Current Search: Hernandez, Caesar (x)
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Title
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Does methionine sulfoxide reductase have a role in maintaining adequate dopamine levels in drosophila melanogaster?.
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Creator
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Hernandez, Caesar, Binninger, David, Graduate College
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Date Issued
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2013-04-12
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PURL
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http://purl.flvc.org/fcla/dt/3361311
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Subject Headings
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Drosophila melanogaster, Methionine Sulfoxide Reductases, Dopamine
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Format
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Document (PDF)
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Title
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Methionine Sulfoxide Reductase Msr Deficiency Leads to a Reduction in Dopamine Levels in Drosophila.
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Creator
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Hernandez, Caesar, Weissbach, Herbert, Binninger, David, Graduate College
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Abstract/Description
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Biological homeostasis relies on protective mechanisms that respond to cellular oxidation caused primarily by free radical reactions. Methionine sulfoxide reductases Msr are a class of enzymes that reverse oxidative damage to methionine. The focus of this study is on the relationship between Msr and dopamine in Drosophila. Dopaminergic neurons in drosophila have comparable roles to those found in humans. A deficit in dopamine leads to the onset of many neurological disorders including the...
Show moreBiological homeostasis relies on protective mechanisms that respond to cellular oxidation caused primarily by free radical reactions. Methionine sulfoxide reductases Msr are a class of enzymes that reverse oxidative damage to methionine. The focus of this study is on the relationship between Msr and dopamine in Drosophila. Dopaminergic neurons in drosophila have comparable roles to those found in humans. A deficit in dopamine leads to the onset of many neurological disorders including the loss of fine motor control—a neurodegenerative condition characteristic of Parkinson’s disease PD. We have found that dopamine levels in the heads of MsrAΔ/ΔBΔ/Δ mutants are significantly reduced in comparison to the wild type. In addition, we have found that TH protein and expression levels are markedly reduced in an Msr-deficient system. Our findings suggest that it is possible the Msr system plays an important role in maintaining dopaminergic neurons alive, and thus, is protectant of the CNS.
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Date Issued
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2014
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PURL
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http://purl.flvc.org/fau/fd/FA00005820
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Format
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Document (PDF)
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Title
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Methionine sulfoxide reductase (Msr) deficiency leads to a reduction of dopamine levels in Drosophila.
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Creator
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Hernandez, Caesar, Binninger, David, Weissbach, Herbert, Florida Atlantic University, Charles E. Schmidt College of Science, Department of Biological Sciences
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Abstract/Description
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Biological homeostasis relies on protective mechanisms that respond to cellular oxidation caused primarily by free radical reactions. Methionine sulfoxide reductases (Msr) are a class of enzymes that reverse oxidative damage to methionine in proteins. The focus of this study is on the relationship between Msr and dopamine levels in Drosophila. Dopaminergic neurons in Drosophila have comparable roles to those found in humans. A deficit in dopamine leads to the onset of many neurological...
Show moreBiological homeostasis relies on protective mechanisms that respond to cellular oxidation caused primarily by free radical reactions. Methionine sulfoxide reductases (Msr) are a class of enzymes that reverse oxidative damage to methionine in proteins. The focus of this study is on the relationship between Msr and dopamine levels in Drosophila. Dopaminergic neurons in Drosophila have comparable roles to those found in humans. A deficit in dopamine leads to the onset of many neurological disorders including the loss of fine motor control—a neurodegenerative condition characteristic of Parkinson’s disease (PD). We found that dopamine levels in the heads of MsrAΔ/ΔBΔ/Δ mutants are significantly reduced in comparison to MsrA ⁺/⁺ B⁺/⁺ heads. In addition, wefound protein and expression levels are markedly reduced in an Msr-deficient system. Our findings suggest an important role for the Msr system in the CNS.
Show less
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Date Issued
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2014
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PURL
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http://purl.flvc.org/fau/fd/FA00004202, http://purl.flvc.org/fau/fd/FA00004202
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Subject Headings
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Cellular signal transduction, Dopamine -- Receptors, Drosophila melanogaster -- Genetics, Mitochondrial pathology, Proteins -- Chemical modification
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Format
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Document (PDF)