ATTR- and AFib amyloid - two different types of amyloid in the annular ligament of trigger finger.

IF 5.2 2区 医学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Amyloid-Journal of Protein Folding Disorders Pub Date : 2023-12-01 Epub Date: 2023-06-23 DOI:10.1080/13506129.2023.2226298
Christian Treitz, Neelis Müller-Marienburg, Rolf Rüdiger Meliß, Peter Urban, Hans-Detlef Axmann, Frank Siebert, Karsten Becker, Klaus Martens, Hans-Michael Behrens, Eva Gericke, Andreas Tholey, Christoph Röcken
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Abstract

Introduction: Histological examination of tissue specimens obtained during surgical treatment of trigger finger frequently encountered unclassifiable amyloid deposits in the annular ligament. We systematically explored this unknown type by a comprehensive analysis using histology, immunohistochemistry, and quantitative mass spectrometry-based proteomics.

Methods: 205 tissue specimens of annular ligaments were obtained from 172 patients. Each specimen was studied by histology and immunohistochemistry. Tissue specimens obtained from ten patients with histology proven amyloid in annular ligament were analysed by label-free quantitative proteomics. Histological and immunohistochemical findings were correlated with patient demographics.

Results: Amyloid was present as band like deposits along the surface of annular ligament, dot like or patchy deposits within the matrix. Immunohistochemistry identified ATTR amyloid in 92 specimens (mostly patchy in the matrix), while the band like deposits of 100 specimens remained unclassifiable. Proteomic profiles identified the unknown amyloid as most likely of fibrinogen origin. The complete cohort was re-examined by immunohistochemistry using a custom-made antibody and confirmed the presence of fibrinogen alpha-chain (FGA) in a hitherto unclassifiable type of amyloid in annular ligament.

Conclusion: Our study shows that two different types of amyloid affect the annular ligament, ATTR amyloid and AFib amyloid, with distinct demographic patient characteristics and histomorphological deposition patterns.

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ATTR和AFib淀粉样蛋白是扳机指环状韧带中两种不同类型的淀粉样蛋白。
导言:对扳机指手术治疗过程中获得的组织标本进行组织学检查,经常发现环状韧带内有无法分类的淀粉样蛋白沉积。我们利用组织学、免疫组织化学和基于定量质谱的蛋白质组学进行综合分析,系统地探索了这种未知类型。方法:对172例患者进行205例环状韧带组织标本采集。对每个标本进行组织学和免疫组织化学研究。采用无标记定量蛋白质组学方法对10例经组织学证实的环状韧带淀粉样蛋白患者的组织标本进行了分析。组织学和免疫组织化学结果与患者人口统计学相关。结果:淀粉样蛋白沿环韧带表面呈带状沉积,基质内呈点状或斑片状沉积。免疫组织化学在92个标本中鉴定出ATTR淀粉样蛋白(大部分在基质中呈斑块状),而100个标本的带状沉积物仍无法分类。蛋白质组学分析鉴定未知淀粉样蛋白最有可能是纤维蛋白原的来源。使用定制抗体对整个队列进行免疫组织化学检查,确认纤维蛋白原α链(FGA)存在于环状韧带中迄今无法分类的淀粉样蛋白类型。结论:我们的研究表明两种不同类型的淀粉样蛋白影响环状韧带,ATTR淀粉样蛋白和AFib淀粉样蛋白,具有不同的人口统计学患者特征和组织形态学沉积模式。
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来源期刊
Amyloid-Journal of Protein Folding Disorders
Amyloid-Journal of Protein Folding Disorders 生物-生化与分子生物学
CiteScore
10.60
自引率
10.90%
发文量
48
审稿时长
6-12 weeks
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.
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