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  1 / 9622 MEDLINE  
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PMID:27778643
Autor:Sparks LM; Redman LM; Conley KE; Harper ME; Yi F; Hodges A; Eroshkin A; Costford SR; Gabriel ME; Shook C; Cornnell HH; Ravussin E; Smith SR
Dirección:Translational Research Institute for Metabolism and Diabetes, Florida Hospital, Orlando, Florida 32804.
Título:Effects of 12 Months of Caloric Restriction on Muscle Mitochondrial Function in Healthy Individuals.
Fuente:J Clin Endocrinol Metab; 102(1):111-121, 2017 Jan 01.
ISSN:1945-7197
País de publicación:United States
Idioma:eng
Resumen:Context: The effects of caloric restriction (CR) on in vivo muscle mitochondrial function in humans are controversial. Objective: We evaluated muscle mitochondrial function and associated transcriptional profiles in nonobese humans after 12 months of CR. Design: Individuals from an ancillary study of the CALERIE 2 randomized controlled trial were assessed at baseline and 12 months after a 25% CR or ad libitum (control) diet. Setting: The study was performed at Pennington Biomedical Research Center in Baton Rouge, LA. Participants: Study participants included 51 (34 female subjects, 25 to 50 years of age) healthy nonobese individuals randomized to 1 of 2 groups (CR or control). Intervention: This study included 12 months of a 25% CR or ad libitum (control) diet. Main Outcomes: In vivo mitochondrial function [maximal ATP synthesis rate (ATPmax), ATPflux/O2 (P/O)] was determined by 31P-magnetic resonance spectroscopy and optical spectroscopy, and body composition was determined by dual-energy X-ray absorptiometry. In a subset of individuals, a muscle biopsy was performed for transcriptional profiling via quantitative reverse transcription polymerase chain reaction and microarrays. Results: Weight, body mass index (BMI), fat, and fat-free mass (P < 0.001 for all) significantly decreased at month 12 after CR vs control. In vivo ATPmax and P/O were unaffected by 12 months of CR. Targeted transcriptional profiling showed no effects on pathways involved in mitochondrial biogenesis, function, or oxidative stress. A subgroup analysis according to baseline P/O demonstrated that a higher (vs lower) P/O was associated with notable improvements in ATPmax and P/O after CR. Conclusions: In healthy nonobese humans, CR has no effect on muscle mitochondrial function; however, having a "more coupled" (versus "less coupled") phenotype enables CR-induced improvements in muscle mitochondrial function.
Tipo de publicación:JOURNAL ARTICLE; MULTICENTER STUDY; RANDOMIZED CONTROLLED TRIAL
Nombre de substancia:0 (Biomarkers)


  2 / 9622 MEDLINE  
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PMID:29269692
Autor:Ishikawa T; Nakamura K; Shimasaki R; Goto K; Umehara F
Dirección:Department of Neurology, Nishibeppu National Hospital.
Título:[A case of mitochondrial disease with multiple mitochondrial DNA deletions suspected amyotrophic lateral sclerosis-frontotemporal dementia].
Fuente:Rinsho Shinkeigaku; 58(1):15-20, 2018 Jan 26.
ISSN:1882-0654
País de publicación:Japan
Idioma:jpn
Resumen:A 76-year-old woman showed a dramatic lowering of her tone of voice in October 2014, followed by muscle weakness of the left arm. The previous attending physician noticed remarkable left dominant frontotemporal lobe atrophy on cranial MRI. Her dysarthria, dysphagia and the muscle weakness of her extremities worsened, and a muscle biopsy revealed mitochondrial abnormality. The mitochondrial DNA from her muscle showed multiple deletions; the previous physician therefore diagnosed the patient with mitochondrial disease. The patient resembled amyotrophic lateral sclerosis-frontotemporal dementia (ALS-FTD). No other cases of ALS-FTD with mitochondrial disease have been reported in Japan. We therefore consider the present case to be valuable.
Tipo de publicación:CASE REPORTS; JOURNAL ARTICLE
Nombre de substancia:0 (DNA, Mitochondrial); 94ZLA3W45F (Arginine)


