Normal Cellular Prion Protein Protects against Manganese-Induced Oxidative Stress and Apoptotic Cell Death
The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxi...
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Published in | Toxicological sciences Vol. 98; no. 2; pp. 495 - 509 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
Oxford University Press
01.08.2007
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Abstract | The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxic metals. In the present study, we systematically examined whether prion protein modifies the neurotoxicity of manganese (Mn) by comparing the effect of Mn on mouse neural cells expressing prion protein (PrPC-cells) and prion-knockout (PrPKO-cells). Exposure to Mn (10μM–10mM) for 24 h produced a dose-dependent cytotoxic response in both PrPC-cells and PrPKO-cells. Interestingly, PrPC-cells (EC50 117.6μM) were more resistant to Mn-induced cytotoxicity, as compared to PrPKO-cells (EC50 59.9μM), suggesting a protective role for PrPC against Mn neurotoxicity. Analysis of intracellular Mn levels showed less Mn accumulation in PrPC-cells as compared to PrPKO-cells, but no significant changes in the expression of the metal transporter proteins transferrin and DMT-1. Furthermore, Mn-induced mitochondrial depolarization and reactive oxygen species (ROS) generation were significantly attenuated in PrPC-cells as compared to PrPKO-cells. Measurement of antioxidant status revealed similar basal levels of glutathione (GSH) in PrPC-cells and PrPKO-cells; however, Mn treatment caused greater depletion of GSH in PrPKO-cells. Mn-induced mitochondrial depolarization and ROS production were followed by time- and dose-dependent activation of the apoptotic cell death cascade involving caspase-9 and -3. Notably, DNA fragmentation induced by both Mn treatment and the oxidative stress inducer hydrogen peroxide (100μM) was significantly suppressed in PrPC-cells as compared to PrPKO-cells. Together, these results demonstrate that prion protein interferes with divalent metal Mn uptake and protects against Mn-induced oxidative stress and apoptotic cell death. |
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AbstractList | The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxic metals. In the present study, we systematically examined whether prion protein modifies the neurotoxicity of manganese (Mn) by comparing the effect of Mn on mouse neural cells expressing prion protein (PrPC-cells) and prion-knockout (PrPKO-cells). Exposure to Mn (10μM-10mM) for 24 h produced a dose-dependent cytotoxic response in both PrPC-cells and PrPKO-cells. Interestingly, PrPC-cells (EC50 117.6μM) were more resistant to Mn-induced cytotoxicity, as compared to PrPKO-cells (EC50 59.9μM), suggesting a protective role for PrPC against Mn neurotoxicity. Analysis of intracellular Mn levels showed less Mn accumulation in PrPC-cells as compared to PrPKO-cells, but no significant changes in the expression of the metal transporter proteins transferrin and DMT-1. Furthermore, Mn-induced mitochondrial depolarization and reactive oxygen species (ROS) generation were significantly attenuated in PrPC-cells as compared to PrPKO-cells. Measurement of antioxidant status revealed similar basal levels of glutathione (GSH) in PrPC-cells and PrPKO-cells; however, Mn treatment caused greater depletion of GSH in PrPKO-cells. Mn-induced mitochondrial depolarization and ROS production were followed by time- and dose-dependent activation of the apoptotic cell death cascade involving caspase-9 and -3. Notably, DNA fragmentation induced by both Mn treatment and the oxidative stress inducer hydrogen peroxide (100μM) was significantly suppressed in PrPC-cells as compared to PrPKO-cells. Together, these results demonstrate that prion protein interferes with divalent metal Mn uptake and protects against Mn-induced oxidative stress and apoptotic cell death. The normal prion protein is abundantly expressed in the CNS, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxic metals. In the present study, we systematically examined whether prion protein modifies the neurotoxicity of manganese (Mn) by comparing the effect of Mn on mouse neural cells expressing