Search bioRxiv⌕ Search

bioRxiv · 10.64898/2025.12.17.694596

Short-term but not long-term triiodothyronine treatment improved cardiac function after myocardial infarction in male wild-type mice

Abstract

ObjectivesThyroid hormone (TH), especially triiodothyronine (T3), plays an important role in cardiac physiology and in the remodeling process following myocardial infarction (MI). We investigated the effects of short-term (until day 5) and long-term (until day 56) post-MI T3 treatment on cardiac function, infarct size, hypertrophy, and gene expression in mice without and with deletion of TR, the main cardiac thyroid hormone receptor (wild-type (WT) and TRKO, respectively) MethodsWT and TRKO mice underwent permanent left anterior descending coronary artery (LAD) ligation or sham surgery followed by either short-term T3 for 5 days post-MI or long-term T3 until day 56, including a subgroup in which T3 treatment commenced 14 days post-MI; all groups were followed up for 4 weeks. T3 was delivered via drinking water at 500 ng/ml. Cardiac function was studied with echocardiography (ejection fraction, EF), infarct size by histology (Sirius red), heart weight normalized to tibia length, and transcriptomic profiling (RNA-seq) in WT hearts. ResultsShort-term T3 improved EF in WT but not in TRKO mice without induction of hypertrophy or changes in infarct size in either genotype. Long-term T3 induced cardiac hypertrophy in both WT and TRKO mice. However, long-term T3 did not improve EF or reduce infarct size. In TRKO mice, baseline EF post-MI was preserved without T3, but T3 treatment decreased EF. RNA-seq in long-term treated WT mice suggested modulation of Rho-GTPase signaling, mitochondrial biogenesis, and immune activation by T3. ConclusionsT3 therapy post-MI improved cardiac function only when applied acutely and for a short term. Long-term exposure led to cardiac hypertrophy without functional improvement and may even worsen cardiac function in TR-deficient settings. Timing, duration, and receptor status are highly relevant for TH-based interventions in MI.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Grund, S. C., Dörr, S., Hönes, G. S., Prinz, A. D., Wenzek, C., Köster, J., Möller, L. C., Lorenz, K., Führer, D.. 2025-12-19. Short-term but not long-term triiodothyronine treatment improved cardiac function after myocardial infarction in male wild-type mice. https://doi.org/10.64898/2025.12.17.694596

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Rad and Phospholamban are Key Drivers of the Ventricular Adrenergic Response and Stress-Induced Arrhythmia

The adrenergic response is a fundamental mechanism that regulates heart rate (chronotropy), cardiac contractility (inotropy) and relaxation (lusitropy). Adrenergic stress is also a recognized trigger of arrhythmia in disease. Yet, our understanding of the underlying molecular basis remains incomplete. Protein kinase A (PKA) and the calcium/calmodulin-dependent kinase II (CaMKII) phosphorylate multiple targets proposed to participate in the adrenergic response, including the GTP-binding protein Rad, phospholamban (PLB) and ryanodine receptor 2 (RyR2). Here we demonstrate that phosphorylation of both Rad and PLB is necessary for inotropy and lusitropy. We show that changes in cardiac contractility and relaxation are primarily dependent on intracellular calcium handling. Finally, we report that Rad and PLB control stress-induced arrhythmogenesis, despite the phosphorylation of other pro-arrhythmic targets. We have identified the essential molecular components of the adrenergic response, resolving a long-standing debate in cardiac excitation-contraction coupling and refining current models of sympathetic regulation in health and disease.

physiology↗

MCT6 is an intestinal Lac-Phe exporter required for metformin-associated weight loss

Metabolites are increasingly recognized as circulating molecules that regulate physiology, yet the mechanisms that couple intracellular production to organism-wide action remain poorly defined. Using the anorexigenic metabolite Lac-Phe as a tractable system, we identify the orphan transporter MCT6 (SLC16A5) as a physiologic intestinal Lac-Phe exporter. This mechanism controls the extent to which intracellularly synthesized Lac-Phe acquires systemic activity. MCT6 transports Lac-Phe, mediates its cellular efflux, and is required for maintaining its blood levels in mice following strong glycolytic stimuli. Both global and intestinal epithelial-specific deletion of MCT6 confers resistance to metformin-associated weight loss on a high-fat diet. Bypassing the transport defect with exogenous Lac-Phe normalizes the body weight phenotype of MCT6-KO mice. Together, these data connect MCT6 to metformin pharmacology and intestinal lactate metabolism, and more generally underscore the importance of transporter-mediated release in the conversion of an intracellular metabolic state into a circulating metabolite effector.

physiology↗

DEPP1 connects nutrient and oxygen availability to maintenance of muscle mass

Nutrients and oxygen are sensed within the muscle to control growth and disruption of either signal is sufficient to lead to muscle atrophy. While nutrient limitation is sensed via a conserved transcriptional atrophy program (commonly referred to as atrogenes) dictated via the Forkhead box O (FoxO) transcription factors, how low oxygen promotes muscle loss remains unknown. Accordingly, the downstream mechanisms that initiate muscle loss when oxygen and nutrients are limiting are only partly understood. Here, we find Hypoxia Inducible Factor (HIF), the master regulator of our adaptation to low oxygen, is necessary and sufficient to mediate muscle loss under hypoxia in mice. RNA sequencing in skeletal muscle isolated from starved or hypoxic mice identifies Decidual Protein Induced by Progesterone 1 (Depp1), which is induced in skeletal muscle when nutrients or oxygen is limiting via FoxO1 and HIF activation, respectively. Whole body Depp1 loss in mice reduces muscle loss under fasting and hypoxia and skeletal muscle Depp1 overexpression is sufficient to mediate muscle atrophy. Mechanistically, Depp1 localizes to the mitochondria and is necessary to control autophagy activation and mitochondrial degradation in skeletal muscle. Taken together, our studies nominate Depp1 as a new atrogene necessary for muscle loss under multiple atrophy scenarios involving FoxO and HIF.

physiology↗