  3 / 9622 MEDLINE  
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PMID:28465283
Autor:Pinto SK; Lamon S; Stephenson EJ; Kalanon M; Mikovic J; Koch LG; Britton SL; Hawley JA; Camera DM
Dirección:Centre for Exercise and Nutrition, Mary MacKillop Institute for Health Research, Australian Catholic University, Melbourne, Victoria, Australia.
Título:Expression of microRNAs and target proteins in skeletal muscle of rats selectively bred for high and low running capacity.
Fuente:Am J Physiol Endocrinol Metab; 313(3):E335-E343, 2017 09 01.
ISSN:1522-1555
País de publicación:United States
Idioma:eng
Resumen:Impairments in mitochondrial function and substrate metabolism are implicated in the etiology of obesity and Type 2 diabetes. MicroRNAs (miRNAs) can degrade mRNA or repress protein translation and have been implicated in the development of such disorders. We used a contrasting rat model system of selectively bred high- (HCR) or low- (LCR) intrinsic running capacity with established differences in metabolic health to investigate the molecular mechanisms through which miRNAs regulate target proteins mediating mitochondrial function and substrate oxidation processes. Quantification of select miRNAs using the rat miFinder miRNA PCR array revealed differential expression of 15 skeletal muscles (musculus tibialis anterior) miRNAs between HCR and LCR rats (14 with higher expression in LCR; < 0.05). Ingenuity Pathway Analysis predicted these altered miRNAs to collectively target multiple proteins implicated in mitochondrial dysfunction and energy substrate metabolism. Total protein abundance of citrate synthase (CS; miR-19 target) and voltage-dependent anion channel 1 (miR-7a target) were higher in HCR compared with LCR cohorts (~57 and ~26%, respectively; < 0.05). A negative correlation was observed for miR-19a-3p and CS ( = 0.32, = 0.015) protein expression. To determine whether miR-19a-3p can regulate CS in vitro, we performed luciferase reporter and transfection assays in C2C12 myotubes. MiR-19a-3p binding to the CS untranslated region did not change luciferase reporter activity; however, miR-19a-3p transfection decreased CS protein expression (∼70%; < 0.05). The differential miRNA expression targeting proteins implicated in mitochondrial dysfunction and energy substrate metabolism may contribute to the molecular basis, mediating the divergent metabolic health profiles of LCR and HCR rats.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (MIRN103 microRNA, rat); 0 (MIRN181 microRNA, rat); 0 (MIRN19 microRNA, rat); 0 (MIRN194 microRNA, rat); 0 (MIRN223 microRNA, rat); 0 (MIRN24 microRNA, rat); 0 (MIRN26 microRNA, rat); 0 (MIRN30 microRNA, rat); 0 (MicroRNAs); 0 (RNA, Messenger); EC 1.6.- (Voltage-Dependent Anion Channel 1); EC 2.3.3.1 (Citrate (si)-Synthase)


  4 / 9622 MEDLINE  
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PMID:28467934
Autor:Fan W; Waizenegger W; Lin CS; Sorrentino V; He MX; Wall CE; Li H; Liddle C; Yu RT; Atkins AR; Auwerx J; Downes M; Evans RM
Dirección:Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
Título:PPARδ Promotes Running Endurance by Preserving Glucose.
Fuente:Cell Metab; 25(5):1186-1193.e4, 2017 May 02.
ISSN:1932-7420
País de publicación:United States
Idioma:eng
Resumen:Management of energy stores is critical during endurance exercise; a shift in substrate utilization from glucose toward fat is a hallmark of trained muscle. Here we show that this key metabolic adaptation is both dependent on muscle PPARδ and stimulated by PPARδ ligand. Furthermore, we find that muscle PPARδ expression positively correlates with endurance performance in BXD mouse reference populations. In addition to stimulating fatty acid metabolism in sedentary mice, PPARδ activation potently suppresses glucose catabolism and does so without affecting either muscle fiber type or mitochondrial content. By preserving systemic glucose levels, PPARδ acts to delay the onset of hypoglycemia and extends running time by ∼100 min in treated mice. Collectively, these results identify a bifurcated PPARδ program that underlies glucose sparing and highlight the potential of PPARδ-targeted exercise mimetics in the treatment of metabolic disease, dystrophies, and, unavoidably, the enhancement of athletic performance.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Fatty Acids); 0 (PPAR delta); IY9XDZ35W2 (Glucose)


