Browsing by Subject "Amyloidosis"

Now showing 1 - 4 of 4
  • Thumbnail Image
    Publication
    Open Access
    Electron microscopic study on amyloid fibril formation in human lymph nodes
    (Murcia : F. Hernández, 1986) Michio Dobashi; Fumiaki Yuda; Akihiro Masuda; Kazuo Terashima; Yutaka lmai
    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.
  • Thumbnail Image
    Publication
    Open Access
    Intestinal uptake of amyloid B protein through columnar epithelial cells in suckling mice
    (Murcia : F. Hernández, 2009) Ano, Yasuhisa; Nakayama, Hiroyuki; Sakudo, Akikazu; Sawano, Yoriko; Tanokura, Masaru; Itohara, Shigeyoshi; Onodera, Takashi
    The mechanism of transmission of amyloid protein, especially the dynamics in the intestine, is still largely unknown. In the present study, a fusion protein (Aß-EGFP) that combined enhanced green fluorescent protein with amyloid-ß protein (Aß) was orally administered to mice before and after weaning, and the uptake and kinetics of amyloid protein within the intestine were elucidated through histopathology. Aß- EGFP was incorporated into the cytoplasm of columnar epithelial cells, rather than M cells, at 3 h after administration and thereafter. Aß-EGFP then accumulated in the crypt, Peyer's patch, and even the spleen. However, this uptake was not observed in weaned mice. These results suggest that a specific tolerant mechanism for incorporation of Aß escaped from the digestion exists during suckling periods. This age-dependent uptake is important for estimating the risk of transmission.
  • Thumbnail Image
    Publication
    Open Access
    Investigation of AGE, their receptor and NF-KB activation and apoptosis in patients with ATTR and Gelsolin amyloidosis
    (Murcia : F. Hernández, 2010) Anan, Intissar; Kiuru-Enari, Sari; Obayashi, Konen; Ranløv, Poul Jørgen; Ando, Yukio
    Background: Transthyretin (TTR) and gelsolin amyloidoses represent two types of hereditary amyloidosis in which point mutations in the respective protein lead to conformational changes of the protein with subsequent amyloid fibril formation. Material and methods: Tissues from Finnish gelsolin amyloid patients, Danish, Japanese and Swedish ATTR patients were immunostained for AGE, RAGE, NF-κB, PARP, and caspases 3 and 8. Results: Amyloid was heavily deposited in myocard, kidney and gastrointestinal tract of all patients. Immunoreactive areas to AGE and RAGE were detected in the heart, kidney, rectum, gut and appendix. AGE and RAGE were well co-localised with amyloid deposits. In five out of 14 patients neither NF-κB activation nor induction of apoptosis marked by positive immunostaining for NF-κB, PARP, or caspases 3 and 8 was found, and markers of apoptosis were detected in some samples without accompanying NF-κB activation. Conclusion: Our results suggest that both AGE and RAGE may have a common role in evolution of TTR and gelsolin-related amyloidoses. Apart from AGE-RAGE interactions both amyloid proteins may directly bind to RAGE and result in cellular perturbations; but in view of this study cytotoxic effects other than those triggered by activation of NF-κB or apoptosis should be considered
  • Thumbnail Image
    Publication
    Open Access
    Secondary amyloidosis and cystic fibrosis. A morphological and histochemical study of five cases
    (Murcia : F. Hernández, 1987) Bontempini, L.; Ghimenton, C.; Colombari, R.; Malena, M.; Luzzolino, P.; Canciani, M.; Doglioni, C.; Sbabo, L.
    The pathological findings of five cases of amyloidosis associated with Cystic Fibrosis are reported. Rectal biopsy led to the diagnosis of amyloidosis in four patients. In three cases the diagnosis was confirmed at autopsy , with involvement of spleen, liver, kidneys, adrenal glands, thyroid and other organs. It seems that Secondary Amyloidosis provokes a significant, although rare, complication of Cystic Fibrosis as greater numbers of these patients survive into adulthood.