
  24. Lewis J., Dickson D.W., Lin Wen-Lang, Chisholm L., Corral A., Jones G., Yen Shu-Hui, Sahara N., Skipper L., Yager D., Eckman C., Hardy J., Hutton M., McGowan E. Enhanced Neurofibrillary Degeneration in Transgenic Mice Expressing Mutant Tau and APP. Science. 2001; 5534: 1487–1491.
  25. Allen K.D., Chernova T.A., Tennant E.P., Wilkinson K.D., Chernoff Y.O. Effects of the ubiquitin system alterations on the de novo formation and loss of a yeast prion. J. Biol. Chem. 2007; 282: 3004–3013.
  26. Bailleul P.A., Newnam G.P., Steenbergen J.N., Chernoff Y.O. Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics. 1999; 153: 81–94.
  27. Ganusova E.E., Ozolins L.N., Bhagat S., Newnam G.P., Wegrzyn R.D., Sherman M.Y., Chernoff Y.O. Modulation of prion formation, aggregation and toxicity by the actin cytoskeleton in yeast. Mol. Cell. Biol. 2006; 26: 617–629.
  28. Strittmatter W., Saunders A., Schmechel D., Pericak-Vance M., Enghild J., Salvesen G., Roses A. Apolipoprotein E: High avidity binding to b-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc. Natl. Acad. Sci. 1993; 90: 1977–1981.
  29. Chernoff Y.O. Protein heredity and evolution. In: Charles Darwin and Modern Biology: The Intern. Sci. Conference. E`.I. Kolchinskii`, A.A. Fedotova (eds). St. Petersburg: Nestor-Istoriia. 2010; 76–94.
  30. Rivas A.L., Tintle L., Meyers-Wallen V., Scarlett J.M.,Van Tassell C., Quimby F.W. Inheritance of renal amyloidosis in Chi-nese Shar Pei dogs. J. Hered. 1993; 84 (6): 438–442.
  31. Vidt J. SPAID — Shar-Pei Autoinflammatory Disorder [Элек-тронный ресурс]. http://drjwv.com/wp/2014/03/20/spaid-sharpei-autoinflammatory-disorder/ свободный (дата обращения: 27.01.2015).
  32. Olsson M., Meadows J.R., Truvé K., Rosengren Pielberg G., Puppo F., Mauceli E., Quilez J., Tonomura N., Zanna G., Docampo M.J., Bassols A., Avery A.C., Karlsson E.K., Thomas A., Kastner D.L., Bongcam-Rudloff E., Webster M.T., Sanchez A., Hedhammar A., Remmers E.F., Andersson L., Ferrer L., Tintle L., Lindblad-Toh K. A novel unstable duplication upstream of HAS2 predisposes to a breed-defining skin phenotype and a periodicfever syndrome in Chinese Shar-Pei dogs. PLoS Genet. 2011; 7 (3): 1001332. DOI: 10.1371
  33. Bowles M.H., Mosier D.A. Renal amyloidosis in a family of beagles. J. Am. Vet. Med. Assoc. 1992; 201 (4). P. 569–574.
  34. Naumenko E.S. Spontannyi amiloidoz u nizshikh obez'yan: (patologicheskaya anatomiya, nekotorye voprosy patogeneza). Avtoref. dis. … kand. biol. nauk [Spontaneous Amyloidosis in the Lower Monkeys (Pathological Anatomy, some Questions of Pathogenesis). Author’s abstract]. Stavropol, 2004. 24 p.
  35. Podlisny M.B., Tolan D.R., Selkoe D.J. Homology of the amyloid beta protein precursor in monkey and human supports a primate model for beta amyloidosis in Alzheimer’s disease. Am. J. Pathol. 1991; 138 (6): 1423–1435.
  36. OakleyH., Cole S.L.,LoganS., Maus E., Shao P., CraftJ.,Guillozet-Bongaarts A., Ohno M., DisterhoftJ., Van EldikL., Berry R.,Vassar R. Intraneuronal beta-amyloidaggregates, neurodegeneration, and neuron loss in transgenic micewith the familial Alzheimer’s disease mutations: potential factors inamyloid plaque formation. J. Neuro-sci. 2006; 26 (40): 10129–10140.
  37. Chew D.J., DiBartola S.P., Boyce J.T., GasperP.W. Renal amyloidosis in related Abyssinian cats. J. Am. Vet. Med. Assoc. 982; 181: 139–142.
