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Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils

Tatsumi Korenaga1, Xiaoying Fu, Yanming Xing

  • 1Department of Aging Biology, Institute on Aging and Adaptation, Shinshu University Graduate School of Medicine, Matsumoto, Japan.

The American Journal of Pathology
|April 28, 2004
PubMed

Insights

Researchers discovered a new type of amyloid fibril, AApoAII(A), composed of apolipoprotein A-II (ApoA-II) protein type A. These fibrils cause distinct amyloidosis in mice, differing from previously known AApoAII(C) fibrils.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pathology

Background:

  • Mice with the amyloidogenic apolipoprotein A-II (ApoA-II) gene (Apoa2c) develop systemic amyloidosis due to type C Apo-AII protein (APOAIIC) forming amyloid fibrils AApoAII(C).
  • Age-associated deposition of amyloid fibrils [AApoAII(A)] composed of type A Apo-AII protein (APOAIIA) was observed in specific mouse strains.

Purpose of the Study:

  • To characterize the novel AApoAII(A) amyloid fibrils and compare their properties to AApoAII(C) and other mouse AA amyloid fibrils.
  • To investigate the amyloidogenic potential and deposition patterns of AApoAII(A) fibrils in different mouse strains.

Main Methods:

  • Isolation and characterization of AApoAII(A) amyloid fibrils.
  • Morphological analysis using transmission electron and atomic force microscopy.
  • Biochemical analysis including thioflavine T binding and beta-pleated sheet structure assessment.
  • In vivo studies involving injection of AApoAII(A) fibrils into different mouse strains to induce amyloidosis.

Main Results:

  • AApoAII(A) fibrils were deposited in the intestine, lungs, tongue, and stomach, but not the liver or spleen.
  • Isolated AApoAII(A) fibrils exhibited distinct protofibril-like shapes and weaker thioflavine T affinity compared to AApoAII(C).
  • APOAIIA protein had less beta-pleated sheet structure than APOAIIC.
  • AApoAII(A) induced amyloidosis in C57BL/6 and DBA2 mice (Apoa2a), with more severe amyloidosis in Apoa2a strains than in Apoa2c strains.

Conclusions:

  • AApoAII(A) fibrils, derived from mildly amyloidogenic APOAIIA protein, possess unique characteristics and induce a distinct form of amyloidosis.
  • Heterologous amyloid fibril injection demonstrated interactions between amyloid protein monomers and fibrils with differing primary structures.

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