Valentina Moccia, Claudia Maria Tucciarone, Silvia Garutti, Melissa Milazzo, Filippo Ferri, Carlo Palizzotto, Maria Mazza, Marco Basset, Eric Zini, Stefano Ricagno, Silvia Ferro
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引用次数: 0
Abstract
AA amyloidosis is a prototypic example of systemic amyloidosis: it results from the prolonged overproduction of SAA protein produced in response to chronic inflammation. AA amyloidosis primarily affects the kidneys, liver, spleen, gastrointestinal tract, leading to a variety of symptoms. First, this review examines AA amyloidosis in humans, focusing on pathogenesis, clinical presentation, and diagnosis and then in animals. In fact AA amyloidosis is the only systemic amyloidosis that has been largely documented in a remarkable number of vertebrate species: mammals, birds, and fishes, especially in individuals with comorbidities, chronic stress, or held in captivity. Secondly, here, we summarise independent sets of evidence obtained on different animal species, exploring the possible transmissibility of AA amyloidosis especially in crowded or confined populations. Finally, biochemical and structural data on native SAA and on AA amyloid fibrils from human, murine, and cat ex vivo samples are discussed. The available structural data depict a complex scenario, where SAA can misfold forming highly different amyloid assemblies. This review highlights the complexity of AA amyloidosis, emphasising the need for further research into its spread in the animal kingdom, its structural aspects, and pathogenetic mechanisms to evaluate its impact on human and animal health.
AA 淀粉样变性是全身性淀粉样变性的一个典型例子:它是由于慢性炎症引起的 SAA 蛋白长期过度生成所致。AA 淀粉样变性主要影响肾脏、肝脏、脾脏和胃肠道,导致多种症状。本综述首先探讨了人类 AA 淀粉样变性,重点是发病机制、临床表现和诊断,然后探讨了动物 AA 淀粉样变性。事实上,AA 淀粉样变性是唯一一种在大量脊椎动物(哺乳动物、鸟类和鱼类)中都有大量记载的全身性淀粉样变性病,尤其是在有合并症、慢性应激或圈养的个体中。其次,我们在此总结了在不同动物物种身上获得的独立证据集,探讨了 AA 淀粉样变性可能的传播性,尤其是在拥挤或封闭的种群中。最后,我们讨论了原生 SAA 以及来自人类、鼠类和猫科动物体内外样本的 AA 淀粉样蛋白纤维的生化和结构数据。现有的结构数据描述了一种复杂的情况,即 SAA 可错误折叠形成高度不同的淀粉样蛋白组合。本综述强调了 AA 淀粉样变性的复杂性,强调有必要进一步研究其在动物界的传播、结构方面和致病机制,以评估其对人类和动物健康的影响。
期刊介绍:
Amyloid: the Journal of Protein Folding Disorders is dedicated to the study of all aspects of the protein groups and associated disorders that are classified as the amyloidoses as well as other disorders associated with abnormal protein folding. The journals major focus points are:
etiology,
pathogenesis,
histopathology,
chemical structure,
nature of fibrillogenesis;
whilst also publishing papers on the basic and chemical genetic aspects of many of these disorders.
Amyloid is recognised as one of the leading publications on amyloid protein classifications and the associated disorders, as well as clinical studies on all aspects of amyloid related neurodegenerative diseases and major clinical studies on inherited amyloidosis, especially those related to transthyretin. The Journal also publishes book reviews, meeting reports, editorials, thesis abstracts, review articles and symposia in the various areas listed above.