Abstract 565: The Activation of AMP-Activated Protein Kinase Ameliorates the Severity of Heart Failure in Dogs

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Hideyuki Sasaki ◽  
Hiroshi Asanuma ◽  
Masashi Fujita ◽  
Hiroyuki Takahama ◽  
Masakatsu Wakeno ◽  
...  
Keyword(s):  
Heart Failure ◽  
Protein Kinase ◽  
Cardiac Myocytes ◽  
Left Ventricular ◽  
Neonatal Rat ◽  
Cellular Damage ◽  
Control Group ◽  
Compound C ◽  
Rapid Pacing ◽  
Amp Activated Protein Kinase

Backgrounds; Since AMP-activated protein kinase (AMPK) is activated in the pressure-overloaded hypertrophic hearts, we investigated whether the activation of AMPK caused by metformin attenuates the progression of heart failure induced by rapid pacing in dogs and decreases cellular damage caused by oxidative stress in neonatal rat cardiac myocytes. Methods and Results; Heart failure was induced by right ventricular (RV) pacing at 230 bpm for 4 weeks in dogs. Treatment of dogs with metformin (100mg/kg/day, orally, n=8, Met group) for 4 weeks prevented significantly the progression of pacing-induced heart failure evaluated by echocardiographical and hemodynamic measurement compared with the control group (n=8). Left ventricular (LV) diastolic and systolic dimension (LVDd and LVDs) were smaller (32.8±0.4 and 26.7±0.9 mm, respectively) and fractional shortening (FS) and ejection fraction (EF) were preserved in Met group (18.6±1.8 and 45.5±3.5 %, respectively) compared with the control group (LVDd and LVDs; 36.5±1.0 and 33.0±1.0 mm, FS and EF; 9.6±0.7 and 27.0±1.9 %, p<0.05 vs. Met group each). Furthermore, both pulmonary capillary wedge pressure (PCWP) and mean pulmonary arterial pressure (mPA) were significantly lower in Met group (11.1±0.9 and 18.1±1.4 mmHg, respectively) compared with the control group (21.0±2.2 and 26.8±2.8 mmHg, respectively). Treatment of cultured cardiac myocytes with a maximal physiological concentration of metformin (10μmol/L) attenuated the cellular damage against H 2 O 2 exposure (50μmol/L). These effects were blunted by an AMPK inhibitor, compound-C (20μmol/L), suggesting that the activation of AMPK increased the cellular viability during H 2 O 2 exposure. Conclusions; Metformin that activates AMPK prevented the progression of heart failure induced by rapid pacing in dogs and attenuated the cellular damage against H 2 O 2 exposure in cardiac myocytes. AMPK may be one of new targets for preventing heart failure in clinical settings.

Abstract 337: Activation of Myocardial AMP-activated Protein Kinase by Metformin Prevents Progression of Heart Failure in Dogs; Involvement of eNOS Activation

Circulation ◽  
2008 ◽  
Vol 118 (suppl_18) ◽  
Author(s):  
Hideyuki Sasaki ◽  
Hiroshi Asanuma ◽  
Masashi Fujita ◽  
Hiroyuki Takahama ◽  
Masanori Asakura ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Nitric Oxide ◽  
Heart Failure ◽  
Cell Death ◽  
Protein Kinase ◽  
Left Ventricular ◽  
Vehicle Group ◽  
Mrna Levels ◽  
Compound C ◽  
Amp Activated Protein Kinase

