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Taegtmeyer, H.

Publications and source records attributed to Taegtmeyer, H..

4 recordsLinked to original sources

Estrogen-Deficiency Degrades Left Ventricular Diastolic Function and Energy Metabolism in Hypertensive Female Mice

AimsHeart failure (HF) due to diastolic dysfunction (DD) but normal left ventricular (LV) ejection fraction (EF) is termed HF with preserved EF (HFpEF). Given its high prevalence in post-menopausal women, we hypothesized that 17{beta}-estradiol (E2) function is mechanistically linked to DD HF and investigated E2-deficiency in the etiology of DD in a mouse model. MethodsFemale C57BL/6J mice were divided into one group with hypertension induced by N({omega})-nitro-L-arginine methyl ester (L) and cardiac pressure overload induced by angiotensin II (A), collectively inducing DD, and one group with sham treatment. Groups were subdivided to receive an ovariectomy (OVX) to induce estrogen-deficiency and emulate menopause or sham surgery. During the next 21 days, mice were tested for cardiac function, food intake, response to E2 agonists, gene profiling, cardiomyocyte-contractility and elasticity, and cardiac mitochondrial function. ResultsOVX-associated E2-deficiency exacerbated DD in a time-dependent way without affecting EF or stroke volume, emulating a severe DD phenotype. These changes paralleled those for mitochondrial dysfunction, i.e., upregulation of genes associated with stress, energy metabolism, and fibrosis, as well as functional and structural defects in cardiomyocytes. Treatment of OVX + (L + A) with E2 or a G-protein-coupled estrogen receptor agonist normalized diastolic function, whereas estrogen receptor beta agonists did not. The OVX DD mice exhibited moderately impaired mitochondrial function, which delayed cardiomyocyte relaxation but not contraction, altered cardiac substrate utilization, reduced cardiomyocyte elasticity, increased production of reactive oxygen species, and potentiated extracellular fibrosis. ConclusionsOVX-induced E2-deficiency generates metabolic, structural, and functional changes in cardiomyocytes and the adjacent extracellular matrix, exacerbating the effects of L and A on diastolic function. This robust DD model revealed a role for E2 via ER in diastole-regulation in female mice and raised questions about similar mechanisms operative in postmenopausal women. HIGHLIGHTSO_LIOvariectomy (OVX)-induced estrogen-deficiency exacerbated diastolic dysfunction (DD) induced by hypertension and pressure overload with preserved ejection fraction in female C57BL/6J mice. C_LIO_LIIn post-OVX-treated DD mice, heart weight and fibrosis preceded other metrics of cardiac dysfunction. C_LIO_LIOVX-induced estrogen-deficiency increased the expression of genes associated with stress, energy metabolism, and especially fibrosis. C_LIO_LIMetabolic imaging of the heart by positron emission tomography revealed that DD with preserved ejection fraction was associated with mitochondrial dysfunction presenting as increased accretion of cardiac energy substrates, [18F]deoxyglucose and [11C]palmitate, effects that worsened following OVX. C_LIO_LIOVX increased cardiomyocyte stiffness and fibrosis and reduced cardiomyocyte lengthening and compliance in the context of female DD. C_LIO_LIImproved diastolic function following delivery of GPER agonists or estradiol to OVX DD female mice implicates estrogen receptor in the maintenance of normal cardiac function. C_LI

physiology↗

Reductive carboxylation via isocitrate dehydrogenase 1 supports cardiac metabolic adaptation during oncometabolic stress.

