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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: closed (20 July 2025) | Viewed by 9219

Special Issue Editor

Dr. Kazufumi Nakamura

E-Mail Website
Guest Editor
Center for Advanced Heart Failure, Okayama University Hospital, Okayama, Japan
Interests: cardiovascular system; cardiac sarcoidosis; coronary artery disease; vein anastomosis; dilated cardiomyopathy
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

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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.

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Keywords

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

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Published Papers (3 papers)

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Research

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20 pages, 2353 KB  
Article
Profibrotic Biomarkers Correlate with Clinical Presentation and Outcome in Cardiac Transthyretin Amyloidosis
by Selina J. Hein, Fabian aus dem Siepen, Arnt V. Kristen, Stefan Schönland, Ute Hegenbart, Katrin Rein, Hugo A. Katus, Norbert Frey, Jennifer Furkel, Mathias H. Konstandin and Maximilian Knoll
Int. J. Mol. Sci. 2025, 26(21), 10714; https://doi.org/10.3390/ijms262110714 - 4 Nov 2025
Viewed by 1109
Abstract
In transthyretin cardiac amyloidosis (ATTR-CA), misfolded transthyretin accumulates in the myocardium, leading to wall thickening and interstitial fibrosis. Recently published in vitro studies revealed direct effects of transthyretin on the structure, function, and gene expression of cardiac fibroblasts. Therefore, we hypothesized that biomarkers [...] Read more.
In transthyretin cardiac amyloidosis (ATTR-CA), misfolded transthyretin accumulates in the myocardium, leading to wall thickening and interstitial fibrosis. Recently published in vitro studies revealed direct effects of transthyretin on the structure, function, and gene expression of cardiac fibroblasts. Therefore, we hypothesized that biomarkers known to modulate myocardial remodeling might be clinically valuable in ATTR-CA and may improve risk stratification in ATTR-CA. To analyze this hypothesis, we evaluated 14 fibrosis-related biomarkers (EN-RAGE, IGFBP-1, -2, -3, -4, -6, FGF-23, MMP-2, -7, -9, -13, TIMP-2, -4, and RAGE-AGE) in 125 patients using Luminex multiplex assays. The study cohort consists of 14 asymptomatic gene carriers (ATTRv-asymp), 47 symptomatic hereditary (ATTRv-CA), 43 wild-type Transthyretin amyloidosis (ATTRwt) patients, and 21 were healthy controls (ctrl). Associations of fibrotic biomarkers and clinical routine data with clinical outcomes—cardiac decompensation (DMP) and transplantation/death (HTX)—were assessed via hierarchical cluster analysis, regression, and prediction modeling. We found that ATTR-CA patients showed distinct biomarker profiles compared to controls. Several markers (e.g., MMP-7, RAGE-AGE, IGFBP-1, FGF-23, TIMP-2) were significantly associated with both endpoints. Cluster analysis identified a high-risk phenotype (Cluster 2) with worse renal function, greater myocardial thickening, and elevated NT-proBNP, hsTNT. Prediction modeling revealed IGFPB-1, -3, -4 and -6 as well as FGF-23, TIMP-2, and RAGE/AGE as the best predictive parameters for cluster assignment. Taken together, these findings confirm our hypothesis that fibrosis-related biomarkers are associated with adverse outcomes in ATTR-CM. Profibrotic mediators such as IGFBP-1, FGF-23, and TIMP-2 may, therefore, provide additional prognostic information beyond established cardiac biomarkers and may reflect underlying fibrotic remodeling pathways. Full article
(This article belongs to the Special Issue Molecular Research on Amyloidosis in Pathobiology and Therapy)
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15 pages, 20093 KB  
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
Cited by 3 | Viewed by 4916
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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Review

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15 pages, 5104 KB  
Review
Serum and Tissue Light-Chains as Disease Biomarkers in AL Amyloidosis
by Alberto Aimo, Yu Fu Ferrari Chen, Michela Chianca, Francesco Mori, Angela Pucci, Vincenzo Castiglione, Veronica Musetti, Laura Caponi, Iacopo Fabiani, Giuseppe Vergaro, Maria Franzini, Michele Emdin and Daniela Cardinale
Int. J. Mol. Sci. 2025, 26(19), 9511; https://doi.org/10.3390/ijms26199511 - 29 Sep 2025
Cited by 1 | Viewed by 2315
Abstract
Amyloid light-chain (AL) amyloidosis is the most prevalent type of diagnosed systemic amyloidosis in Western countries, characterized by the deposition of misfolded immunoglobulin light chains (LCs) in various organs, most commonly the heart and kidneys. Circulating free LC (FLC) measurement, which can be [...] Read more.
Amyloid light-chain (AL) amyloidosis is the most prevalent type of diagnosed systemic amyloidosis in Western countries, characterized by the deposition of misfolded immunoglobulin light chains (LCs) in various organs, most commonly the heart and kidneys. Circulating free LC (FLC) measurement, which can be performed by mass spectrometry or antibody-based techniques, is a crucial tool for AL amyloidosis diagnosis, risk assessment, and management. Additionally, diagnosing AL amyloidosis requires accurate detection of LC deposits in tissues. In addition to immunohistochemical techniques, mass spectrometry-based methods are now available. Full article
(This article belongs to the Special Issue Molecular Research on Amyloidosis in Pathobiology and Therapy)
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