Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A
Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and sev...
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doaj-ad74507e238f41678c36268cb8d8aa8a2021-01-22T00:02:35ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-01-01221036103610.3390/ijms22031036Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid AXuguang Lin0Kenichi Watanabe1Masahiro Kuragano2Kiyotaka Tokuraku3Muroran Institute of Technology, Graduate School of Engineering, Muroran 050-8585, JapanResearch Center of Global Agromedicine, Department of Veterinary Medicine, Obihiro University of Agriculture and Veterinary Medicine, Obihiro 080-8555, JapanMuroran Institute of Technology, Graduate School of Engineering, Muroran 050-8585, JapanMuroran Institute of Technology, Graduate School of Engineering, Muroran 050-8585, JapanAmyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis.https://www.mdpi.com/1422-0067/22/3/1036amyloid A amyloidosisamyloid enhancing factorhomologyserum amyloid Aquantum-dot |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Xuguang Lin Kenichi Watanabe Masahiro Kuragano Kiyotaka Tokuraku |
spellingShingle |
Xuguang Lin Kenichi Watanabe Masahiro Kuragano Kiyotaka Tokuraku Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A International Journal of Molecular Sciences amyloid A amyloidosis amyloid enhancing factor homology serum amyloid A quantum-dot |
author_facet |
Xuguang Lin Kenichi Watanabe Masahiro Kuragano Kiyotaka Tokuraku |
author_sort |
Xuguang Lin |
title |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
title_short |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
title_full |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
title_fullStr |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
title_full_unstemmed |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
title_sort |
aggregation of mouse serum amyloid a protein was promoted by amyloid-enhancing factors with the more genetically homologous serum amyloid a |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-01-01 |
description |
Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis. |
topic |
amyloid A amyloidosis amyloid enhancing factor homology serum amyloid A quantum-dot |
url |
https://www.mdpi.com/1422-0067/22/3/1036 |
work_keys_str_mv |
AT xuguanglin aggregationofmouseserumamyloidaproteinwaspromotedbyamyloidenhancingfactorswiththemoregeneticallyhomologousserumamyloida AT kenichiwatanabe aggregationofmouseserumamyloidaproteinwaspromotedbyamyloidenhancingfactorswiththemoregeneticallyhomologousserumamyloida AT masahirokuragano aggregationofmouseserumamyloidaproteinwaspromotedbyamyloidenhancingfactorswiththemoregeneticallyhomologousserumamyloida AT kiyotakatokuraku aggregationofmouseserumamyloidaproteinwaspromotedbyamyloidenhancingfactorswiththemoregeneticallyhomologousserumamyloida |
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