Background; Several studies have shown that metformin activates AMP-activated protein kinase (AMPK), which mediates potent cardioprotection against ischemia-reperfusion injury. AMPK is also activated in experimental failing myocardium, suggesting that activation of AMPK is beneficial for the pathophysiology of heart failure. We investigated whether metformin prevents oxidative stress-induced cell death in rat cardiomyocytes and attenuates the progression of heart failure in dogs. Methods and Results; The treatment with metformin (10 μmol/L) protected the rat cultured cardiomyocytes against cell death due to H 2 O 2 exposure (50 μmol/L) as indicated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT), TUNEL staining, and flow cytometry. These effects were blunted by an AMPK inhibitor, compound-C (20 μmol/L), suggesting that the activation of AMPK decreased the extent of apoptosis-induced cell death due to H 2 O 2 exposure. Continuous rapid ventricular pacing (230/min for 4 weeks) in dogs caused heart failure and the treatment with metformin (100 mg/kg/day PO, n=8) decreased left ventricular (LV) end-diastolic dimension (32.8±0.4 vs. 36.5±1.0 mm, p< 0.01) and pressure (11.8±1.1 vs. 22±0.9 mmHg, p< 0.01), and increased LV fractional shortening (18.6±1.8 vs. 9.6±0.7 %, p< 0.01) along with enhanced phosphorylation of AMPK and the decreased the number of TUNEL-positive cells of the LV myocardium compared with the vehicle group (n=8). Interestingly, metformin increased the protein and mRNA levels of endothelial nitric oxide synthase of the LV myocardium and plasma nitric oxide levels. Metformin improved the plasma insulin resistance without increased myocardial GLUT-4 translocation. Furthermore, the subcutaneous administration of AICAR (50 mg/kg/every other day), another AMPK activator mediated the equivalent effects to metformin, strengthening the pivotal role of AMPK in reduction of apoptosis and prevention of heart failure. Conclusions; Activation of myocardial AMPK attenuated the oxidative stress-induced cardiomyocyte apoptosis and prevented the progression of heart failure in dogs, along with eNOS activation. Thus, metformin or AICAR may be applicable as a novel therapy for heart failure.

Abstract 2423: B-type Natriuretic Peptide Upregulates Erythropoietin Receptor Gene Expression via Protein Kinase G in Heart Failure

Circulation ◽  
2008 ◽  
Vol 118 (suppl_18) ◽  
Author(s):  
Yoshiaki Ohyama ◽  
Toru Tanaka ◽  
Takehisa Shimizu ◽  
Hiroshi Doi ◽  
Norimichi Koitabashi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heart Failure ◽  
Protein Kinase ◽  
Cardiac Myocytes ◽  
Natriuretic Peptide ◽  
Neonatal Rat ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Failing Heart ◽  
Epor Expression

Backgroud: Recent studies demonstrated non-hematopoietical effects of Erythropoietin (Epo) and its receptor (EpoR) in a variety of tissues including cardiovascular system. Epo treatment improves cardiac function in patients with heart failure and reduces infarct size after ischemia/reperfusion injury in the heart. However, little attention has been paid for the endogenous regulatory mechanisms regulating EpoR expression. In this study, we hypothesize that B-type natriuretic peptide upregulates EpoR gene expression in failing heart. Methods and Results: Wister rats underwent transverse aortic constriction surgery to induce hypertrophy. RT-PCR analyses of those rats showed that EpoR mRNA levels were increased in the left ventricle and positively correlated with the levels of BNP mRNA (n=10, r=0.67, p<0.05). Next we examined the expression of EpoR in human failing heart by using autopsy specimens and found that EpoR mRNA levels were significantly elevated in patients with dilated cardiomyopathy compared with those in normal heart. Immunohistochemistry of endomyocardial biopsy specimens of failing heart (n=54) showed that EpoR mRNA levels were correlated with severity of cardiac dysfunction estimated by diameter of cardiac chambers, pathomorphology, serum BNP concentration and functional class of New York Heart Association. Interestingly, stimulation of cultured neonatal rat cardiac myocytes with BNP, but not with hypertrophic reagents including endothelin I, angiotensin II and norepinephrine, significantly increased the EpoR mRNA levels in a time-dependent manner. Overexpression of cGMP-dependent protein kinase (PKG) increased EpoR transcript in cultured cardiac myocytes. BNP-induced EpoR expression was abrogated in the presence of KT5823, a specific inhibitor for PKG. Conclusion: These results suggest a role for BNP in mediating an induction of EpoR expression in failing myocardium and indicate that the cardiac EpoR gene is a target of cGMP/PKG signaling.

