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Cardioselective dominant-negative thyroid hormone receptor (Delta337T) modulates myocardial metabolism and contractile efficiency.
Hyyti, Outi M; Olson, Aaron K; Ge, Ming; Ning, Xue-Han; Buroker, Norman E; Chung, Youngran; Jue, Thomas; Portman, Michael A.
Affiliation
  • Hyyti OM; Children's Hospital and Regional Medical Center MSW 4841, 4800 Sand Point Way NE, Seattle, WA 98105, USA.
Am J Physiol Endocrinol Metab ; 295(2): E420-7, 2008 Aug.
Article in En | MEDLINE | ID: mdl-18523124
Dominant-negative thyroid hormone receptors (TRs) show elevated expression relative to ligand-binding TRs during cardiac hypertrophy. We tested the hypothesis that overexpression of a dominant-negative TR alters cardiac metabolism and contractile efficiency (CE). We used mice expressing the cardioselective dominant-negative TRbeta(1) mutation Delta337T. Isolated working Delta337T hearts and nontransgenic control (Con) hearts were perfused with (13)C-labeled free fatty acids (FFA), acetoacetate (ACAC), lactate, and glucose at physiological concentrations for 30 min. (13)C NMR spectroscopy and isotopomer analyses were used to determine substrate flux and fractional contributions (Fc) of acetyl-CoA to the citric acid cycle (CAC). Delta337T hearts exhibited rate depression but higher developed pressure and CE, defined as work per oxygen consumption (MVo(2)). Unlabeled substrate Fc from endogenous sources was higher in Delta337T, but ACAC Fc was lower. Fluxes through CAC, lactate, ACAC, and FFA were reduced in Delta337T. CE and Fc differences were reversed by pacing Delta337T to Con rates, accompanied by an increase in FFA Fc. Delta337T hearts lacked the ability to increase MVo(2). Decreases in protein expression for glucose transporter-4 and hexokinase-2 and increases in pyruvate dehydrogenase kinase-2 and -4 suggest that these hearts are unable to increase carbohydrate oxidation in response to stress. These data show that Delta337T alters the metabolic phenotype in murine heart by reducing substrate flux for multiple pathways. Some of these changes are heart rate dependent, indicating that the substrate shift may represent an accommodation to altered contractile protein kinetics, which can be disrupted by pacing stress.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetyl Coenzyme A / Thyroid Hormone Receptors beta / Myocardial Contraction / Myocardium Limits: Animals Language: En Journal: Am J Physiol Endocrinol Metab Journal subject: ENDOCRINOLOGIA / FISIOLOGIA / METABOLISMO Year: 2008 Document type: Article Affiliation country: Estados Unidos Country of publication: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetyl Coenzyme A / Thyroid Hormone Receptors beta / Myocardial Contraction / Myocardium Limits: Animals Language: En Journal: Am J Physiol Endocrinol Metab Journal subject: ENDOCRINOLOGIA / FISIOLOGIA / METABOLISMO Year: 2008 Document type: Article Affiliation country: Estados Unidos Country of publication: Estados Unidos