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Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities

Reactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxid... Full description

Journal Title: Antioxidants & redox signaling 2011, Vol.15 (7), p.1957-1997
Main Author: Lubos, Edith
Other Authors: Loscalzo, Joseph , Handy, Diane E.
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Mary Ann Liebert, Inc
ID: ISSN: 1523-0864
Link: https://www.ncbi.nlm.nih.gov/pubmed/21087145
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title: Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities
format: Article
creator:
  • Lubos, Edith
  • Loscalzo, Joseph
  • Handy, Diane E.
subjects:
  • Active oxygen
  • Amino Acid Sequence
  • Animals
  • Antioxidants
  • Cardiovascular Diseases - etiology
  • Cardiovascular Diseases - genetics
  • Cardiovascular Diseases - therapy
  • Cell Death
  • Cellular signal transduction
  • Comprehensive Invited Review
  • Diabetes Mellitus - etiology
  • Diabetes Mellitus - genetics
  • Diabetes Mellitus - therapy
  • Enzyme Inhibitors - pharmacology
  • Enzyme Inhibitors - therapeutic use
  • Gene Expression
  • Gene Expression Regulation
  • Genetic Predisposition to Disease
  • Glutathione Peroxidase - antagonists & inhibitors
  • Glutathione Peroxidase - chemistry
  • Glutathione Peroxidase - genetics
  • Glutathione Peroxidase - metabolism
  • Health aspects
  • Humans
  • Molecular Sequence Data
  • Neoplasms - etiology
  • Neoplasms - genetics
  • Neoplasms - therapy
  • Oxidation-Reduction
  • Oxidative Stress
  • Peroxidase
  • Physiological aspects
  • Polymorphism, Genetic
  • Protein Conformation
  • Reactive Oxygen Species - metabolism
  • Risk Factors
  • Selenocysteine - chemistry
  • Selenocysteine - metabolism
ispartof: Antioxidants & redox signaling, 2011, Vol.15 (7), p.1957-1997
description: Reactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explores the molecular mechanisms involved in regulating the expression and function of GPx-1, with an emphasis on the role of GPx-1 in modulating cellular oxidant stress and redox-mediated responses. As a selenocysteine-containing enzyme, GPx-1 expression is subject to unique forms of regulation involving the trace mineral selenium and selenocysteine incorporation during translation. In addition, GPx-1 has been implicated in the development and prevention of many common and complex diseases, including cancer and cardiovascular disease. This review discusses the role of GPx-1 in these diseases and speculates on potential future therapies to harness the beneficial effects of this ubiquitous antioxidant enzyme. Antioxid. Redox Signal. 15, 1957–1997.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 1523-0864
fulltext: fulltext
issn:
  • 1523-0864
  • 1557-7716
url: Link


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descriptionReactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explores the molecular mechanisms involved in regulating the expression and function of GPx-1, with an emphasis on the role of GPx-1 in modulating cellular oxidant stress and redox-mediated responses. As a selenocysteine-containing enzyme, GPx-1 expression is subject to unique forms of regulation involving the trace mineral selenium and selenocysteine incorporation during translation. In addition, GPx-1 has been implicated in the development and prevention of many common and complex diseases, including cancer and cardiovascular disease. This review discusses the role of GPx-1 in these diseases and speculates on potential future therapies to harness the beneficial effects of this ubiquitous antioxidant enzyme. Antioxid. Redox Signal. 15, 1957–1997.
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subjectActive oxygen ; Amino Acid Sequence ; Animals ; Antioxidants ; Cardiovascular Diseases - etiology ; Cardiovascular Diseases - genetics ; Cardiovascular Diseases - therapy ; Cell Death ; Cellular signal transduction ; Comprehensive Invited Review ; Diabetes Mellitus - etiology ; Diabetes Mellitus - genetics ; Diabetes Mellitus - therapy ; Enzyme Inhibitors - pharmacology ; Enzyme Inhibitors - therapeutic use ; Gene Expression ; Gene Expression Regulation ; Genetic Predisposition to Disease ; Glutathione Peroxidase - antagonists & inhibitors ; Glutathione Peroxidase - chemistry ; Glutathione Peroxidase - genetics ; Glutathione Peroxidase - metabolism ; Health aspects ; Humans ; Molecular Sequence Data ; Neoplasms - etiology ; Neoplasms - genetics ; Neoplasms - therapy ; Oxidation-Reduction ; Oxidative Stress ; Peroxidase ; Physiological aspects ; Polymorphism, Genetic ; Protein Conformation ; Reactive Oxygen Species - metabolism ; Risk Factors ; Selenocysteine - chemistry ; Selenocysteine - metabolism
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descriptionReactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explores the molecular mechanisms involved in regulating the expression and function of GPx-1, with an emphasis on the role of GPx-1 in modulating cellular oxidant stress and redox-mediated responses. As a selenocysteine-containing enzyme, GPx-1 expression is subject to unique forms of regulation involving the trace mineral selenium and selenocysteine incorporation during translation. In addition, GPx-1 has been implicated in the development and prevention of many common and complex diseases, including cancer and cardiovascular disease. This review discusses the role of GPx-1 in these diseases and speculates on potential future therapies to harness the beneficial effects of this ubiquitous antioxidant enzyme. Antioxid. Redox Signal. 15, 1957–1997.
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1Amino Acid Sequence
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4Cardiovascular Diseases - etiology
5Cardiovascular Diseases - genetics
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7Cell Death
8Cellular signal transduction
9Comprehensive Invited Review
10Diabetes Mellitus - etiology
11Diabetes Mellitus - genetics
12Diabetes Mellitus - therapy
13Enzyme Inhibitors - pharmacology
14Enzyme Inhibitors - therapeutic use
15Gene Expression
16Gene Expression Regulation
17Genetic Predisposition to Disease
18Glutathione Peroxidase - antagonists & inhibitors
19Glutathione Peroxidase - chemistry
20Glutathione Peroxidase - genetics
21Glutathione Peroxidase - metabolism
22Health aspects
23Humans
24Molecular Sequence Data
25Neoplasms - etiology
26Neoplasms - genetics
27Neoplasms - therapy
28Oxidation-Reduction
29Oxidative Stress
30Peroxidase
31Physiological aspects
32Polymorphism, Genetic
33Protein Conformation
34Reactive Oxygen Species - metabolism
35Risk Factors
36Selenocysteine - chemistry
37Selenocysteine - metabolism
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9Comprehensive Invited Review
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35Risk Factors
36Selenocysteine - chemistry
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notesReviewing Editors: Regina Brigelius-Flohe, Fong-Fong Chu, Michael Davies, Sergey Dikalov, Aron Fisher, Leopold Flohé, Judith Haendeler, Mark Hampton, Matilde Maiorino, and Hiroshi Masutani
abstractReactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explores the molecular mechanisms involved in regulating the expression and function of GPx-1, with an emphasis on the role of GPx-1 in modulating cellular oxidant stress and redox-mediated responses. As a selenocysteine-containing enzyme, GPx-1 expression is subject to unique forms of regulation involving the trace mineral selenium and selenocysteine incorporation during translation. In addition, GPx-1 has been implicated in the development and prevention of many common and complex diseases, including cancer and cardiovascular disease. This review discusses the role of GPx-1 in these diseases and speculates on potential future therapies to harness the beneficial effects of this ubiquitous antioxidant enzyme. Antioxid. Redox Signal. 15, 1957–1997.
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