Technetium-99m-pyrophosphate imaging-based computed tomography-guided core-needle biopsy of internal oblique muscle in wild-type transthyretin cardiac amyloidosis.

IF 5.2 2区 医学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Amyloid-Journal of Protein Folding Disorders Pub Date : 2024-03-01 Epub Date: 2023-07-24 DOI:10.1080/13506129.2023.2235881
Koji Takahashi, Yoshiyasu Hiratsuka, Takaaki Iwamura, Daisuke Sasaki, Nobuhisa Yamamura, Sohei Kitazawa, Mitsuharu Ueda, Hiroe Morioka, Takafumi Okura, Daijiro Enomoto, Shigeki Uemura, Taizo Kono, Tomoki Sakaue, Shuntaro Ikeda
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引用次数: 0

Abstract

Background: Technetium-99m-pyrophosphate (99mTc-PYP) uptake in the internal oblique muscle (IOM), which is often observed in patients with wild-type transthyretin cardiac amyloidosis (ATTR-CA), indicates amyloid transthyretin (ATTR) deposition.

Objective: This study aimed to assess the safety and efficacy of 99mTc-PYP imaging-based computed tomography (CT)-guided core-needle biopsy of the IOM as a new extracardiac screening biopsy for confirming the presence of ATTR deposits.

Methods: Patients with suspected ATTR-CA in whom myocardial tracer uptake was detected on chest- and abdomen-centered images of 99mTc-PYP scintigraphy underwent CT-guided core-needle biopsy at the site with the highest tracer uptake in the IOM between September 2021 and November 2022.

Results: All 18 consecutive patients (mean age, 86.3 years ± 6.5; 61.1% male) enrolled in the study showed 99mTc-PYP uptake into the IOM. Adequate tissue samples were obtained from all patients except one without serious complications. Immunohistochemical analysis confirmed ATTR deposits in 16/18 (88.9%) patients. In the remaining two patients, ATTR deposits were observed via endomyocardial biopsy. All patients were diagnosed with wild-type ATTR-CA based on transthyretin gene sequence testing results.

Conclusion: In wild-type ATTR-CA, 99mTc-PYP imaging-based CT-guided core-needle biopsy of the IOM could be used as an extracardiac screening biopsy to confirm the presence of ATTR deposits.

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基于锝-99m-焦磷酸成像的计算机断层扫描引导的野生型转甲状腺素心脏淀粉样变性内斜肌核心针活检。
背景:在野生型转甲状腺素心脏淀粉样变性(ATTR-CA)患者中经常观察到的内斜肌(IOM)中锝-99m-焦磷酸(99mTc-PYP)摄取表明淀粉样转甲状腺素(ATTR)沉积:本研究旨在评估基于99m锝-PYP成像的计算机断层扫描(CT)引导的IOM核心针活检作为一种新的心外筛查活检的安全性和有效性,以确认是否存在ATTR沉积:方法:2021年9月至2022年11月期间,在99m锝-PYP闪烁成像的胸腹部中心图像上检测到心肌示踪剂摄取的疑似ATTR-CA患者在CT引导下在IOM示踪剂摄取量最高的部位进行核心穿刺活检:参加研究的所有18名连续患者(平均年龄为86.3岁±6.5岁;61.1%为男性)均显示IOM摄取99m锝-PYP。除一名无严重并发症的患者外,所有患者都获得了足够的组织样本。免疫组化分析证实了16/18(88.9%)名患者体内存在ATTR沉积物。其余两名患者的 ATTR 沉积是通过心内膜活检观察到的。根据转甲状腺素基因序列检测结果,所有患者均被诊断为野生型ATTR-CA:结论:在野生型ATTR-CA患者中,基于99m锝-PYP成像的CT引导IOM核心针活检可用作心外筛查活检,以确认ATTR沉积物的存在。
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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.
期刊最新文献
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