Abstract 1574: Low Myocardial Protein Kinase G Activity Raises Cardiomyocyte Resting Tension in Diastolic Heart Failure

Circulation ◽  
2008 ◽  
Vol 118 (suppl_18) ◽  
Author(s):  
Loek van Heerebeek ◽  
Nazha Hamdani ◽  
Martin L Handoko ◽  
Jolanda van der Velden ◽  
Ger J Stienen ◽  
...  
Keyword(s):  
Heart Failure ◽  
Protein Kinase ◽  
Diastolic Heart Failure ◽  
Left Ventricular ◽  
Volume Index ◽  
Protein Kinase G ◽  
Control Group ◽  
Resting Tension ◽  
Vitro Effect

Cardiomyocytes (CM) of diastolic heart failure (DHF) patients (pts) are hypertrophied and have high diastolic resting tension (RT), which elevates left ventricular (LV) diastolic stiffness. In rodent LV pressure overload models, development of pathological CM hypertrophy has been related to low myocardial protein kinase G (PKG) activity. Myocardial PKG activity and in-vitro effect of PKG on RT of isolated CM were therefore determined using LV endomyocardial biopsies procured from DHF pts. All DHF pts (n=36) had been admitted to hospital for worsening heart failure (NYHA 3– 4), were free of coronary artery disease, had a LV ejection fraction > 50%, a LV end-diastolic volume index < 97 ml/m 2 , a LV end-diastolic pressure > 16 mmHg and no histological evidence in the biopsies of myocardial infiltration or inflammation. Myocardial PKG activity was assessed by immunohistochemistry using antibodies against the specific PKG substrate vasodilator stimulated phosphoprotein (VASP) and against phosphorylated VASP ((P)-VASP). Myocardial PKG activity corresponded to the ratio of (P)-VASP/VASP. CM were isolated from the biopsies, treated with Triton X-100 to remove all membranes, attached to a force transducer and stretched to 2.2 μm to measure RT. In DHF pts, (P)-VASP/VASP ratio (0.67±0.15) was lower than in a control group (n=22) (0.98±0.19; p<0.0001). CM isolated from LV myocardium of DHF pts had higher RT (7.2±0.5 kN/m 2 ) than CM of a control group (4.8±0.2 kN/m 2 ; p<0.0001). In-vitro administration of PKG lowered RT of CM of DHF pts to levels similar to the control group (PKG: 4.0±0.7 kN/m 2 ; p<0.01). Subsequent treatment with PKA did not further decrease RT (3.8±0.9 kN/m 2 ). DHF patients had low myocardial PKG activity. This low myocardial PKG activity could have elevated RT of CM as in-vitro administration of PKG corrected the high RT. Absence of an additional in-vitro effect of PKA after PKG suggested that high RT results from hypophosphorylation of myofilamentary proteins, whose phosphorylation sites are targets for both PKA and PKG. In pts with DHF, phosphodiesterase 5A inhibition could raise myocardial PKG activity and thereby correct their high CM RT, which is an important determinant of their high diastolic LV stiffness.

scholarly journals Activation of AMP-Activated Protein Kinase by Metformin Improves Left Ventricular Function and Survival in Heart Failure

2009 ◽  
Vol 104 (3) ◽  
pp. 403-411 ◽  
Author(s):  
Susheel Gundewar ◽  
John W. Calvert ◽  
Saurabh Jha ◽  
Iris Toedt-Pingel ◽  
Sang Yong Ji ◽  
...  
Keyword(s):  
Heart Failure ◽  
Protein Kinase ◽  
Left Ventricular Function ◽  
Ventricular Function ◽  
Left Ventricular ◽  
Amp Activated Protein Kinase

