Distribution of Transmissible Amyloid Proteins in the Liver with Apolipoprotein A-II Amyloidosis

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  • LIU Yingye
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine
  • SAWASHITA Jinko
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine Department of Biomedical Sciences for Intractable Neurological Diseases, Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University
  • WANG Yaoyong
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine Fenyang Hospital Affiliated with Shanxi Medical University, Shanxi, China
  • LI Lin
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine
  • MIYAHARA Hiroki
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine
  • DING Xin
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine
  • YANG Mu
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine
  • HIGUCHI Keiichi
    Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine Department of Biomedical Sciences for Intractable Neurological Diseases, Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University

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Abstract

In some amyloidoses, transmission by self-propagating amyloid proteins plays a critical role in the progression of the disease. Mouse senile amyloidosis is a disorder in which apolipoprotein A-II (ApoA-II) deposits as amyloid fibrils (AApoAII), and it might be transmitted by ingestion of those amyloid fibrils. Characterization of protein species responsible for transmission of mouse AApoAII amyloidosis should provide valuable information. Here, we studied the distributions of ApoA-II and inducing activities in liver fractions that were insoluble or soluble and had different degrees of amyloid deposition. ApoA-II was mainly contained in the 3,000 x g pellet fractions regardless of the degree of amyloid deposition. The 3,000 x g pellet fraction showed strong amyloid fibril-specific fluorescence of fibril-bound thioflavin T and strong amyloidosis-inducing activity. Sonication of liver homogenate increased the proportion of ApoA-II and inducing activity of the 100,000 x g pellet fraction. Weak inducing activity was found in the soluble fraction. We fractionated and isolated multiple assemblies of AApoAII amyloid fibrils by non-denaturing polyacrylamide gel electrophoresis. ApoA-II proteins ranging from monomers to large oligomers had low amyloidosis inducing activity. These results suggest that transmission of AApoAII amyloidosis may be primarily associated with the insoluble amyloid fibril structure.

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