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(American Journal of Pathology. 1999;155:1319-1326.)
© 1999 American Society for Investigative Pathology

Regular Articles

Mouse Senile Amyloid Deposition Is Suppressed by Adenovirus-Mediated Overexpression of Amyloid-Resistant Apolipoprotein A-II

Takuya Chiba*§, Kumiko Kogishi*, Jing Wang*, Chen Xia*, Takatoshi Matsushita*, Jun-ichi Miyazaki{dagger}, Izumu Saito{ddagger}, Masanori Hosokawa* and Keiichi Higuchi§

From the Field of Regeneration Control,*
Institute for Frontier Medical Science, Kyoto University, Kyoto; the Department of Nutrition and Physiological Chemistry,{dagger}
Osaka University Medical School, Osaka; the Laboratory of Molecular Genetics,{ddagger}
Institute of Medical Science, University of Tokyo, Tokyo; and the Department of Aging Angiology,§
Research Center on Aging and Adaptation, Shinshu University School of Medicine, Matsumoto, Japan

Apolipoprotein A-II (apoA-II), the second most abundant apolipoprotein of serum high density lipoprotein, deposits as an amyloid fibril (AApoAII) in old mice. Mouse strains with a high incidence of senile amyloidosis have the type C apoA-II gene (Apoa2c), whereas the strains with a low incidence of amyloidosis have the type B apoA-II gene (Apoa2b). In this study, to investigate whether the type B apoA-II protein inhibits the extension of amyloid fibrils, we constructed an adenovirus vector bearing the Apoa2b cDNA (Adex1CATApoa2b), which is expressed under the control of a hepatocyte-specific promoter. The mice were infected with Adex1CATApoa2b before induction of amyloidosis by the injection of AApoAII amyloid fibril seeds. Compared with the mice infected with the control virus, amyloid deposition was suppressed significantly in the mice infected with Adex1CATApoa2b. Fluorometry using thioflavine T also revealed that AApoAII fibril extension was inhibited by the addition of type B apoA-II in vitro. Thus, we propose that Apoa2b contributes as an active inhibitor of amyloid fibril extension and overexpression of amyloid-resistant gene variant may be an attractive therapeutic target in amyloidosis.




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