  38. Niewold T.A., van der Linde-Sipman J.S., Murphy C., TootenP.C., Gruys E. Familial amyloidosis in cats: Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition. Amyloid. 1999; 6 (3): 205–209.
  39. Littman M.P. Protein-losing Nephropathy in Small Animals. Vet. Clin. Small Anim. 2011; 41: 31–62. doi: 10.1016/j.cvsm.2010.09.006
  40. Multhaup G., Schlicksupp A., Hesse L. The amyloidprecursor protein of Alzheimer`s disease in the reduction ofcopper (II) to copper (I). Science. 1996; 271: 1406–1409.
  41. Xia W., Zhang J., Rezer R., Koo E. H., Selkoe D.J. Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease. Proc. Natl. Acad. Sci. USA. 1997; 94 (15): 8208–8213.
  42. Zhong Z., Hieaki J., Murakami K., Wang Y., Catalano R., Quon D., Cordell B. Secretion of beta-amyloid precursor protein involves multiple cleavage sites. J. Biol. Chem. 1994; 269: 627–632.
  43. Qverfurth H.W., Jiang J., Geiger J.P. Caffeine stimulates amyloid beta-peptide release from beta-amyloid precursor protein-trans-fected HEK293 cells. J. Neurochem. 1997; 69 (4): 1580–1591.
  44. Kapinus L.N. Immunomorphological study of the early stages of amyloidogenesis. Bull. Exp. Biol. Med.(Russia). 1978; 85 (2): 232–234.
  45. Domagk G. Untersuchungenuber die Bedeutung des reticuloendothelial systems fur die Entstehung d. Amyloids, Virchows Archiv. B. CCLIII. 1924; 253: 594–638.
  46. Cui D., Kawano H., Takahashi M. Hoshii Y., Setoguchi M., Gon-do T., Ishihara T. Acceleration of murine AA amyloidosis by oral administration of amyloid fibrils extracted from different species. Pathol. Int. 2002; 52 (1): 40–45.
  47. Kennedy J.S., Anderson J.D. The effect of treatment of the associated disease on the development of amyloidosis in the experimental animal. J. Pathol. 1983; 141 (1): 11–15.
  48. ГGritsman A.Yu. Nekotorye voprosy eksperimental'noi terapii amiloidoza i rezorbtsii amiloida. Avtoref. dis. ... kand. med. nauk [Some Questions Experimental Therapeutics Amyloidosis and Amyloid Resorption. Author’s abstract]. Moscow, 1974. 24 p.
  49. Zaalishvili T.V., Kozy`rev K.M. Methods simulation of amyloidosis in experimental animals. Adv. Curr. Nat. Sci. (Russia). 2005; 2: 78–79.
  50. Pat. 2269825 Russian Federation (51) IPC G09B23/28 the Way of modeling of experimental amyloidosis in animals. Zaalishvili T.V., Kozyrev K.M. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2004127649/14, Appl. 15.09.2004; Publ. 10.02.2006. Bull. № 11. 7 p.
  51. Kravkov N.P. Ob amiloide, eksperimental'no vyzyvaemom u zhivotnykh. Dis. … dokt. med. nauk [On Amyloid Experimentally Causes in Animals. Author’s abstract]. St. Petersburg, 1894. 46 p.
  52. Pat. 2373581 Russian Federation (51) IPC G09B23/28 Method modeling of experimental amyloidosis in animals. Gabueva A.A., Kozyrev K.M., Brin V.B. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2008128201/14, Appl. 10.07.2008; Publ. 20.11.2009. Bull. № 32. 8 p.
  53. Sokolovskiy N.V. Functionally and morphological characteristics of the experimental prophilactic of cardiac amyloidosis rats acizol and succinic acid. Modern Probl. Sci Ed. 2014; 1: 19. http://www. science-education.ru/pdf/2014/1/450.pdf (available: 27.01.2015).
  54. Pat. 2347279 Russian Federation (51) IPC G09B23/28 the Way of modeling of experimental amyloidosis in animals. Puhova I.U., Brin V.B., Kozyrev C.M. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2007135901/14, Appl. 27.09.2007; Publ. 20.02.2009. Bull. № 6. 7 p.
