Abstract
The localization of amyloid fibril components and the cells related to the formation and resorption of the fibrils are still controversial. In this study we undertook a time-kinetic study to analyze the process of amyloid fibril deposition in the spleen of AA amyloidosis animal model immunohistochemically and ultrastructurally. Murine amyloid A (AA) amyloidosis was induced by the emulsion injection composed of Freund’s complete adjuvant and Mycobacterium butyricum. Serum amyloid A (SAA) level was the highest at 3 days after the induction and gradually decreased. The amyloid deposition was first detected in extracellular spaces in the marginal zone of the spleen at 7 days after induction. The F4/80 positive red pulp macrophages increased in number after the induction and accumulated near the amyloid deposition areas. Amyloid P component (APC) and chondroitin sulfate proteoglycan (CSPG), which are composed of amyloid fibril, were detected in the cytoplasm of F4/80 positive red pulp macrophages and ER-TR9-positive marginal zone macrophages, respectively, then localized in the amyloid deposition areas. APC was also localized in CSPG-positive and F4/80-negative cells, which might be fibroblasts at 3 days. Ultrastructural examination indicated that macrophages in the marginal zone contained lysosome-derived fibrillar structures of amyloid, and that fibroblasts extended amyloid fibrils into the extracellular area in the marginal zone. These results suggested the close association of APC-positive/ER-TR9-positive macrophages and APC-positive/CSPG-positive fibroblasts with the formation of amyloid fibrils and F4/80-positive macrophages with the resorption of the fibrils.
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Kuroiwa, M., Aoki, K., Izumiyama, N. (2006). Immunohistological Study of Experimental Murine AA Amyloidosis. In: Uversky, V.N., Fink, A.L. (eds) Protein Misfolding, Aggregation, and Conformational Diseases. Protein Reviews, vol 4. Springer, Boston, MA. https://doi.org/10.1007/0-387-25919-8_13
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DOI: https://doi.org/10.1007/0-387-25919-8_13
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