Current methods of diagnosis and monitoring of a systemic amyloidosis course


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Aim. To determine clinical significance of measuring blood levels of protein precursors of AA- and AL-amyloidosis - SAA and immunoglobulin free light chains (ILC), respectively.
Material and methods. SAA concentrations were studied with ELISA in 43 rheumatoid arthritis (RA) patients including complicated with reactive AA-amyloidosis (n = 31). Inflammation activity and its severity were studied (indices Li, richi, HAQ, DAS4). A modern quantitative nephelometric method Freelite estimated ILC levels in 31 patients with AL-amyloidosis.
Results. Patients with RA complicated with AA-amyloidosis and free of it had a strong correlation between blood serum SAA concentration and activity of joint disease. Elevated SAA concentrations to 160 mg/l (normal 10 mg/l) were detected in many patients with clinical remission of the joint syndrome. Significal inhibition of AA-amyloidosis progression was seen only in SAA concentration drop under 60 mg/l. For AL-amyloidosis patients ILC fall by less than 3 normal value means a 6-time increase in chances of a favourable outcome.
Conclusion. Monitoring of blood levels of proteins precursors of AA- and AL-amyloidosis is a key factor in prognosis of the disease and treatment efficacy.

About the authors

Vilen Vilevich Rameev

Email: vvrameev@mtu-net.ru

Lidiya Vladimirovna Kozlovskaya

Elena Aleksandrovna Malinina

Email: knvpb@mma.ru

Anna Grigor'evna Serova

Ivetta Nikolaevna Kogarko

Bronislav Stanislavovich Kogarko

Nina Vasil'evna Lyubimova

V V Rameev

I.M. Sechenov First Moscow State Medical University

I.M. Sechenov First Moscow State Medical University

L V Kozlovskaya

I.M. Sechenov First Moscow State Medical University

I.M. Sechenov First Moscow State Medical University

E A Malinina

I.M. Sechenov First Moscow State Medical University

I.M. Sechenov First Moscow State Medical University

A G Serova

I.M. Sechenov First Moscow State Medical University

I.M. Sechenov First Moscow State Medical University

I N Kogarko

N.N. Semenov Institute of Chemical Physics, Moscow

N.N. Semenov Institute of Chemical Physics, Moscow

B S Kogarko

N.N. Semenov Institute of Chemical Physics, Moscow

N.N. Semenov Institute of Chemical Physics, Moscow

N V Lyubimova

N.N. Blokhin Russian Cancer Research Center, Moscow

N.N. Blokhin Russian Cancer Research Center, Moscow

References

  1. Glenner G. G., Terry W., Harada M. et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analysis. Science 1971; 171: 1150-1151.
  2. Benditt E. P., Eriksen N. Chemical classes of amyloid substance. Am. J. Pathol. 1971; 65: 231-252.
  3. Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J. Exp. Med. 1973; 138: 373-380.
  4. Liepnieks J. J., Kluve-Beckerman B., Benson M. D. Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum-amyloid A1. Biochim. Biophys. Acta 1995; 1270: 81-86.
  5. Bradwell A. R. Serum free light chain analysis. 4th ed.: The Binding Site Ltd.; 2006.
  6. Sipe J. D. ed. Amyloid proteins. The beta sheet conformation and disease. WILEY-VCH; 2005.
  7. Moriguchi M., Terai C., Koseki Y. et al. Influence of genotypes at SAA1 and SAA2 loci on the development and the length of latent period of secondary AA- amyloidosis in patients with rheumatoid arthritis. Hum. Genet. 1999; 105: 360-366.
  8. Moriguchi M., Terai C., Kaneko H. et al. A novel single-nucleotide polymorphism at the 5-lanking region of SAA1 associated with risk or type AA amyloidosis secondary to rheumatoid arthritis. Arthr. and Rheum. 2001; 44: 1266-1272.
  9. Yamada T., Okuda Y., Takasugi K. et al. An allele of serum amyloid A1 associated with amyloidosis in both Japanese and Caucasians. Amyloid: J. Protein Folding Disord. 2003; 10: 7- 11.
  10. Booth D. R., Booth S. E., Gillimore J. D. et al. SAA1 alleles as risk factors in reactive systemic amyloidosis. Amyloid: Int. J. Exp. Clin. Invest. 1998; 5: 262-265.
  11. Cazeneuve C., Ajrapetyan H., Papin S. et al. Identification of MEFV-independent modifying genetic factors for familial Mediterranean fever. Am. J. Hum. Genet. 2000; 67: 1136- 1143.
  12. Medlej-Hashim M., Delague V., Chouery E. et al. Amyloidosis in familial Mediterranean fever patients: correlation with MEFV genotype and SAA1 and MICA polymorphisms effects. BMC Med. Genet. 2004; 5: 4.
  13. Gershoni-Baruch R., Brik R., Zacks N. et al. The contribution of genotypes at the MEFV and SAA1 loci to amyloidosis and disease severity in patients with familial Mediterranean fever. Arthr. and Rheum. 2003; 48: 1149-1155.
  14. Bakkaloglu A., Duzova A., Ozen S. et al. Influence of serum amyloid A (SAA1) and SAA2 gene polymorphisms on renal amyloidosis, and on SAA/C-reactive protein values in patients with familial Mediterranean fever in the Turkish population. J. Rheumatol. 2004; 31: 1139-1142.
  15. Akar N., Hasipek M., Akar E. et al. Serum amyloid A1 and tumor necrosis factor-alpha alleles in Turkish familial Mediterranean fever patients with and without amyloidosis. Amyloid: J. Protein Folding Disord 2003; 10: 12-16.
  16. Gillmore J. D., Lovat L. B., Persey M. R. et al. Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein. Lancet 2001; 358: 24-29.
  17. Козловская Л. В., Рамеев В. В., Саркисова И. А. Патогенез и клиническое значение анемии хронических заболеваний. Анемия 2005; 4: 22- 31.
  18. Baba A., Takahashi T., Kasama T. et al. A novel polymorphism of human serum amyloid A protein, SAA1 is characterized by alanines at both residues 52 and 57. Biochim. Biophys. Acta 1992; 1180 (2): 615-620.
  19. Baba S., Masago S. A., Takahashi T. et al. A novel allelic variant of serum amyloid A, SAA1 gamma: genomic evidence, evolution, frequency, and implication as a risk factor for reactive systemic AA-amyloidosis. Hum. Mol. Genet. 1995; 4: 1083-1087.
  20. Magy N,. Benson M. D., Liepnieks J. J., Kluve-Beckerman B. Cellular events associated with the initial phase of AA amyloidogenesis: insights from a human monocyte model. Amyloid 2007; 14 (1): 51-63.
  21. Финкельштейн А. В., Птицин О. Б. Физика белка. М.: Книжный дом "Университет"; 2002.
  22. Kyle R. A., Gertz M. A. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin. Hematol. 1995; 32 (1): 45-59.

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