  55. Pat. 2473133 Russian Federation (51) IPC G09B 23/28; A61K 31/502; A61P 13/12 Method of prevention of systemic amyloidosis and its renal forms in experimental animals. Brin V.B., Belikova A.T., Kozyrev K.M. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2011112243/14, Appl. 30.03.2011; Publ. 20.01.2013. Bull. № 2. 10 p.
  56. Pat. 2270672 Russian Federation (51) IPC A61K 31/15; A61P 13/12 Method of prevention and treatment of systemic amyloidosis and its renal forms in experimental animals. Zaalishvili T.V., Kozyrev K.M. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2004127648/14, Appl. 15.09.2004; Publ. 27.02.2006. Bull. № 6. 7 p.
  57. Pat. 2306617 Russian Federation (51) МПКG09B23/28 the Way of modeling of experimental amyloidosis in animals. Kozyrev K.M., Zaalishvili T.V., Brin V.B., Gioeva Z.V. applicants and patent holder of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2006113109/13, Appl. 18.04.2006; Publ. 20.09.2007. Bull. № 36. 8 p.
  58. Pat. 2446482 Russian Federation (51) IPC G09В23/28 the Way of modeling of experimental amyloidosis in animals. Brin V.B., Belikova A.T., Kozyrev K.M. applicants and patent owner of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2010146365/14, Appl. 13.11.2010; Publ. 27.03.2012. Bull. № 9. 9 p.
  59. Pat. 2473134 Russian Federation (51) IPC G09В23/28 Method of prevention of systemic amyloidosis and its renal forms in experimental animals. Belikova A.T., Brin V.B., Kozyrev K.M. applicants and patent owner of the State Educational Institution of Higher Professional Education North-Ossetian State Medical Academy of the Federal Agency for Healthcare and Social Development of the Russian Federation. No. 2011111891/14, Appl. 29.03.2011; Publ. 20.01.2013. Bull. № 2. 9 p.
  60. Akamatsu Y., Ikegami R. Induction of hepatoma and systemic amyloidosis in mice by 4-(dimethylamino) azobenzene feeding. Gann. 1968; 59 (3): 201–206.
  61. Shvarts S.S. Ekologicheskie zakonomernosti evolyutsii [Environmental Laws of Evolution]. Moscow, Nauka, 1980. 153 p.
  62. Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003; 81: 678–699.
  63. Sapozhnikov S. P. Role of silicon compounds in the development of autoimmune processes. Trace Elements in Medicine (Russia). 2013; 3: 3–13.
  64. Lansbury P.T., Jr., Caughey B. The chemistry of scrapie infection: implications of the ‘ice 9′ metaphor. Chemistry & Biology. 1995; 2: 1–5.
  65. Kim J.I., Cali I., Surewicz K., Kong Q., Raymond G.J., Atarashi R., Race B., Qing L., Gambetti P., Caughey B., Surewicz W.K. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J. Biol. Chem. 2010; 285: 14083–14087.
  66. Wang F., Wang X., Yuan C.G., Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science. 2010; 327: 1132–1135.
  67. Teilum G. Studies on pathogeneiss of amyloidosis; effect of nitrogen mustard in inducing amyloidosis. J. Lab. Clin. Med. 1954; 43: 367.
  68. Letterer E. Studienuber Art und Enstehung des Amyloids. Beitr. Path. Anat. 1926; 75: 486–588.
  69. Loeschke H. Vorstellungenuber das Wesen von Hyalin und amlyoid auf Grund von serologische. Versuchen. Beitr. path. Anat. 1927; 77: 231–239.
  70. Cagli V. La amiloidosi. Policlinico. Sez. prat. 1961; 68 (49): 1801– 1814.

Views

Abstract - 54

PDF (Russian) - 7

Cited-By


PlumX

Dimensions



Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies