Manganese superoxide dismutase deficiency triggers mitochondrial uncoupling and the Warburg effect

Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout ( Sod2 +/− ) mice...

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Published inOncogene Vol. 34; no. 32; pp. 4229 - 4237
Main Authors Xu, Y, Miriyala, S, Fang, F, Bakthavatchalu, V, Noel, T, Schell, D M, Wang, C, St Clair, W H, St Clair, D K
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 06.08.2015
Nature Publishing Group
Subjects
1-Phosphatidylinositol 3-kinase
13/1
13/106
13/109
13/31
13/89
13/95
38/39
38/61
38/77
631/67/2327
64/60
Adenosine Triphosphate - metabolism
AKT protein
Animals
Antioxidants
Apoptosis
Blotting, Western
Cancer
Carcinogenesis
Cell Biology
Cells, Cultured
Enzymes
Genetic aspects
Glycolysis
Human Genetics
Humans
Internal Medicine
Ion Channels - genetics
Ion Channels - metabolism
Lactates - metabolism
Lactic acid
Manganese
Medicine
Medicine & Public Health
Mice, Knockout
Mitochondria
Mitochondria - genetics
Mitochondria - metabolism
Mitochondrial diseases
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Oncology
original-article
Oxidation
Phosphatidylinositol 3-Kinases - metabolism
Physiological aspects
PPAR alpha - genetics
PPAR alpha - metabolism
Protein expression
Proto-Oncogene Proteins c-akt - metabolism
Reactive oxygen species
Reactive Oxygen Species - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Risk factors
RNA Interference
Signal transduction
Signal Transduction - genetics
Superoxide dismutase
Superoxide Dismutase - deficiency
Superoxide Dismutase - genetics
TOR protein
TOR Serine-Threonine Kinases - genetics
TOR Serine-Threonine Kinases - metabolism
Tumorigenesis
Uncoupling Protein 1
Uncoupling Protein 2
United States
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Abstract Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout ( Sod2 +/− ) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
AbstractList Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout (Sod2 super(+/-)) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPAR alpha ), suggesting that the activation of PPAR alpha signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout ( Sod2 +/− ) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout ([Sod.sup.2+/-]) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect. Oncogene (2015) 34, 4229-4237; doi: 10.1038/onc.2014.355; published online 3 November 2014
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deciency in skin tissues of MnSOD-heterozygous knockout (Sod2+/) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is decient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPAR), suggesting that the activation of PPAR signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria.
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to play important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout ( Sod2 +/− ) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout (Sod2(+/-)) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to have important roles in tumorigenesis. Here, we show that MnSOD deficiency in skin tissues of MnSOD-heterozygous knockout (Sod2+/−) mice leads to increased expresson of uncoupling proteins (UCPs). When MnSOD is deficient, superoxide radical and its resulting reactive oxygen species (ROS) activate ligand binding to peroxisome proliferator-activated receptor alpha (PPARα), suggesting that the activation of PPARα signaling is a major mechanism underlying MnSOD-dependent UCPs expression that consequently triggers the PI3K/Akt/mTOR pathway, leading to increased aerobic glycolysis. Knockdown of UCPs and mTOR suppresses lactate production and increases ATP levels, suggesting that UCPs contribute to increased glycolysis. These results highlight the existence of a free radical-mediated mechanism that activates mitochondria uncoupling to reduce ROS production, which precedes the glycolytic adaptation described as the Warburg Effect.
Audience Academic
Author Xu, Y
St Clair, W H
St Clair, D K
Schell, D M
Fang, F
Noel, T
Miriyala, S
Wang, C
Bakthavatchalu, V
AuthorAffiliation 1 Department of Oncology, First Affiliated Hospital, Nanjing Medical University, Nanjing, China
4 Markey Cancer Center, University of Kentucky, Lexington, KY 40536, USA
2 Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40536, USA
3 Department of Radiation Medicine, University of Kentucky, Lexington, KY 40536, USA
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PublicationDateYYYYMMDD 2015-08-06
PublicationDate_xml – month: 08
  year: 2015
  text: 2015-08-06
  day: 06
PublicationDecade 2010
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
– name: New York
PublicationTitle Oncogene
PublicationTitleAbbrev Oncogene
PublicationTitleAlternate Oncogene
PublicationYear 2015
Publisher Nature Publishing Group UK
Nature Publishing Group
Publisher_xml – sequence: 0
  name: Nature Publishing Group
– name: Nature Publishing Group UK
– name: Nature Publishing Group
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Snippet Manganese superoxide dismutase (MnSOD) is a mitochondrially localized primary antioxidant enzyme, known to be essential for the survival of aerobic life and to...
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SubjectTerms 1-Phosphatidylinositol 3-kinase
13/1
13/106
13/109
13/31
13/89
13/95
38/39
38/61
38/77
631/67/2327
64/60
Adenosine Triphosphate - metabolism
AKT protein
Animals
Antioxidants
Apoptosis
Blotting, Western
Cancer
Carcinogenesis
Cell Biology
Cells, Cultured
Enzymes
Genetic aspects
Glycolysis
Human Genetics
Humans
Internal Medicine
Ion Channels - genetics
Ion Channels - metabolism
Lactates - metabolism
Lactic acid
Manganese
Medicine
Medicine & Public Health
Mice, Knockout
Mitochondria
Mitochondria - genetics
Mitochondria - metabolism
Mitochondrial diseases
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Oncology
original-article
Oxidation
Phosphatidylinositol 3-Kinases - metabolism
Physiological aspects
PPAR alpha - genetics
PPAR alpha - metabolism
Protein expression
Proto-Oncogene Proteins c-akt - metabolism
Reactive oxygen species
Reactive Oxygen Species - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Risk factors
RNA Interference
Signal transduction
Signal Transduction - genetics
Superoxide dismutase
Superoxide Dismutase - deficiency
Superoxide Dismutase - genetics
TOR protein
TOR Serine-Threonine Kinases - genetics
TOR Serine-Threonine Kinases - metabolism
Tumorigenesis
Uncoupling Protein 1
Uncoupling Protein 2
Title Manganese superoxide dismutase deficiency triggers mitochondrial uncoupling and the Warburg effect
URI https://link.springer.com/article/10.1038/onc.2014.355
https://www.ncbi.nlm.nih.gov/pubmed/25362851
https://www.proquest.com/docview/1702101580
https://www.proquest.com/docview/2331643671
https://search.proquest.com/docview/1702659967
https://search.proquest.com/docview/1722171576
https://pubmed.ncbi.nlm.nih.gov/PMC4859767
Volume 34
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