  5 / 9622 MEDLINE  
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PMID:28467933
Autor:Koh JH; Hancock CR; Terada S; Higashida K; Holloszy JO; Han DH
Dirección:Division of Geriatrics and Nutritional Sciences, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.
Título:PPARß Is Essential for Maintaining Normal Levels of PGC-1α and Mitochondria and for the Increase in Muscle Mitochondria Induced by Exercise.
Fuente:Cell Metab; 25(5):1176-1185.e5, 2017 May 02.
ISSN:1932-7420
País de publicación:United States
Idioma:eng
Resumen:The objective of this study was to evaluate the specific mechanism(s) by which PPARß regulates mitochondrial content in skeletal muscle. We discovered that PPARß increases PGC-1α by protecting it from degradation by binding to PGC-1α and limiting ubiquitination. PPARß also induces an increase in nuclear respiratory factor 1 (NRF-1) expression, resulting in increases in mitochondrial respiratory chain proteins and MEF2A, for which NRF-1 is a transcription factor. There was also an increase in AMP kinase phosphorylation mediated by an NRF-1-induced increase in CAM kinase kinase-ß (CaMKKß). Knockdown of PPARß resulted in large decreases in the levels of PGC-1α and mitochondrial proteins and a marked attenuation of the exercise-induced increase in mitochondrial biogenesis. In conclusion, PPARß induces an increase in PGC-1α protein, and PPARß is a transcription factor for NRF-1. Thus, PPARß plays essential roles in the maintenance and adaptive increase in mitochondrial enzymes in skeletal muscle by exercise.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Nuclear Respiratory Factor 1); 0 (PPAR-beta); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Kinase); EC 2.7.11.31 (AMP-Activated Protein Kinases)


  6 / 9622 MEDLINE  
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PMID:28467930
Autor:Park SJ; Gavrilova O; Brown AL; Soto JE; Bremner S; Kim J; Xu X; Yang S; Um JH; Koch LG; Britton SL; Lieber RL; Philp A; Baar K; Kohama SG; Abel ED; Kim MK; Chung JH
Dirección:Laboratory of Obesity and Aging Research, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Título:DNA-PK Promotes the Mitochondrial, Metabolic, and Physical Decline that Occurs During Aging.
Fuente:Cell Metab; 25(5):1135-1146.e7, 2017 May 02.
ISSN:1932-7420
País de publicación:United States
Idioma:eng
Resumen:Hallmarks of aging that negatively impact health include weight gain and reduced physical fitness, which can increase insulin resistance and risk for many diseases, including type 2 diabetes. The underlying mechanism(s) for these phenomena is poorly understood. Here we report that aging increases DNA breaks and activates DNA-dependent protein kinase (DNA-PK) in skeletal muscle, which suppresses mitochondrial function, energy metabolism, and physical fitness. DNA-PK phosphorylates threonines 5 and 7 of HSP90α, decreasing its chaperone function for clients such as AMP-activated protein kinase (AMPK), which is critical for mitochondrial biogenesis and energy metabolism. Decreasing DNA-PK activity increases AMPK activity and prevents weight gain, decline of mitochondrial function, and decline of physical fitness in middle-aged mice and protects against type 2 diabetes. In conclusion, DNA-PK is one of the drivers of the metabolic and fitness decline during aging, and therefore DNA-PK inhibitors may have therapeutic potential in obesity and low exercise capacity.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 ((3aS,4S,9bS)-N-(2-(8-cyano-1-formyl-2,3,3a,4,5,9b-hexahydro-1H-pyrrolo(3,2-c)quinolin-4-yl)-2-methylpropyl)-4,6-difluorobenzofuran-2-carboxyamide); 0 (Benzofurans); 0 (Quinolines); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.31 (AMP-Activated Protein Kinases)


