EDA-fibronectin defines an early molecular target for imaging cardiac remodeling

Fibrotic remodeling is a primary driver of heart failure, yet early molecular events remain difficult to detect non-invasively. Cellular fibronectin (cFN), an alternatively spliced fibronectin isoform containing the extra domain A (EDA), is rapidly induced during early tissue repair and precedes collagen deposition. This study identifies the molecular target responsible for myocardial uptake of 18 F-fluoroglucaric acid (FGA) and determines whether this tracer can report early extracellular matrix remodeling associated with cardiac injury. We employed an integrated approach combining quantitative SILAC-based proteomics, microscale thermophoresis (MST), and competitive binding assays. Using a biotinylated surrogate (BGA), tracer kinetics and target specificity were evaluated in human AC16 cardiomyocytes under ischemic and profibrotic stress. In vivo validation was performed using PET/CT imaging and biodistribution studies in murine models of cardiac injury, including isoproterenol-induced cardiomyopathy and autoimmune myocarditis. Proteomic profiling identified fibronectin as the primary interacting partner of surrogate BGA. MST revealed that FGA binds cFN with submicromolar affinity (Kd ≈ 0.42 µM), while showing substantially weaker, micromolar-range binding to plasma fibronectin (Kd ≈ 7.6 µM). In vivo, 18 F-FGA uptake was significantly elevated in damaged myocardium and strongly correlated with EDA-FN expression (r 2 = 0.92; Pearson r = 0.958, 95% CI 0.661–0.996; p = 0.0026, n = 6). Temporal analyses in cellular and tissue models indicated that cFN induction and BGA accumulation occur early in fibrogenesis, preceding significant collagen deposition. 18 F-FGA preferentially and EDA-dependently associates with cFN, a marker of early extracellular matrix activation, supporting its potential as a candidate PET probe for early cardiac remodeling. Direct characterization of the binding interface and longitudinal in vivo studies will be required to confirm detection of a pre-fibrotic state.

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Publication Details

Journal
Journal of Translational Medicine
Published
2026-08-25
DOI
https://doi.org/10.1186/s12967-026-08850-3
Primary Topic
Cardiac Fibrosis and Remodeling
Type
article
Field-Weighted Citation Impact
0.00

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article

EDA-fibronectin defines an early molecular target for imaging cardiac remodeling

Vibhudutta Awasthi, Venkateswararao Eeda, Andria Hedrick, Tarun W. Dasari et al.
Journal of Translational Medicine
Cardiac Fibrosis and Remodeling
article

EDA-fibronectin defines an early molecular target for imaging cardiac remodeling

Vibhudutta Awasthi, Venkateswararao Eeda, Andria Hedrick, Tarun W. Dasari, Hung Anh Nguyen, Andrea S. Ramirez-Sagredo, Maitreyee Das
article en

Abstract

Fibrotic remodeling is a primary driver of heart failure, yet early molecular events remain difficult to detect non-invasively. Cellular fibronectin (cFN), an alternatively spliced fibronectin isoform containing the extra domain A (EDA), is rapidly induced during early tissue repair and precedes collagen deposition. This study identifies the molecular target responsible for myocardial uptake of 18 F-fluoroglucaric acid (FGA) and determines whether this tracer can report early extracellular matrix remodeling associated with cardiac injury. We employed an integrated approach combining quantitative SILAC-based proteomics, microscale thermophoresis (MST), and competitive binding assays. Using a biotinylated surrogate (BGA), tracer kinetics and target specificity were evaluated in human AC16 cardiomyocytes under ischemic and profibrotic stress. In vivo validation was performed using PET/CT imaging and biodistribution studies in murine models of cardiac injury, including isoproterenol-induced cardiomyopathy and autoimmune myocarditis. Proteomic profiling identified fibronectin as the primary interacting partner of surrogate BGA. MST revealed that FGA binds cFN with submicromolar affinity (Kd ≈ 0.42 µM), while showing substantially weaker, micromolar-range binding to plasma fibronectin (Kd ≈ 7.6 µM). In vivo, 18 F-FGA uptake was significantly elevated in damaged myocardium and strongly correlated with EDA-FN expression (r 2 = 0.92; Pearson r = 0.958, 95% CI 0.661–0.996; p = 0.0026, n = 6). Temporal analyses in cellular and tissue models indicated that cFN induction and BGA accumulation occur early in fibrogenesis, preceding significant collagen deposition. 18 F-FGA preferentially and EDA-dependently associates with cFN, a marker of early extracellular matrix activation, supporting its potential as a candidate PET probe for early cardiac remodeling. Direct characterization of the binding interface and longitudinal in vivo studies will be required to confirm detection of a pre-fibrotic state.

Journal of Translational Medicine
Oklahoma City University (US), University of Oklahoma (US)
National Heart, Lung, and Blood Institute
Good health and well-being
Openalex Percentile: Top 10%
Cardiac Fibrosis and Remodeling
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