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Molecular Research on Amyloidosis in Pathobiology and Therapy
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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: 30 May 2024 | Viewed by 1022

Special Issue Editor

Dr. Kazufumi Nakamura

E-Mail Website
Guest Editor
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; antioxidant; heart failure; hyperlipidemia; atherosclerosis; cardiomyopathy; pulmonary hypertension
Special Issues, Collections and Topics in MDPI journals

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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

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 - 04 Apr 2024
Viewed by 818
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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