Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia.
Identifieur interne : 000114 ( Ncbi/Checkpoint ); précédent : 000113; suivant : 000115Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia.
Auteurs : D. Frankel [Canada] ; K. Mehindate ; H M SchipperSource :
- Journal of cellular physiology [ 0021-9541 ] ; 2000.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Heme Oxygenase (Decyclizing), Superoxide Dismutase.
- physiology : Astrocytes.
- Animals, Gene Expression Regulation, Enzymologic, Heme Oxygenase-1, Humans, Membrane Proteins, Oxidative Stress, Rats, Rats, Sprague-Dawley, Transcriptional Activation.
Abstract
Manganese superoxide dismutase (MnSOD) is an antioxidant enzyme that reduces superoxide anion to hydrogen peroxide in cell mitochondria. MnSOD is overexpressed in normal aging brain and in various central nervous system disorders; however, the mechanisms mediating the upregulation of MnSOD under these conditions remain poorly understood. We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. In the present study, we demonstrate that antecedent upregulation of HO-1 is necessary and sufficient for subsequent induction of the MnSOD gene in neonatal rat astroglia challenged with CSH or dopamine, and in astroglial cultures transiently transfected with full-length human HO-1 cDNA. Treatment with potent antioxidants attenuates MnSOD expression in HO-1-transfected astroglia, strongly suggesting that intracellular oxidative stress signals MnSOD gene induction in these cells. Activation of this HO-1-MnSOD axis may play an important role in the pathogenesis of Alzheimer disease, Parkinson disease and other free radical-related neurodegenerative disorders. In these conditions, compensatory upregulation of MnSOD may protect mitochondria from oxidative damage accruing from heme-derived free iron and carbon monoxide liberated by the activity of HO-1.
DOI: 10.1002/1097-4652(200010)185:1<80::AID-JCP7>3.0.CO;2-W
PubMed: 10942521
Affiliations:
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Mehindate</name></author><author><name sortKey="Schipper, H M" sort="Schipper, H M" uniqKey="Schipper H" first="H M" last="Schipper">H M Schipper</name></author></analytic><series><title level="j">Journal of cellular physiology</title><idno type="ISSN">0021-9541</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Astrocytes (physiology)</term><term>Gene Expression Regulation, Enzymologic</term><term>Heme Oxygenase (Decyclizing) (genetics)</term><term>Heme Oxygenase-1</term><term>Humans</term><term>Membrane Proteins</term><term>Oxidative Stress</term><term>Rats</term><term>Rats, Sprague-Dawley</term><term>Superoxide Dismutase (genetics)</term><term>Transcriptional Activation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Heme Oxygenase (Decyclizing)</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Astrocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Gene Expression Regulation, Enzymologic</term><term>Heme Oxygenase-1</term><term>Humans</term><term>Membrane Proteins</term><term>Oxidative Stress</term><term>Rats</term><term>Rats, Sprague-Dawley</term><term>Transcriptional Activation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese superoxide dismutase (MnSOD) is an antioxidant enzyme that reduces superoxide anion to hydrogen peroxide in cell mitochondria. MnSOD is overexpressed in normal aging brain and in various central nervous system disorders; however, the mechanisms mediating the upregulation of MnSOD under these conditions remain poorly understood. We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. In the present study, we demonstrate that antecedent upregulation of HO-1 is necessary and sufficient for subsequent induction of the MnSOD gene in neonatal rat astroglia challenged with CSH or dopamine, and in astroglial cultures transiently transfected with full-length human HO-1 cDNA. Treatment with potent antioxidants attenuates MnSOD expression in HO-1-transfected astroglia, strongly suggesting that intracellular oxidative stress signals MnSOD gene induction in these cells. Activation of this HO-1-MnSOD axis may play an important role in the pathogenesis of Alzheimer disease, Parkinson disease and other free radical-related neurodegenerative disorders. In these conditions, compensatory upregulation of MnSOD may protect mitochondria from oxidative damage accruing from heme-derived free iron and carbon monoxide liberated by the activity of HO-1.</div></front></TEI><affiliations><list><country><li>Canada</li></country><region><li>Québec</li></region><settlement><li>Montréal</li></settlement></list><tree><noCountry><name sortKey="Mehindate, K" sort="Mehindate, K" uniqKey="Mehindate K" first="K" last="Mehindate">K. Mehindate</name><name sortKey="Schipper, H M" sort="Schipper, H M" uniqKey="Schipper H" first="H M" last="Schipper">H M Schipper</name></noCountry><country name="Canada"><region name="Québec"><name sortKey="Frankel, D" sort="Frankel, D" uniqKey="Frankel D" first="D" last="Frankel">D. 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