PDF(Pubmed)
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.
摘要：
这项研究旨在阐明在前列腺和肺中形成淀粉样蛋白的黄体（CA）之间的异同。检查房室结囊性肿瘤（CTAVN）中CA的性质，并阐明淀粉样蛋白形成性CA和球形淀粉样蛋白沉积之间的区别。我们使用液相色谱-串联质谱，激光显微切割和免疫组织化学进行了蛋白质组学分析，以验证肺和前列腺中CA的特征。我们的发现表明，这些器官中的CA主要由常见蛋白质（β2-微球蛋白和溶菌酶）和局部产生的蛋白质组成。此外，我们观察到CTAVN相关CA的组织病理学和蛋白质组学分析结果之间存在差异.此外,虽然形成淀粉样蛋白的CA和球形淀粉样蛋白沉积物的组织病理学外观几乎相同，后者的沉积缺乏β2-微球蛋白和溶菌酶，并表现出对周围组织的明显破坏。文献综述进一步支持了这些发现。这些结果表明，肺和前列腺中形成淀粉样蛋白的CA是通过共同的机制形成的，用作废物容器（废物体）和/或储存多余的蛋白质（功能性淀粉样蛋白）。相比之下,我们假设在形成淀粉样蛋白的CA和球形淀粉样蛋白沉积物的同时，在某种程度上,通过共同机制，后者是病态的。