Abstract 259: Dysregulation of AMP-activated Protein Kinase-alpha Isoforms in Left Ventricular Myocardium of Dogs With Chronic Heart Failure

2020 ◽  
Vol 127 (Suppl_1) ◽  
Author(s):  
Ramesh C Gupta ◽  
Vinita Singh-Gupta ◽  
Hani N Sabbah
Keyword(s):  
Heart Failure ◽  
Protein Kinase ◽  
Chronic Heart Failure ◽  
Protein Expression ◽  
Mrna Expression ◽  
Left Ventricular ◽  
Nuclear Fraction ◽  
Α Subunit ◽  
Protein Levels ◽  
Amp Activated Protein Kinase

Background: The adenosine 5′-monophosphate (AMP)-activated protein kinase (AMPK) plays critical roles in regulating cellular growth and metabolism and is activated when cellular ATP levels decrease. The heterotrimeric structure of AMPK consists of a catalytic alpha (α) subunit and regulatory beta (β) and gamma (γ) subunits. The two isoforms of the catalytic α subunit have different cellular localization: AMPKα1 is predominantly found in the non-nuclear fraction and AMPKα2 is found in both the nuclear and the non-nuclear fractions. Both AMPKα isoforms reside in cardiomyocytes, increased expression of AMPKα1 during stress can trigger an increased inflammatory state whereas AMPKα2 has recently been recognized as a regulator of mitophagy, the selective degradation of damaged mitochondria by autophagy. Dysregulation in AMPKα1 and AMPKα2 has been reported in explanted failed human hearts. This study tested the hypothesis that mRNA and protein expression levels of AMPKα1 increase and that of AMPKα2 decrease in LV myocardium of dogs with chronic heart failure (HF) produced by microembolization. Methods: RNA was extracted and sodium dodecyl sulfate (SDS)-extract homogenate prepared from LV tissue of 6 dogs with microembolization-induced HF and 6 normal (NL) dogs. mRNA expression of AMPKα1 and AMPKα2 was measured using real-time PCR and normalized to GAPDH. Protein expression of AMPKα1 and AMPKα2 was measured by Western blotting and normalized to GAPDH. Bands were quantified in densitometric units (du). Results: mRNA and protein levels of GAPDH, used as internal control, were similar between NL and HF dogs. In HF dogs, mRNA expression of AMPKα2 was reduced by 5.09 fold and protein levels were reduced by 2.08 fold (1.02 ± 0.09 vs. 2.12 ± 0.18 du, p<0.05) compared to NL dogs. In HF dogs, AMPKa1 mRNA and protein levels were increased 5.67 fold and 2.09 fold (0.67 ± 0.10 vs. 0.32 ± 0.03 du, p<0.05), respectively compared to NL dogs. Conclusions: The results indicate that in LV myocardium of dogs with chronic HF, mRNA and protein levels for AMPKα1 are upregulated while AMPKα2 levels are downregulated compared to NL dogs. This AMPK isoform shift can trigger abnormalities of mitochondrial respiration and turnover that contribute to an abnormal energetic state characteristic of the failing heart.

Abstract 1478: AMP-Activated Protein Kinase Phosphorylates Cardiac Troponin I and Alters Contractility in Murine Ventricular Myocytes

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
S Marisa Oliveira ◽  
Yin-Hua Zhang ◽  
Joanne Davies ◽  
David Carling ◽  
Barbara Casadei ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Ventricular Myocytes ◽  
Intracellular Localization ◽  
Left Ventricular ◽  
Cardiac Troponin I ◽  
Compound C ◽  
Cardiac Phenotype ◽  
Amp Activated Protein Kinase

