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Poster Abstract PresentationsSession Title: Poster Session 3

Abstract 357: Manganese Superoxide Dismutase: a Novel Mediator of Heart Failure Development and Progression

Sumitra Miriyala, Mini Chandra, Benjamin Maxey, Daret K St. Clair, Manikandan Panchatcharam
Circulation Research. 2015;117:A357
Sumitra Miriyala
LSU Health Sciences Cntr - Shreveport, Shreveport, LA
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Mini Chandra
LSU Health Sciences Cntr - Shreveport, Shreveport, LA
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Benjamin Maxey
Loyola Coll Prep, Shreveport, LA
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Daret K St. Clair
Univ of Kentucky, Lexington, KY
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Manikandan Panchatcharam
LSU Health Sciences Cntr - Shreveport, Shreveport, LA
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Abstract

Manganese Superoxide Dismutase (MnSOD), an antioxidant enzyme that catalyzes the conversion of superoxide radicals (O2•-) in mitochondria. Constitutive activation mitochondrial reactive oxygen species (ROS) has been implicated in both the pathogenesis and the progression of cardiovascular disease. Absence of SOD2 (gene that encodes MnSOD) is found to be embryonic lethal in animal models due to impairment of mitochondrial function, most noticeably in the heart. In our earlier investigation, we have shown that the MnSOD mimetic, MnTnBuOE-2-PyP5+ distributes 3-fold more in mitochondria than in cytosol. The exceptional ability of MnTnBuOE-2-PyP5+ to dismute O2•- parallels its ability to reduce ONOO– and CO3–. Based on our earlier reports, we have generated mice that specifically lack MnSOD in cardiomyocytes (Mhy6-SOD2Δ). These mice showed early mortality ~4 months due to cardiac mitochondrial dysfunction. Oxidative phosphorylation (OXPHOS) in mitochondria is the predominant mode for O2 consumption in cells, and the mitochondria are the primary source of ROS in cells due to leaked electrons. FACS analyses using Mito-Tracker Green indicated that the mass of mitochondria per cell was slightly decreased in the Mhy6-SOD2Δ to the wild type. We then examined OXPHOS levels in Mhy6-SOD2Δ v.s. wild type using a Seahorse XF analyzer. The rate of oxygen consumption per cells was signi[[Unable to Display Character: fi]]cantly lower in Mhy6-SOD2Δ cardiomyocytes than that in wild type. The most noticeable difference in the O2 consumption was found in the presence of FCCP (H+ ionophore / uncoupler). FCCP is an inner membrane pore opener which resets the proton gradient between the mitochondrial matrix and the interspace, resulting in continuous transport of protons and consuming O2 at the maximum potential. Remarkably, while the FCCP treatment increased O2 consumption in wild type, the treatment showed no effect on the O2 consumption in the Mhy6-SOD2Δ cardiomyocytes. The result indicated that the low basal OXPHOS activity in Mhy6-SOD2Δ was due to unusually low OXPHOS potential. We examined glycolysis in these cells by measuring extracellular acidi[[Unable to Display Character: fi]]cation (ECAR) and the pattern exactly opposite to that of oxygen consumption rate (OCR) was observed for glycolysis rates between Mhy6-SOD2Δ and wild type.

  • Manganese Superoxide Dismutase
  • reactive oxygen species
  • Oxidative phosphorylation
  • Author Disclosures: S. Miriyala: None. M. Chandra: None. B. Maxey: None. D.K. St. Clair: None. M. Panchatcharam: None.

  • © 2015 by American Heart Association, Inc.
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July 17, 2015, Volume 117, Issue Suppl 1
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    Abstract 357: Manganese Superoxide Dismutase: a Novel Mediator of Heart Failure Development and Progression
    Sumitra Miriyala, Mini Chandra, Benjamin Maxey, Daret K St. Clair and Manikandan Panchatcharam
    Circulation Research. 2015;117:A357, originally published October 21, 2015

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    Abstract 357: Manganese Superoxide Dismutase: a Novel Mediator of Heart Failure Development and Progression
    Sumitra Miriyala, Mini Chandra, Benjamin Maxey, Daret K St. Clair and Manikandan Panchatcharam
    Circulation Research. 2015;117:A357, originally published October 21, 2015
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