  7 / 9622 MEDLINE  
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PMID:28460005
Autor:Herbst A; Widjaja K; Nguy B; Lushaj EB; Moore TM; Hevener AL; McKenzie D; Aiken JM; Wanagat J
Dirección:Department of Agricultural, Food and Nutritional Sciences, University of Alberta, Edmonton, Canada.
Título:Digital PCR Quantitation of Muscle Mitochondrial DNA: Age, Fiber Type, and Mutation-Induced Changes.
Fuente:J Gerontol A Biol Sci Med Sci; 72(10):1327-1333, 2017 Oct 01.
ISSN:1758-535X
País de publicación:United States
Idioma:eng
Resumen:Definitive quantitation of mitochondrial DNA (mtDNA) and mtDNA deletion mutation abundances would help clarify the role of mtDNA instability in aging. To more accurately quantify mtDNA, we applied the emerging technique of digital polymerase chain reaction to individual muscle fibers and muscle homogenates from aged rodents. Individual fiber mtDNA content correlated with fiber type and decreased with age. We adapted a digital polymerase chain reaction deletion assay that was accurate in mixing experiments to a mutation frequency of 0.03% and quantitated an age-induced increase in deletion frequency from rat muscle homogenates. Importantly, the deletion frequency measured in muscle homogenates strongly correlated with electron transport chain-deficient fiber abundance determined by histochemical analyses. These data clarify the temporal accumulation of mtDNA deletions that lead to electron chain-deficient fibers, a process culminating in muscle fiber loss.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (DNA, Mitochondrial)


  8 / 9622 MEDLINE  
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PMID:28455453
Autor:Volodina O; Ganesan S; Pearce SC; Gabler NK; Baumgard LH; Rhoads RP; Selsby JT
Dirección:Department of Animal Science, Iowa State University, Ames, Iowa.
Título:Short-term heat stress alters redox balance in porcine skeletal muscle.
Fuente:Physiol Rep; 5(8), 2017 Apr.
ISSN:2051-817X
País de publicación:United States
Idioma:eng
Resumen:Heat stress contributes to higher morbidity and mortality in humans and animals and is an agricultural economic challenge because it reduces livestock productivity. Redox balance and associated mitochondrial responses appear to play a central role in heat stress-induced skeletal muscle pathology. We have previously reported increased oxidative stress and mitochondrial content in oxidative muscle following 12 h of heat stress. The purposes of this investigation were to characterize heat stress-induced oxidative stress and changes in mitochondrial content and biogenic signaling in oxidative skeletal muscle. Crossbred gilts were randomly assigned to either thermal neutral (21°C;  = 8, control group) or heat stress (37°C) conditions for 2 h ( = 8), 4 h ( = 8), or 6 h ( = 8). At the end, their respective environmental exposure, the red portion of the semitendinosus muscle (STR) was harvested. Heat stress increased concentration of malondialdehyde (MDA) following 2 and 4 h compared to thermal neutral and 6 h, which was similar to thermal neutral, and decreased linearly with time. Protein carbonyl content was not influenced by environment. Catalase activity was increased following 4 h of heat stress and superoxide dismutase activity was decreased following 6 h of heat stress compared to thermal neutral conditions. Heat stress-mediated changes in antioxidant activity were independent of altered protein abundance or transcript expression. Mitochondrial content and mitochondrial biogenic signaling were similar between groups. These data demonstrate that heat stress caused a transient increase in oxidative stress that was countered by a compensatory change in catalase activity. These findings contribute to our growing understanding of the chronology of heat stress-induced intracellular dysfunctions in skeletal muscle.
Tipo de publicación:JOURNAL ARTICLE