In the heart, AMP-activated protein kinase (AMPK) is critical in the regulation of energy balance and in myocardial signaling, and is activated especially during ischaemia and exercise. It is a αβγ heterotrimer, with α being the catalytic subunit. Mutations affecting the regulatory γ2 subunit have been shown to cause a cardiac phenotype of hypertrophy and conduction disease, thus suggesting a specific role for this subunit in the heart. The γ isoforms are highly conserved at their C-termini but very different at their N-termini; hence we have investigated whether the unique N-terminus of γ2 could be involved in conferring substrate specificity or in determining intracellular localization. We have undertaken a GAL4 -based yeast two-hybrid assay to screen a human heart cDNA library using the N-terminal 273 residues of γ2 as bait. Five proteins were identified as true interactors in the yeast assay, one of these being cardiac troponin I (cTnI). In vitro studies showed that cTnI (isolated or reconstituted as troponin complex) is a good substrate for AMPK. Studies using site-specific cTnI mutants and mass spectrometry identified Ser-150 as the principal residue phosphorylated by AMPK. Actomyosin ATPase assays showed that phosphorylation at this residue resulted in increased Ca 2+ sensitivity of contractile regulation (ΔpCa 50 =+0.07). Treatment of cardiomyocytes with the AMPK activator AICAR for 15 min resulted in prolonged relaxation (time to 50% relaxation, TR50) in field stimulated left ventricular myocytes of C57B/6 mice (TR50 in ms: 29.8±1.4 in control and 38.0±2.4 with AICAR, n=11, 3 Hz and 35 o C). There was a tendency towards an increase in contraction with AICAR. Pretreatment of myocytes with AMPK inhibitor compound C (10 μM) abolished the effects of AICAR on myocytes (TR50 in ms: 30.9±1.7 before AICAR and 31.5±2.6 after AICAR, n=9). The effect of AICAR was mediated without altering the amplitude of the Ca 2+ transient, suggesting that it may be caused by a change in myofilament Ca 2+ -sensitivity and consistent with AMPK phosphorylation of cTnI. We hypothesize that cTnI phosphorylation by AMPK may represent a novel mechanism of regulation of cardiac function.

scholarly journals Trimetazidine Attenuates Heart Failure by Improving Myocardial Metabolism via AMPK

2021 ◽  
Vol 12 ◽  
Author(s):  
Hongyang Shu ◽  
Weijian Hang ◽  
Yizhong Peng ◽  
Jiali Nie ◽  
Lujin Wu ◽  
...  
Keyword(s):  
Heart Failure ◽  
Glucose Uptake ◽  
Glucose Transporter ◽  
Myocardial Metabolism ◽  
Pressure Overload ◽  
Left Ventricular ◽  
Neonatal Rat ◽  
Mitochondrial Morphology ◽  
Mouse Heart ◽  
Compound C

Energic deficiency of cardiomyocytes is a dominant cause of heart failure. An antianginal agent, trimetazidine improves the myocardial energetic supply. We presumed that trimetazidine protects the cardiomyocytes from the pressure overload-induced heart failure through improving the myocardial metabolism. C57BL/6 mice were subjected to transverse aortic constriction (TAC). After 4 weeks of TAC, heart failure was observed in mice manifested by an increased left ventricular (LV) chamber dimension, an impaired LV ejection fraction evaluated by echocardiography analysis, which were significantly restrained by the treatment of trimetazidine. Trimetazidine restored the mitochondrial morphology and function tested by cardiac transmission electron microscope and mitochondrial dynamic proteins analysis. Positron emission tomography showed that trimetazidine significantly elevated the glucose uptake in TAC mouse heart. Trimetazidine restrained the impairments of the insulin signaling in TAC mice and promoted the translocation of glucose transporter type IV (GLUT4) from the storage vesicle to membrane. However, these cardioprotective effects of trimetazidine in TAC mice were notably abolished by compound C (C.C), a specific AMPK inhibitor. The enlargement of neonatal rat cardiomyocyte induced by mechanical stretch, together with the increased expression of hypertrophy-associated proteins, mitochondria deformation and dysfunction were significantly ameliorated by trimetazidine. Trimetazidine enhanced the isolated cardiomyocyte glucose uptake in vitro. These benefits brought by trimetazidine were also removed with the presence of C.C. In conclusion, trimetazidine attenuated pressure overload-induced heart failure through improving myocardial mitochondrial function and glucose uptake via AMPK.