prion protein (PrP C -cells) and prion-knockout (PrP KO -cells). Exposure to Mn (10 μM-1 mM) for 24 hr produced a dose-dependent cytotoxic response in both PrP C -cells and PrP KO -cells. Interestingly, PrP C -cells (EC 50 117.6μM) were more resistant to Mn-induced cytotoxicity, as compared to PrP KO -cells (EC 50 59.9μM), suggesting a protective role for PrP C against Mn neurotoxicity. Analysis of intracellular Mn levels showed less Mn accumulation in PrP C -cells as compared to PrP KO -cells. Furthermore, Mn-induced mitochondrial depolarization and ROS generation were significantly attenuated in PrP C -cells as compared to PrP KO -cells. Measurement of antioxidant status revealed similar basal levels of glutathione (GSH) in PrP C -cells and PrP KO -cells; however, Mn treatment caused greater depletion of GSH in PrP KO -cells. Mn-induced mitochondrial depolarization and ROS production were followed by time- and dose-dependent activation of the apoptotic cell death cascade involving caspase-9 and -3. Notably, DNA fragmentation induced by both Mn treatment and oxidative stress-inducer hydrogen peroxide (100μM) was significantly suppressed in PrP C -cells as compared to PrP KO -cells. Together, these results demonstrate that prion protein interferes with divalent metal Mn uptake and protects against Mn-induced oxidative stress and apoptotic cell death. The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxic metals. In the present study, we systematically examined whether prion protein modifies the neurotoxicity of manganese (Mn) by comparing the effect of Mn on mouse neural cells expressing prion protein (PrP super(C)-cells) and prion-knockout (PrP super(KO)-cells). Exposure to Mn (10 mu M-10mM) for 24 h produced a dose-dependent cytotoxic response in both PrP super(C)-cells and PrP super(KO)-cells. Interestingly, PrP super(C)-cells (EC sub(50) 117.6 mu M) were more resistant to Mn-induced cytotoxicity, as compared to PrP super(KO)-cells (EC sub(50) 59.9 mu M), suggesting a protective role for PrP super(C) against Mn neurotoxicity. Analysis of intracellular Mn levels showed less Mn accumulation in PrP super(C)-cells as compared to PrP super(KO)-cells, but no significant changes in the expression of the metal transporter proteins transferrin and DMT-1. Furthermore, Mn-induced mitochondrial depolarization and reactive oxygen species (ROS) generation were significantly attenuated in PrP super(C)-cells as compared to PrP super(KO)-cells. Measurement of antioxidant status revealed similar basal levels of glutathione (GSH) in PrP super(C)-cells and PrP super(KO)-cells; however, Mn treatment caused greater depletion of GSH in PrP super(KO)-cells. Mn-induced mitochondrial depolarization and ROS production were followed by time- and dose-dependent activation of the apoptotic cell death cascade involving caspase-9 and -3. Notably, DNA fragmentation induced by both Mn treatment and the oxidative stress inducer hydrogen peroxide (100 mu M) was significantly suppressed in PrP super(C)-cells as compared to PrP super(KO)-cells. Together, these results demonstrate that prion protein interferes with divalent metal Mn uptake and protects against Mn-induced oxidative stress and apoptotic cell death. The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide repeat regions that bind to several divalent metals, suggesting that the prion proteins may alter the toxic effect of environmental neurotoxic metals. In the present study, we systematically examined whether prion protein modifies the neurotoxicity of manganese (Mn) by comparing the effect of Mn on mouse neural cells expressing prion protein (PrP(C)-cells) and prion-knockout (PrP(KO)-cells). Exposure to Mn (10microM-10mM) for 24 h produced a dose-dependent cytotoxic response in both PrP(C)-cells and PrP(KO)-cells. Interestingly, PrP(C)-cells (EC(50) 117.6microM) were more resistant to Mn-induced cytotoxicity, as compared to PrP(KO)-cells (EC(50) 59.9microM), suggesting a protective role for PrP(C) against Mn neurotoxicity. Analysis of intracellular Mn levels showed less Mn accumulation in PrP(C)-cells as compared to PrP(KO)-cells, but no significant changes in the expression of the metal transporter proteins transferrin and