Ca2+-independent alterations in diastolic sarcomere length and relaxation kinetics in a mouse model of lipotoxic diabetic cardiomyopathy

Circ Res. 2009 Jan 2;104(1):95-103. doi: 10.1161/CIRCRESAHA.108.186809. Epub 2008 Nov 20.

Abstract

Previous studies demonstrated increased fatty acid uptake and metabolism in MHC-FATP transgenic mice that overexpress fatty acid transport protein (FATP)1 in the heart under the control of the alpha-myosin heavy chain (alpha-MHC) promoter. Doppler tissue imaging and hemodynamic measurements revealed diastolic dysfunction, in the absence of changes in systolic function. The experiments here directly test the hypothesis that the diastolic dysfunction in MHC-FATP mice reflects impaired ventricular myocyte contractile function. In vitro imaging of isolated adult MHC-FATP ventricular myocytes revealed that mean diastolic sarcomere length is significantly (P<0.01) shorter than in wild-type (WT) cells (1.79+/-0.01 versus 1.84+/-0.01 microm). In addition, the relaxation rate (dL/dt) is significantly (P<0.05) slower in MHC-FATP than WT myocytes (1.58+/-0.09 versus 1.92+/-0.13 microm/s), whereas both fractional shortening and contraction rates are not different. Application of 40 mmol/L 2,3-butadionemonoxime (a nonspecific ATPase inhibitor that relaxes actin-myosin interactions) increased diastolic sarcomere length in both WT and MHC-FATP myocytes to the same length, suggesting that MHC-FATP myocytes are partially activated at rest. Direct measurements of intracellular Ca(2+) revealed that diastolic [Ca(2+)](i) is unchanged in MHC-FATP myocytes and the rate of calcium removal is unexpectedly faster in MHC-FATP than WT myocytes. Moreover, diastolic sarcomere length in MHC-FATP and WT myocytes was unaffected by removal of extracellular Ca(2+) or by buffering of intracellular Ca(2+) with the Ca(2+) chelator BAPTA (100 micromol/L), indicating that elevated intracellular Ca(2+) does not underlie impaired diastolic function in MHC-FATP ventricular myocytes. Functional assessment of skinned myocytes, however, revealed that myofilament Ca(2+) sensitivity is markedly increased in MHC-FATP, compared with WT, ventricular cells. In addition, biochemical experiments demonstrated increased expression of the beta-MHC isoform in MHC-FATP, compared with WT ventricles, which likely contributes to the slower relaxation rate observed in MHC-FATP myocytes. Collectively, these data demonstrate that derangements in lipid metabolism in MHC-FATP ventricles, which are similar to those observed in the diabetic heart, result in impaired diastolic function that primarily reflects changes in myofilament function, rather than altered Ca(2+) cycling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / physiology
  • Chelating Agents / pharmacology
  • Diabetes Complications / pathology
  • Diabetes Complications / physiopathology*
  • Diacetyl / analogs & derivatives
  • Diacetyl / pharmacology
  • Diastole
  • Disease Models, Animal
  • Egtazic Acid / analogs & derivatives
  • Egtazic Acid / pharmacology
  • Fatty Acid Transport Proteins / genetics
  • Fatty Acid Transport Proteins / physiology*
  • Fatty Acids / metabolism*
  • Heart Failure, Diastolic / pathology
  • Heart Failure, Diastolic / physiopathology*
  • Heart Ventricles / pathology
  • Isometric Contraction
  • Mice
  • Mice, Transgenic
  • Myocardial Contraction
  • Myocardium / metabolism
  • Myocytes, Cardiac / drug effects
  • Myocytes, Cardiac / physiology*
  • Myocytes, Cardiac / ultrastructure
  • Myosin Heavy Chains / biosynthesis
  • Myosin Heavy Chains / genetics
  • Recombinant Fusion Proteins / physiology
  • Sarcomeres / drug effects
  • Sarcomeres / ultrastructure*

Substances

  • Chelating Agents
  • Fatty Acid Transport Proteins
  • Fatty Acids
  • Recombinant Fusion Proteins
  • Slc27a1 protein, mouse
  • diacetylmonoxime
  • Egtazic Acid
  • Myosin Heavy Chains
  • 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid
  • Diacetyl
  • Calcium