Key result
Plasma proteomics model distinguishes ATTR-CM from heart failure controls with an AUC of ~0.89.
Why the study?
Does plasma proteomics profiling discriminate transthyretin amyloid cardiomyopathy from heart failure and hypertensive left ventricular hypertrophy?
Case-Control (n=550)
Yes
Does plasma proteomics profiling discriminate transthyretin amyloid cardiomyopathy from heart failure and hypertensive left ventricular hypertrophy?
Answers are grounded in this paper and cite their sources.
Extensive plasma proteomics profiling reveals a distinct biomarker signature for ATTR-CM, highlighting the PI3K-Akt and JAK-STAT pathways as potential mediators of disease progression and targets for future therapies.
BACKGROUND: Transthyretin amyloid cardiomyopathy (ATTR-CM) causes a restrictive cardiomyopathy resulting in heart failure (HF). Signaling pathways associated with ATTR-CM are not well defined. The purpose of this study was to identify signaling pathways that are dysregulated in ATTR-CM compared with controls. METHODS: This was a case-control study of cases with ATTR-CM, internal controls with hypertensive left ventricular hypertrophy, and external controls with HF. For model development, ATTR-CM cases were age- and sex-matched with internal controls with hypertensive left ventricular hypertrophy. Plasma proteomics profiling of 7289 proteins was conducted. A sparse partial least squares discriminant analysis was performed to develop a proteomics-based discrimination model from 70% of the data (ie, the training set), and the discriminative ability was tested in the remaining 30% of the data (ie, the internal test set). External validation using HF controls was also conducted. Pathway analysis of significantly (ie, univariable P <10 −6 ) dysregulated proteins was executed. Signaling pathways with a false discovery rate <0.05 were declared positive. RESULTS: The analysis included 169 cases and 220 controls. A total of 211 discriminant proteins were identified in the training set from the proteomics-based model developed to distinguish ATTR-CM cases from 170 internal controls with hypertensive left ventricular hypertrophy. The area under the receiver-operating characteristic curve to discriminate ATTR-CM in the test set from 50 external controls with HF was 0.89 (95% CI, 0.82–0.96). The sensitivity was 0.90 (95% CI, 0.75–0.97), and the specificity was 0.86 (95% CI, 0.72–0.96). Pathway analysis revealed the PI3K-Akt (phosphoinositide-3-kinase-protein kinase) pathway and its related pathways (eg, JAK-STAT [Janus kinase-signal transducer and activator of transcription]) were dysregulated. Dysregulation of previously identified pathways, such as the complement and coagulation cascade pathways, was also observed. CONCLUSIONS: This study reveals a distinct proteomic profile of ATTR-CM compared with controls with HF, and elucidates both novel and known signaling pathways that are differentially regulated in ATTR-CM.
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Lu et al. (2026) conducted a case-control in Transthyretin amyloid cardiomyopathy (ATTR-CM) (n=550). Transthyretin amyloid cardiomyopathy vs. Controls with hypertensive left ventricular hypertrophy or heart failure was evaluated on Discrimination of ATTR-CM from external controls with heart failure using a proteomics-based model (AUC 0.89, 95% CI 0.82-0.96). A plasma proteomics-based discrimination model successfully distinguished transthyretin amyloid cardiomyopathy from external heart failure controls with an AUC of 0.89.
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