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Abstract <p><b>Objective:</b> Secondary systemic amyloidosis occurs in patients with chronic inflammation and is a consequence of abnormal fibrillogenesis of the acute phase protein serum amyloid A. The causes of this disease development described in the literature include the possibility of inducing fibrillogenesis by introducing serum amyloid A fibrils or other proteins. This paper describes the optimization of an animal model of induced secondary amyloidosis. The prospects for using such models to search for new methods of combating amyloidosis, as well as studying the safety of new drugs based on peptides and recombinant proteins are discussed. The aim of the work was to optimize the previously described in the literature model of induced secondary systemic amyloidosis amyloidosis and to use it to assess the amyloidogenic potential of bovine serum albumin or human serum amyloid P as model proteins for development of testing methods for potential protein or peptide-based drugs. <b>Methods:</b> The work involved optical microscopy of animal tissue sections using the amyloid-specific dye Congo red, and the kinetics of accumulation of radioactively labeled or human serum amyloid P in the spleen were studied. <b>Results and Discussion:</b> A model of induced secondary systemic amyloidosis was reproduced, the presence of amyloid in the spleen of mice was confirmed microscopically and by the accumulation of radioactively labeled serum amyloid P in the spleen. Using optical microscopy, it was shown that parenteral administration of bovine serum albumin or human serum amyloid P to mice also leads to the formation of amyloid deposits in the spleen. <b>Conclusions:</b> In the model of secondary systemic amyloidosis used, splenic amyloidosis in mice occurs during chronic aseptic inflammation with the simultaneous administration of bovine serum albumin or human serum amyloid P. It is proposed to recommend testing potential biologically active polypeptides for their ability to induce the formation of amyloid deposits in the spleen in a murine model.</p>

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Model of Induced Secondary Systemic Amyloidosis: Problems and Prospects

  • 期刊论文

  • 发表日期：

    2025年7月28日

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  • K. V. Masterova,
  • N. A. Grudinina,
  • N. A. Verlov,
  • V. S. Burdakov,
  • V. V. Egorov,
  • M. M. Shavlovsky

摘要

Abstract

Objective: Secondary systemic amyloidosis occurs in patients with chronic inflammation and is a consequence of abnormal fibrillogenesis of the acute phase protein serum amyloid A. The causes of this disease development described in the literature include the possibility of inducing fibrillogenesis by introducing serum amyloid A fibrils or other proteins. This paper describes the optimization of an animal model of induced secondary amyloidosis. The prospects for using such models to search for new methods of combating amyloidosis, as well as studying the safety of new drugs based on peptides and recombinant proteins are discussed. The aim of the work was to optimize the previously described in the literature model of induced secondary systemic amyloidosis amyloidosis and to use it to assess the amyloidogenic potential of bovine serum albumin or human serum amyloid P as model proteins for development of testing methods for potential protein or peptide-based drugs. Methods: The work involved optical microscopy of animal tissue sections using the amyloid-specific dye Congo red, and the kinetics of accumulation of radioactively labeled or human serum amyloid P in the spleen were studied. Results and Discussion: A model of induced secondary systemic amyloidosis was reproduced, the presence of amyloid in the spleen of mice was confirmed microscopically and by the accumulation of radioactively labeled serum amyloid P in the spleen. Using optical microscopy, it was shown that parenteral administration of bovine serum albumin or human serum amyloid P to mice also leads to the formation of amyloid deposits in the spleen. Conclusions: In the model of secondary systemic amyloidosis used, splenic amyloidosis in mice occurs during chronic aseptic inflammation with the simultaneous administration of bovine serum albumin or human serum amyloid P. It is proposed to recommend testing potential biologically active polypeptides for their ability to induce the formation of amyloid deposits in the spleen in a murine model.