0000000000240881

AUTHOR

Vladimir Veksler

showing 3 related works from this author

Cardiolipin content controls mitochondrial coupling and energetic efficiency in muscle

2020

Decreasing mitochondrial energy-production efficiency in skeletal muscle can confer protection against diet-induced obesity.

muscle[SDV]Life Sciences [q-bio]Respiratory chainDiseases and DisordersOxidative phosphorylation[SDV.BC]Life Sciences [q-bio]/Cellular Biology030204 cardiovascular system & hematology03 medical and health scienceschemistry.chemical_compound0302 clinical medicinemedicineCardiolipin[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyInner mitochondrial membrane[SDV.BC] Life Sciences [q-bio]/Cellular BiologyResearch ArticlesFatty acid synthesisComputingMilieux_MISCELLANEOUS030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciencesMultidisciplinary[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyATP synthasebiologyfungifood and beveragesSciAdv r-articlesSkeletal muscleFatty acidCell BiologymitochondrialCell biologymedicine.anatomical_structurechemistryCardiolipinbiology.protein[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyResearch Article
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Down-regulation of OPA1 alters mouse mitochondrial morphology, PTP function, and cardiac adaptation to pressure overload

2012

AIMS: The optic atrophy 1 (OPA1) protein is an essential protein involved in the fusion of the mitochondrial inner membrane. Despite its high level of expression, the role of OPA1 in the heart is largely unknown. We investigated the role of this protein in Opa1(+/-) mice, having a 50% reduction in OPA1 protein expression in cardiac tissue. METHODS AND RESULTS: In mutant mice, cardiac function assessed by echocardiography was not significantly different from that of the Opa1(+/+). Electron and fluorescence microscopy revealed altered morphology of the Opa1(+/-) mice mitochondrial network; unexpectedly, mitochondria were larger with the presence of clusters of fused mitochondria and altered c…

Cardiac function curveendocrine systemPhysiologyAdaptation BiologicalDown-RegulationBiologyMitochondrionMitochondrial Membrane Transport ProteinsPermeabilityGTP PhosphohydrolasesMitochondrial ProteinsMice03 medical and health sciencesMitochondrial membrane transport protein0302 clinical medicinePhysiology (medical)Optic Atrophy Autosomal DominantPressuremedicineAnimalsMyocyteMyocytes CardiacInner mitochondrial membrane030304 developmental biologyMice KnockoutPressure overload0303 health sciencesMitochondrial Permeability Transition Poremedicine.diseaseeye diseasesMitochondriaCell biologyBiochemistryMitochondrial permeability transition poreMitochondrial Membranesbiology.proteinOptic Atrophy 1Cardiology and Cardiovascular Medicine030217 neurology & neurosurgeryCardiovascular Research
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Creatine kinase is the main target of reactive oxygen species in cardiac myofibrils.

1996

Abstract Reactive oxygen species (ROS) have been reported to alter cardiac myofibrillar function as well as myofibrillar enzymes such as myosin ATPase and creatine kinase (CK). To understand their precise mode and site of action in myofibrils, the effects of the xanthine/xanthine oxidase (X/XO) system or of hydrogen peroxide (H 2 O 2 ) have been studied in the presence and in the absence of phosphocreatine (PCr) in Triton X-100–treated cardiac fibers. We found that xanthine oxidase (XO), with or without xanthine, induced a decrease in maximal Ca 2+ -activated tension. We attributed this effect to the high contaminating proteolytic activity in commercial XO preparations, since it could be p…

Xanthine OxidasebiologyFree RadicalsPhysiologyMyosin ATPaseSuperoxideHydrogen PeroxideMyosinsXanthineMyocardial ContractionPhosphocreatineRatschemistry.chemical_compoundchemistryBiochemistryMyofibrilsbiology.proteinAnimalsCreatine kinasePMSFCardiology and Cardiovascular MedicineMyofibrilXanthine oxidaseReactive Oxygen SpeciesCreatine KinaseCirculation research
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