BackgroundCardiovascular disease and cancer are the two leading causes of morbidity and mortality worldwide. Metabolic dysregulation of cancer cells extends beyond the tumor microenvironment and increases the risk for cardiovascular diseases. One common somatic mutation in cancer cells affects isocitrate dehydrogenase (IDH) 1 and 2, which catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate in the cytosol and mitochondria, respectively. IDH1 and 2 mutations cause the production of the oncometabolite D-2-hydroxyglutarate (D2-HG), which allosterically inhibits -ketoglutarate dehydrogenase (-KGDH) and is associated with reduced cardiac contractile function. MethodsWe combined stable isotope tracer studies with computational modeling to investigate the fundamental role of IDH isoforms in cardiac adaptation under oncometabolic stress. ResultsWe uncovered an unexpected cardiac phenotype that expands the role of IDH1 in the heart beyond oxidative metabolism. We quantified the stable isotopomer distributions from glucose and glutamine in perfused working rat hearts and isolated adult ventricular cardiomyocytes using mass spectrometry-based metabolomics. Our analysis revealed that defective mitochondrial metabolism causes the redirection of carbon flux from oxidative towards reductive pathways. Reductive carboxylation of -KGDH increases glutamine uptake and glutamine-derived citrate formation in working rat heart perfusions and cultured adult mouse ventricular cardiomyocytes. To identify which IDH isoform is responsible for redirecting carbon flux, we developed knockout models of IDH1, IDH2, and IDH3 in adult mouse ventricular cardiomyocytes. Loss of IDH1 expression impaired the reductive formation of citrate and caused functional defects in cardiomyocytes. Lastly, epigenetic analyses of histone marks revealed that IDH1 induces widespread alterations in histone acetylation and tri-methylation. ConclusionOur results highlight a novel role for IDH1 in cardiac metabolism and transcriptional control of metabolic adaptation to tumor-mediated stress and provide evidence that reductive-citrate formation may induce epigenetic modifications in the heart.

systems biology↗

ATP-dependent citrate lyase Drives Left Ventricular Dysfunction by Metabolic Remodeling of the Heart

BackgroundMetabolic remodeling is a hallmark of the failing heart. Oncometabolic stress during cancer increases the activity and abundance of the ATP-dependent citrate lyase (ACL, Acly), which promotes histone acetylation and cardiac adaptation. ACL is critical for the de novo synthesis of lipids, but how these metabolic alterations contribute to cardiac structural and functional changes remains unclear. MethodsWe utilized human heart tissue samples from healthy donor hearts and patients with hypertrophic cardiomyopathy. Further, we used CRISPR/Cas9 gene editing to inactivate Acly in cardiomyocytes of MyH6-Cas9 mice. In vivo, positron emission tomography and ex vivo stable isotope tracer labeling were used to quantify metabolic flux changes in response to the loss of ACL. We conducted a multi-omics analysis using RNA-sequencing and mass spectrometry-based metabolomics and proteomics. Experimental data were integrated into computational modeling using the metabolic network CardioNet to identify significantly dysregulated metabolic processes at a systems level. ResultsHere, we show that in mice, ACL drives metabolic adaptation in the heart to sustain contractile function, histone acetylation, and lipid modulation. Notably, we show that loss of ACL increases glucose oxidation while maintaining fatty acid oxidation. Ex vivo isotope tracing experiments revealed a reduced efflux of glucose-derived citrate from the mitochondria into the cytosol, confirming that citrate is required for reductive metabolism in the heart. We demonstrate that YAP inactivation facilitates ACL deficiency. Computational flux analysis and integrative multi-omics analysis indicate that loss of ACL induces alternative isocitrate dehydrogenase 1 flux to compensate. ConclusionsThis study mechanistically delineates how cardiac metabolism compensates for suppressed citrate metabolism in response to ACL loss and uncovers metabolic vulnerabilities in the heart.

molecular biology↗

Oncometabolism Drives Autophagy Activation in Skeletal Muscle

About 20-30% of cancer-associated deaths are due to complications from cachexia which is characterized by skeletal muscle atrophy. Metabolic reprogramming in cancer cells causes body-wide metabolic and proteomic remodeling, which remain poorly understood. Here, we present evidence that the oncometabolite D-2-hydroxylgutarate (D2-HG) impairs NAD+ redox homeostasis in skeletal myotubes, causing atrophy via deacetylation of LC3-II by the nuclear deacetylase Sirt1. Overexpression of p300 or silencing of Sirt1 abrogate its interaction with LC3, and subsequently reduced levels of LC3 lipidation. Using RNA-sequencing and mass spectrometry-based metabolomics and proteomics, we demonstrate that prolonged treatment with the oncometabolite D2-HG in mice promotes cachexia in vivo and increases the abundance of proteins and metabolites, which are involved in energy substrate metabolism, chromatin acetylation and autophagy regulation. We further show that D2-HG promotes a sex-dependent adaptation in skeletal muscle using network modeling and machine learning algorithms. Our multi-omics approach exposes new metabolic vulnerabilities in response to D2-HG in skeletal muscle and provides a conceptual framework for identifying therapeutic targets in cachexia.

systems biology↗