The Pattern of Ventricular Remodeling Influences the Level of Oxidative Stress in Heart Failure Patients

2017 ◽  
Vol 68 (7) ◽  
pp. 1506-1511
Author(s):  
Cerasela Mihaela Goidescu ◽  
Anca Daniela Farcas ◽  
Florin Petru Anton ◽  
Luminita Animarie Vida Simiti
Keyword(s):  
Oxidative Stress ◽  
Heart Failure ◽  
Ventricular Remodeling ◽  
Clinical Laboratory ◽  
Left Ventricular ◽  
Control Group ◽  
Reactive Protein ◽  
Lv Mass ◽  
Few Data

Oxidative stress (OS) is increased in chronic diseases, including cardiovascular (CV), but there are few data on its effects on the heart and vessels. The isoprostanes (IsoP) are bioactive compounds, with 8-iso-PGF25a being the most representative in vivo marker of OS. They correlate with the severity of heart failure (HF), but because data regarding OS levels in different types of HF are scarce, our study was aimed to evaluate it by assessing the urinary levels of 8-iso-PGF2aand its correlations with various biomarkers and parameters. Our prospective study included 53 consecutive patients with HF secondary to ischemic heart disease or dilative cardiomyopathy, divided according to the type of HF (acute, chronic decompensated or chronic compensated HF). The control group included 13 hypertensive patients, effectively treated. They underwent clinical, laboratory - serum NT-proBNP, creatinine, uric acid, lipids, C reactive protein (CRP) and urinary 8-iso-PGF2a and echocardiographic assessment. HF patients, regardless the type of HF, had higher 8-iso-PGF2a than controls (267.32pg/�mol vs. 19.82pg/�mol, p[0.001). The IsoP level was directly correlated with ejection fraction (EF) (r=-0.31, p=0.01) and NT-proBNP level (r=0.29, p=0.019). The relative wall thickness (RWT) was negatively correlated with IsoP (r=-0.55, p[0.001). Also 8-iso-PGF25a was higher by 213.59pg/�mol in the eccentric left ventricular (LV) hypertrophy subgroup comparing with the concentric subgroup (p=0.014), and the subgroups with severe mitral regurgitation (MR) and moderate/severe pulmonary hypertension (PAH) had the highest 8-iso-PGF2a levels. Male sex, severe MR, moderate/severe PAH, high LV mass and low RWT values were predictive for high OS level in HF patients.Eccentric cardiac remodeling, MR severity and PAH severity are independent predictors of OS in HF patients.

Cardiac mitofusin-1 is declined in non-responding patients with idiopathic dilated cardiomyopathy

2020 ◽  
Vol 41 (Supplement_2) ◽  
Author(s):  
Y Hsiao ◽  
I Shimizu ◽  
T Wakasugi ◽  
S Jiao ◽  
T Watanabe ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Heart Failure ◽  
Ventricular Myocytes ◽  
Severe Heart Failure ◽  
Left Ventricular ◽  
Neonatal Rat ◽  
Heart Failure Patients ◽  
Underlying Mechanisms ◽  
Neonatal Rat Ventricular Myocytes ◽  
Mitofusin 1

