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Article

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

1
Department of Legal Medicine, Faculty of Medicine, University of Toyama, Toyama 930-0194, Japan
2
Department of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto 390-8621, Japan
3
Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan
4
Institute for Biomedical Sciences, Shinshu University, Matsumoto 390-8621, Japan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2024, 25(7), 4040; https://doi.org/10.3390/ijms25074040
Submission received: 6 March 2024 / Revised: 31 March 2024 / Accepted: 3 April 2024 / Published: 4 April 2024
(This article belongs to the Special Issue Molecular Research on Amyloidosis in Pathobiology and Therapy)

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 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.
Keywords: amyloid; beta-2 micro-globulin; corpora amylacea; functional amyloids; lactoferrin; lysosome; macrophage; pulmonary surfactant protein amyloid; beta-2 micro-globulin; corpora amylacea; functional amyloids; lactoferrin; lysosome; macrophage; pulmonary surfactant protein
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MDPI and ACS Style

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. https://doi.org/10.3390/ijms25074040

AMA Style

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. International Journal of Molecular Sciences. 2024; 25(7):4040. https://doi.org/10.3390/ijms25074040

Chicago/Turabian Style

Ichimata, Shojiro, Yukiko Hata, Tsuneaki Yoshinaga, Nagaaki Katoh, Fuyuki Kametani, Masahide Yazaki, Yoshiki Sekijima, and Naoki Nishida. 2024. "Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review" International Journal of Molecular Sciences 25, no. 7: 4040. https://doi.org/10.3390/ijms25074040

APA Style

Ichimata, S., Hata, Y., Yoshinaga, T., Katoh, N., Kametani, F., Yazaki, M., Sekijima, Y., & Nishida, N. (2024). Amyloid-Forming Corpora Amylacea and Spheroid-Type Amyloid Deposition: Comprehensive Analysis Using Immunohistochemistry, Proteomics, and a Literature Review. International Journal of Molecular Sciences, 25(7), 4040. https://doi.org/10.3390/ijms25074040

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