Cardiac amyloidosis after lumbar spinal stenosis surgery - a comprehensive prospective cohort study.

IF 5.2 2区医学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Amyloid-Journal of Protein Folding Disorders Pub Date : 2025-03-25 DOI:10.1080/13506129.2025.2481310

Per Eldhagen, Antonios Tzortzakakis, Lars H Lund, Liselott Söderström, Svante Berg, Per Westermark, Peder Sörensson

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引用次数: 0

Abstract

Background: Wild-type transthyretin (ATTRwt) amyloidosis is underdiagnosed and generally diagnosed with manifest cardiac involvement. Lumbar spinal stenosis (LSS) might be an early sign of systemic transthyretin amyloidosis and a possible screening target for early diagnosis.

Objectives: To assess the prevalence of cardiac amyloidosis (CA) 6 years post-LSS surgery, among patients with transthyretin amyloid deposits in ligamentum flavum.

Methods: Twenty-one patients who had surgery for LSS in 2016-2018 and grade 3-4 ATTR amyloid deposits in ligamentum flavum were followed up in 2022-2023, including biomarkers, echocardiography, cardiac magnetic resonance (CMR) and nuclear imaging.

Results: At follow-up, median age was 79 years, 16% (3/19) displayed cardiac uptake on scintigraphy consistent with ATTR-CA. Forty-eight percent (10/21) had a history of other tenosynovial conditions associated with ATTRwt. We observed a small increase in tissue characteristics using CMR, and a decrease in left ventricular global longitudinal strain and left atrial strain on echocardiography.

Conclusions: In this prospective cohort study, 16% were diagnosed with ATTRwt cardiomyopathy, six years following surgery for LSS. History of other tenosynovial conditions associated with ATTRwt amyloidosis was common. These findings strengthen the hypothesis that LSS is a possible manifestation of ATTRwt amyloidosis and that in selected patients with LSS, cardiac follow-up is of value.

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来源期刊

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

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.