Abstract Background/Introduction Mitochondria are dynamic regulators of cellular metabolism and homeostasis. The dysfunction of mitochondria has long been considered a major contributor to aging and age-related diseases. The prognosis of severe heart failure is still unacceptably poor and it is urgent to establish new therapies for this critical condition. Some patients with heart failure do not respond to established multidisciplinary treatment and they are classified as “non-responders”. The outcome is especially poor for non-responders, and underlying mechanisms are largely unknown. Purpose Studies indicate mitochondrial dysfunction has causal roles for metabolic remodeling in the failing heart, but underlying mechanisms remain to be explored. This study tried to elucidate the role of Mitofusin-1 in a failing heart. Methods We examined twenty-two heart failure patients who underwent endomyocardial biopsy of intraventricular septum. Patients were classified as non-responders when their left-ventricular (LV) ejection fraction did not show more than 10% improvement at remote phase after biopsy. Fourteen patients were classified as responders, and eight as non-responders. Electron microscopy, quantitative PCR, and immunofluorescence studies were performed to explore the biological processes or molecules involved in failure to respond. In addition to studies with cardiac tissue specific knockout mice, we also conducted functional in-vitro studies with neonatal rat ventricular myocytes. Results Twenty-two patients with IDCM who underwent endomyocardial biopsy were enrolled in this study, including 14 responders and 8 non-responders. Transmission electron microscopy (EM) showed a significant reduction in mitochondrial size in cardiomyocytes of non-responders compared to responders. Quantitative PCR revealed that transcript of mitochondrial fusion protein, Mitofusin-1, was significantly reduced in non-responders. Studies with neonatal rat ventricular myocytes (NRVMs) indicated that the beta-1 adrenergic receptor-mediated signaling pathway negatively regulates Mitofusin-1 expression. Suppression of Mitofusin-1 resulted in a significant reduction in mitochondrial respiration of NRVMs. We generated left ventricular pressure overload model with thoracic aortic constriction (TAC) in cardiac specific Mitofusin-1 knockout model (c-Mfn1 KO). Systolic function was reduced in c-Mfn1 KO mice, and EM study showed an increase in dysfunctional mitochondria in the KO group subjected to TAC. Conclusions Mitofusin-1 becomes a biomarker for non-responders with heart failure. In addition, our results suggest that therapies targeting mitochondrial dynamics and homeostasis would become next generation therapy for severe heart failure patients. Funding Acknowledgement Type of funding source: None

scholarly journals A Randomized Controlled Trial to Study the Effect of Yoga Therapy on Cardiac Function and N Terminal Pro BNP in Heart Failure

2014 ◽  
Vol 9 ◽  
pp. IMI.S13939 ◽  
Author(s):  
Bandi Hari Krishna ◽  
Pravati Pal ◽  
G. K. Pal ◽  
J. Balachander ◽  
E. Jayasettiaseelon ◽  
...  
Keyword(s):  
Heart Failure ◽  
Cardiac Function ◽  
Medical Therapy ◽  
Left Ventricular ◽  
Left Ventricular Ejection ◽  
Control Group ◽  
Tei Index ◽  
Ventricular Ejection Fraction ◽  
Yoga Therapy ◽  
Standard Medical Therapy

Aims The purpose of this study was to evaluate whether yoga training in addition to standard medical therapy can improve cardiac function and reduce N terminal pro B-type natriuretic peptide (NT pro BNP) in heart failure (HF). Methods 130 patients were recruited and randomized into two groups: Control Group (CG) ( n = 65), Yoga Group (YG). In YG, 44 patients and in CG, 48 patients completed the study. Cardiac function using left ventricular ejection fraction (LVEF), myocardial performance index (Tei index), and NT pro BNP, a biomarker of HF, was assessed at baseline and after 12 weeks. Result Improvement in LVEF, Tei index, and NT pro BNP were statistically significant in both the groups. Furthermore, when the changes in before and after 12 weeks were in percentage, LVEF increased 36.88% in the YG and 16.9% in the CG, Tei index was reduced 27.87% in the YG and 2.79% in the CG, NT pro BNP was reduced 63.75% in the YG and 10.77% in the CG. The between group comparisons from pre to post 12 weeks were significant for YG improvements (LVEF, P < 0.01, Tei index, P < 0.01, NT pro BNP, P < 0.01). Conclusion These results indicate that the addition of yoga therapy to standard medical therapy for HF patients has a markedly better effect on cardiac function and reduced myocardial stress measured using NT pro BNP in patients with stable HF.

Sign in / Sign up

Export Citation Format

Share Document