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Molecular Research on Amyloidosis in Pathobiology and Therapy

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 20 December 2024 | Viewed by 2599

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Department of Cardiovascular Medicine, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Kita-ku, Okayama 700-8558, Japan
Interests: fish oil; postprandial hyperlipidemia; antioxidants; heart failure; hyperlipidemia; atherosclerosis; cardiomyopathy; pulmonary hypertension
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Special Issue Information

Dear Colleagues,

Amyloidosis describes a large group of diseases caused by the deposition of insoluble amyloid fibrils formed by misfolded soluble proteins in organs or tissues. The most common types of systemic amyloidosis are amyloid light-chain (AL) amyloidosis, amyloid A (AA) amyloidosis, and transthyretin (TTR) amyloidosis, which are caused by the deposition of amyloid fibrils constituted from immunoglobulin-free light chains (FLCs), serum amyloid A protein, and TTR, respectively. Although the understanding of amyloidosis pathobiology and therapy has increased substantially in recent years, molecular mechanisms, molecular therapeutic targets, and molecular imaging have not been fully elucidated.

This Special Issue is dedicated to molecular research on amyloidosis. Research articles and reviews will inform you about recent developments and update the current state of knowledge.

Dr. Kazufumi Nakamura
Guest Editor

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Keywords

  • amyloidosis
  • ATTR
  • transthyretin
  • misfolding
  • molecular mechanisms
  • molecular therapeutic targets
  • molecular imaging
  • SPECT
  • tracers

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Published Papers (1 paper)

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Research

15 pages, 20093 KiB  
Article
Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review
by Shojiro Ichimata, Yukiko Hata, Tsuneaki Yoshinaga, Nagaaki Katoh, Fuyuki Kametani, Masahide Yazaki, Yoshiki Sekijima and Naoki Nishida
Int. J. Mol. Sci. 2024, 25(7), 4040; https://doi.org/10.3390/ijms25074040 - 4 Apr 2024
Viewed by 2189
Abstract
This study aimed to elucidate the similarities and differences between amyloid-forming corpora amylacea (CA) in the prostate and lung, examine the nature of CAs in cystic tumors of the atrioventricular node (CTAVN), and clarify the distinctions between amyloid-forming CA and spheroid-type amyloid deposition. [...] Read more.
This study aimed to elucidate the similarities and differences between amyloid-forming corpora amylacea (CA) in the prostate and lung, examine the nature of CAs in cystic tumors of the atrioventricular node (CTAVN), and clarify the distinctions between amyloid-forming CA and spheroid-type amyloid deposition. We conducted proteomics analyses using liquid chromatography–tandem mass spectrometry with laser microdissection and immunohistochemistry to validate the characteristics of CAs in the lung and prostate. Our findings revealed that the CAs in these organs primarily consisted of common proteins (β2-microglobulin and lysozyme) and locally produced proteins. Moreover, we observed a discrepancy between the histopathological and proteomic analysis results in CTAVN-associated CAs. In addition, while the histopathological appearance of the amyloid-forming CAs and spheroid-type amyloid deposits were nearly identical, the latter deposition lacked β2-microglobulin and lysozyme and exhibited evident destruction of the surrounding tissue. A literature review further supported these findings. These results suggest that amyloid-forming CAs in the lung and prostate are formed through a shared mechanism, serving as waste containers (wasteosomes) and/or storage for excess proteins (functional amyloids). In contrast, we hypothesize that while amyloid-forming CA and spheroid-type amyloid deposits are formed, in part, through common mechanisms, the latter are pathological. Full article
(This article belongs to the Special Issue Molecular Research on Amyloidosis in Pathobiology and Therapy)
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