  9 / 9622 MEDLINE  
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PMID:28456637
Autor:Vienne JC; Cimetta C; Dubois M; Duburcq T; Favory R; Dessein AF; Fontaine M; Joncquel-Chevalier Curt M; Cuisset JM; Douillard C; Mention-Mulliez K; Dobbelaere D; Vamecq J
Dirección:Department of Biochemistry and Molecular Biology, Laboratory of Hormonology, Metabolism-Nutrition & Oncology (HMNO), Center of Biology and Pathology (CBP) Pierre-Marie Degand, CHRU Lille, France.
Título:A fast method for high resolution oxymetry study of skeletal muscle mitochondrial respiratory chain complexes.
Fuente:Anal Biochem; 528:57-62, 2017 07 01.
ISSN:1096-0309
País de publicación:United States
Idioma:eng
Resumen:High resolution oxymetry study (HROS) of skeletal muscle usually requires 90-120 min preparative phase (dissection, permeabilization and washing). This work reports on the suitability of a rapid muscle preparation which by-passes this long preparation. For a few seconds only, muscle biopsy from pigs is submitted to gentle homogenization at 8000 rotations per minute using an ultra-dispersor apparatus. Subsequent HROS is performed using FCCP instead of ADP, compounds crossing and not plasma membrane, respectively. This simplified procedure compares favorably with classical (permeabilized fibers) HROS in terms of respiratory chain complex activities. Mitochondria from cells undergoing ultradispersion were functionally preserved as attested by relative inefficacy of added cytochrome C (not crossing intact mitochondrial outer membrane) to stimulate mitochondrial respiration. Responsiveness of respiration to ADP (in the absence of FCCP) suggested that these intact mitochondria were outside cells disrupted by ultradispersion or within cells permeated by this procedure.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Electron Transport Chain Complex Proteins)


  10 / 9622 MEDLINE  
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PMID:29261667
Autor:Eldor R; Norton L; Fourcaudot M; Galindo C; DeFronzo RA; Abdul-Ghani M
Dirección:Diabetes Unit, Institute for Metabolism, Endocrinology and Hypertension, Tel Aviv Sourasky Medical Center, Tel Aviv, Israel.
Título:Increased lipid availability for three days reduces whole body glucose uptake, impairs muscle mitochondrial function and initiates opposing effects on PGC-1α promoter methylation in healthy subjects.
Fuente:PLoS One; 12(12):e0188208, 2017.
ISSN:1932-6203
País de publicación:United States
Idioma:eng
Resumen:AIMS: FFA and FFA metabolites cause insulin resistance and impair beta cell function. The goal of our research was to examine whether elevation of plasma FFA impairs mitochondrial function and alters PGC-1α promoter methylation. METHODS: In this uncontrolled, change from baseline study design, insulin sensitivity and glucose-stimulated insulin secretion were measured in 9 normal glucose tolerant subjects before and after 3 day lipid infusion to elevate plasma FFA concentration. Vastus lateralis muscle biopsies were obtained and mitochondrial function, PGC-1α expression, and PGC-1α promoter methylation were quantitated. RESULTS: Increased plasma FFA (440±93 µmol/Lto 997±242 µM, p<0.001) decreased insulin-stimulated total glucose disposal (TGD) by 25% (p = 0.008), impaired suppression of endogenous glucose production (p = 0.01), and reduced mitochondrial ATP synthesis with complex 1 (34%, p<0.05) and complex 2 (30%, p<0.05) substrates. Lipid infusion had no effect on muscle PGC-1α RNA expression, total methylation or non-CpG methylation, but methylation of the alternative PGC-1α promoter decreased (1.30±0.30 to 0.84±0.15% methylated residues/patient•strand, p = 0.055). Within PGC-1α promoter there was demethylation of CpT residues (0.72±0.16 vs. 0.28±0.10 methylated residues/patient•strand) (p = 0.002), which was inversely correlated with PGC-1α mRNA expression (r = -0.94, p<0.0001) and ATP synthesis with complex 1 (r = -0.80, p<0.01) and complex 2 (r = -0.69, p<0.05) substrates. Lipid infusion increased DNMT-3B (methyltransferase associated with PGC-1α promoter non-CpG methylation) mRNA expression (0.87 ± 0.09 to 1.62 ± 0.22 arbitrary units, p = 0.005), which correlated inversely with CpT demethylation (r = 0.67, p<0.05). CONCLUSION/INTERPRETATION: Physiologic plasma FFA elevation in NGT individuals has opposing effects on PGC-1α non-CpG residue methylation (CpT demethylation and increased DNMT-3B expression), which is correlated with changes in PGC-1α expression and skeletal muscle mitochondrial function.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Fatty Acids, Nonesterified); 0 (Insulin); 0 (PPARGC1A protein, human); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 8L70Q75FXE (Adenosine Triphosphate); IY9XDZ35W2 (Glucose)



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