Distribution of Transmissible Amyloid Proteins in the Liver with Apolipoprotein A-Ⅱ Amyloidosis Distribution of Transmissible Amyloid Proteins in the Liver with Apolipoprotein A-II Amyloidosis
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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.
- THE SHINSHU MEDICAL JOURNAL
THE SHINSHU MEDICAL JOURNAL 64(4), 183-194, 2016
The Shinshu Medical Society