Exploring the Molecular Pathology of Iatrogenic Amyloidosis

Bernardo Bonilauri
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Abstract

Iatrogenic amyloidosis results from medical therapeutic interventions, leading to the misfolding and aggregation of proteins into amyloid fibrils or to their direct deposition in different tissues. This review aims to provide a comprehensive overview of the iatrogenic amyloidosis pathology, underlying the possible molecular mechanisms, associated pathological manifestations, and clinical implications within modern medicine. By conducting a systematic analysis of the current literature, this paper highlights the diverse instances of iatrogenic amyloidosis triggered by medical procedures such as dialysis, organ and tissue transplantation, and therapeutic drugs. Exploring the intricate molecular pathways and contributing factors involved in protein misfolding and amyloidogenesis, and uncovering the pathological consequences observed in various tissues and organs, allows us to establish appropriate nomenclature and to gain a more profound understanding of the condition, working towards improved medical interventions and treatments.
探索先天性淀粉样变性的分子病理学
先天性淀粉样变性是由于医学治疗干预导致蛋白质错误折叠和聚集成淀粉样纤维,或直接沉积在不同的组织中。这篇综述旨在全面概述先天性淀粉样变性的病理特征、可能的分子机制、相关病理表现以及对现代医学的临床影响。通过对现有文献进行系统分析,本文强调了由透析、器官和组织移植以及治疗药物等医疗程序引发的各种先天性淀粉样变性。探索蛋白质错误折叠和淀粉样蛋白生成所涉及的错综复杂的分子途径和致病因素,揭示在不同组织和器官中观察到的病理后果,使我们能够建立适当的命名方法,并对这种疾病有更深刻的了解,从而改进医疗干预和治疗方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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