Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review

Shojiro Ichimata
* ORCID logo ,
Yukiko Hata
,
Tsuneaki Yoshinaga
ORCID logo ,
Nagaaki Katoh
,
Fuyuki Kametani
ORCID logo ,
Masahide Yazaki
ORCID logo ,
Yoshiki Sekijima
,
Naoki Nishida
Version 1 : Received: 6 March 2024 / Approved: 6 March 2024 / Online: 6 March 2024 (14:06:29 CET)

A peer-reviewed article of this Preprint also exists.

Ichimata, S.; Hata, Y.; Yoshinaga, T.; Katoh, N.; Kametani, F.; Yazaki, M.; Sekijima, Y.; Nishida, N. Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review. Int. J. Mol. Sci. 2024, 25, 4040. Ichimata, S.; Hata, Y.; Yoshinaga, T.; Katoh, N.; Kametani, F.; Yazaki, M.; Sekijima, Y.; Nishida, N. Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review. Int. J. Mol. Sci. 2024, 25, 4040.

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. 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 CAs in these organs primarily consist 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 amyloid-forming CAs and spheroid-type amyloid deposits were nearly identical, the latter deposition lacked β2-microglobulin and lysozyme, and exhibited evident destruction of 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.

Keywords

Amyloid; beta-2 micro-globulin; corpora amylacea; functional amyloids; lactoferrin; lysosome; macrophage; pulmonary surfactant protein

Subject

Medicine and Pharmacology, Pathology and Pathobiology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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