1
40
2
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1002/pmic.200500447" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/pmic.200500447</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
1250-1260
Issue
4
Volume
6
Search for Full-text
Locate full-text within NEOMED Library's e-journal collections
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Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Increased Oxidation And Degradation Of Cytosolic Proteins In Alcohol-exposed Mouse Liver And Hepatoma Cells
Publisher
An entity responsible for making the resource available
Proteomics
Date
A point or period of time associated with an event in the lifecycle of the resource
2006
2006-02
Subject
The topic of the resource
alcoholism; apoptosis; Biochemistry & Molecular Biology; CYP2E1; cytochrome p-4502e1; Degradation; disease; ethanol; in-vitro; induced; injury; nitric-oxide; oxidative stress; oxidized proteins; peroxiredoxin; protein; protein oxidation; rat-liver; stress
Creator
An entity primarily responsible for making the resource
Kim B J; Hood B L; Aragon R A; Hardwick Jr; Conrads T R; Veenstra T D; Song B J
Description
An account of the resource
We recently developed a sensitive method using biotin-N-maleimide (biotin-NM) as a probe to positively identify oxidized mitochondrial proteins. In this study, biotin-NM was used to identify oxidized cytosolic proteins in alcohol-fed mouse livers. Alcohol treatment for 6 wk elevated the levels of CYP2E1 and nitrotyrosine, a marker of oxidative stress. Markedly increased levels of oxidized proteins were detected in alcohol-fed mouse livers compared to pair-fed controls. The biotin-NM-labeled oxidized proteins from alcohol-exposed mouse livers were subsequently purified with streptavidin-agarose and resolved on 2-DE. More than 90 silver-stained protein spots that displayed differential intensities on 2-D gels were identified by MS. Peptide sequence analysis revealed that many enzymes or proteins involved in stress response, chaperone activity, intermediary metabolism, and antioxidant defense systems such as peroxiredoxin were oxidized after alcohol treatment. Smaller fragments of many proteins were repeatedly detected only in alcohol-fed mice, indicating that many oxidized proteins after alcohol exposure were degraded. Immunoblot results showed that the level of oxidized peroxiredoxin (inactivated) was markedly increased in the alcohol-exposed mouse livers and ethanol-sensitive hepatoma cells compared to the corresponding controls. Our results may explain the underlying mechanism for cellular dysfunction and increased susceptibility to other toxic agents following alcohol-mediated oxidative stress.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1002/pmic.200500447" target="_blank" rel="noreferrer noopener">10.1002/pmic.200500447</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2006
alcoholism
Apoptosis
Aragon R A
Biochemistry & Molecular Biology
Conrads T R
CYP2E1
cytochrome p-4502e1
degradation
Disease
ETHANOL
Hardwick Jr
Hood B L
in-vitro
Induced
Injury
Journal Article or Conference Abstract Publication
Kim B J
nitric-oxide
Oxidative Stress
oxidized proteins
peroxiredoxin
Protein
Protein oxidation
proteomics
rat-liver
Song B J
Stress
Veenstra T D
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1016/j.freeradbiomed.2009.06.017" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.freeradbiomed.2009.06.017</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
767-778
Issue
6
Volume
47
Search for Full-text
Locate full-text within NEOMED Library's e-journal collections
<p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p>
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Role of peroxisome proliferator-activated receptor-alpha in fasting-mediated oxidative stress
Publisher
An entity responsible for making the resource available
Free Radical Biology and Medicine
Date
A point or period of time associated with an event in the lifecycle of the resource
2009
2009-09
Subject
The topic of the resource
Aldehyde dehydrogenase; Biochemistry & Molecular Biology; differential expression; dismutase; Endocrinology & Metabolism; Fasting; fatty-acid oxidation; glutathione-s-transferase; hepatic steatosis; Lipid peroxidation; Lipid peroxidation; liver; manganese-superoxide-dismutase; mitochondrial aldehyde dehydrogenase; nitric-oxide; Null mice; oxidative stress; PPAR-alpha; PPAR-alpha; Protein nitration; Protein oxidation; rat-liver; Steatosis; Superoxide
Creator
An entity primarily responsible for making the resource
Abdelmegeed M A; Moon K H; Hardwick J P; Gonzalez F J; Song B J
Description
An account of the resource
The peroxisome proliferator-activated receptor-alpha (PPAR alpha) regulates lipid homeostasis, particularly in the liver. This study was aimed at elucidating the relationship between hepatosteatosis and oxidative stress during fasting. Fasted Ppara-null mice exhibited marked hepatosteatosis, which was associated with elevated levels of lipid peroxidation, nitric oxide synthase activity, and hydrogen peroxide accumulation. Total glutathione (GSH), mitochondrial GSH, and the activities of major antioxidant enzymes were also lower in the fasted Ppara-null mice. Consequently, the number and extent of nitrated proteins were markedly increased in the fasted Ppara-null mice, although high levels of protein nitration were still detected in the fed Ppara-null mice while many oxidatively modified proteins were only found in the fasted Ppara-null mice. However, the role of inflammation in increased oxidative stress in the fasted Ppara-null mice was minimal based on the similar levels of tumor necrosis factor-alpha change in all groups. These results with increased oxidative stress observed in the fasted Ppara-null mice compared with other groups demonstrate a role for PPAR alpha in fasting-mediated oxidative stress and that inhibition of PPAR alpha functions may increase the susceptibility to oxidative damage in the presence of another toxic agent. Published by Elsevier Inc.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.freeradbiomed.2009.06.017" target="_blank" rel="noreferrer noopener">10.1016/j.freeradbiomed.2009.06.017</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2009
Abdelmegeed M A
Aldehyde Dehydrogenase
Biochemistry & Molecular Biology
differential expression
dismutase
Endocrinology & Metabolism
Fasting
fatty-acid oxidation
Free Radical Biology and Medicine
glutathione-s-transferase
Gonzalez F J
Hardwick J P
hepatic steatosis
Journal Article or Conference Abstract Publication
Lipid Peroxidation
Liver
manganese-superoxide-dismutase
mitochondrial aldehyde dehydrogenase
Moon K H
nitric-oxide
Null mice
Oxidative Stress
PPAR-alpha
Protein nitration
Protein oxidation
rat-liver
Song B J
Steatosis
superoxide