DMT-1. Furthermore, Mn-induced mitochondrial depolarization and reactive oxygen species (ROS) generation were significantly attenuated in PrP(C)-cells as compared to PrP(KO)-cells. Measurement of antioxidant status revealed similar basal levels of glutathione (GSH) in PrP(C)-cells and PrP(KO)-cells; however, Mn treatment caused greater depletion of GSH in PrP(KO)-cells. Mn-induced mitochondrial depolarization and ROS production were followed by time- and dose-dependent activation of the apoptotic cell death cascade involving caspase-9 and -3. Notably, DNA fragmentation induced by both Mn treatment and the oxidative stress inducer hydrogen peroxide (100microM) was significantly suppressed in PrP(C)-cells as compared to PrP(KO)-cells. Together, these results demonstrate that prion protein interferes with divalent metal Mn uptake and protects against Mn-induced oxidative stress and apoptotic cell death. |
Author | Kanthasamy, Arthi Saetveit, Nathan J. Kanthasamy, Anumantha G. Anantharam, Vellareddy Houk, Robert S. Choi, Christopher J. |
AuthorAffiliation | Ames Laboratory, U. S. Department of Energy, Department of Chemistry, Iowa State University Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, Iowa State University |
AuthorAffiliation_xml | – name: Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, Iowa State University – name: Ames Laboratory, U. S. Department of Energy, Department of Chemistry, Iowa State University |
Author_xml | – sequence: 1 givenname: Christopher J. surname: Choi fullname: Choi, Christopher J. organization: Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, College of Veterinary Medicine – sequence: 2 givenname: Vellareddy surname: Anantharam fullname: Anantharam, Vellareddy organization: Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, College of Veterinary Medicine – sequence: 3 givenname: Nathan J. surname: Saetveit fullname: Saetveit, Nathan J. organization: Ames Laboratory, U.S. Department of Energy, Department of Chemistry, Iowa State University, Ames, Iowa 50011 – sequence: 4 givenname: Robert S. surname: Houk fullname: Houk, Robert S. organization: Ames Laboratory, U.S. Department of Energy, Department of Chemistry, Iowa State University, Ames, Iowa 50011 – sequence: 5 givenname: Arthi surname: Kanthasamy fullname: Kanthasamy, Arthi organization: Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, College of Veterinary Medicine – sequence: 6 givenname: Anumantha G. surname: Kanthasamy fullname: Kanthasamy, Anumantha G. email: akanthas@iastate.edu, To whom correspondence should be addressed at Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, 2062 Veterinary Medicine Bldg., Iowa State University, Ames, IA 50011. Fax: (515) 294-2315. akanthas@iastate.edu. organization: Neuroscience and Toxicology Graduate Programs, Iowa Center for Advanced Neurotoxicology, Department of Biomedical Sciences, College of Veterinary Medicine |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17483122$$D View this record in MEDLINE/PubMed |
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Copyright | The Author 2007. Published by Oxford University Press on behalf of the Society of Toxicology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org 2007 |
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Snippet | The normal prion protein is abundantly expressed in the central nervous system, but its biological function remains unclear. The prion protein has octapeptide... The normal prion protein is abundantly expressed in the CNS, but its biological function remains unclear. The prion protein has octapeptide repeat regions that... |
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SubjectTerms | Animals Apoptosis Caspase 3 - metabolism Caspase 9 - metabolism caspases Cell Line DNA Fragmentation Glutathione - metabolism manganese Manganese - toxicity metals Mice Mice, Knockout Neurons neurotoxicity Oxidative Stress prion disease PrPC Proteins - deficiency PrPC Proteins - genetics PrPC Proteins - metabolism Reactive Oxygen Species - metabolism ROS Superoxide Dismutase - metabolism |
Title | Normal Cellular Prion Protein Protects against Manganese-Induced Oxidative Stress and Apoptotic Cell Death |
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