Please use this identifier to cite or link to this item: http://hdl.handle.net/10201/17826

Title: Electron microscopic study on amyloid fibril formation in human lymph nodes
Issue Date: 1986
Publisher: Murcia : F. Hernández
ISSN: 0213-3911
Related subjects: CDU::6 - Ciencias aplicadas::61 - Medicina
Keywords: Amyloidosis
Ultrastructure
Abstract: The purpose of this investigation was to clarify the mechanisms of amyloid fibril formation in human lymph nodes. In our present study, amyloid deposition was observed diffusely in all compartments of the lymph nodes. The deposition form showed extremely characteristic findings in its morphological features. Namely, amyloid deposits mainly consisted of clusters of round or oval nodules. Each amyloid nodule was frequently enclosed with long-stretched cytoplasmic processes of abutting reticulum cells and/or macrophages. Amyloid fibrils often formed parallel amyloid bundles radiating to outlying sections of the nodule from the center. The amyloid bundles closely adhered to the cytoplasmic membrane of not only the abutting reticulum cells, macrophages and sinus endothelium but also to the lymphocytes and plasma cells. In the central portion of the amyloid nodules, a concentric core was also observed. The most interesting finding was the intracellular formation of amyloid fibrils in all cells, such as macrophages, reticulum cells, foreign body giant cells and lymphocytes in the process of degeneration. Some fibrils localized in the limited area of the cytoplasm and others appeared in all parts of the cells, including the nucleus. Their cell membranes were missing in several areas and the cell organella had gradually dissolved. Finally the cell residuums were completely replaced by amyloid fibrils and transformed into a nodular structure with radiating bundles of amyloid fibrils.
Primary author: Michio Dobashi
Fumiaki Yuda
Akihiro Masuda
Kazuo Terashima
Yutaka lmai
Published in: Histology and histopathology
URI: http://hdl.handle.net/10201/17826
Document type: info:eu-repo/semantics/article
Number of pages / Extensions: 13
Rights: info:eu-repo/semantics/openAccess
Appears in Collections:Vol. 1, nº 3 (1986)

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