1
40
1
-
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/10.1006/abbi.2000.2119" target="_blank" rel="noreferrer noopener">http://doi.org/10.1006/abbi.2000.2119</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
81-87
Issue
1
Volume
384
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
Cytochrome P450 2e1 (cyp2e1)-dependent Production Of A 37-kda Acetaldehyde-protein Adduct In The Rat Liver
Publisher
An entity responsible for making the resource available
Archives of Biochemistry and Biophysics
Date
A point or period of time associated with an event in the lifecycle of the resource
2000
2000-12
Subject
The topic of the resource
acetaldehyde; acetaldehyde-protein adduct; alcohol; alcohol metabolism; aldehyde; Biochemistry & Molecular Biology; Biophysics; CYP2E1; CYP2E1 inhibitor; dehydrogenase; ethanol; expression; hepatocytes; hydroxyethyl radical adducts; induction; lipid-peroxidation; plasma-membrane
Creator
An entity primarily responsible for making the resource
Jeong K S; Soh Y; Jeng J; Felder M R; Hardwick J P; Song B J
Description
An account of the resource
Ethanol-inducible cytochrome P450 2E1 (CYP2E1) has been shown to be involved in the metabolism of both ethanol and acetaldehyde, Acetaldehyde, produced from ethanol metabolism, is highly reactive and can form various protein adducts, In this study, we investigated the role of CYP2E1 in the production of a 37-kDa acetaldehyde-protein adduct, Rats were pair-fed an isocaloric control or an alcohol liquid diet with and without cotreatment of YH439, an inhibitor of CYP2E1 gene transcription, for 4 weeks. The soluble proteins from rat livers of each group were separated on SDS-polyacrylamide gels followed by immunoblot analysis using specific antibodies against the 37-kDa protein acetaldehyde adduct, In addition, catalytic activities of the enzymes involved in alcohol and acetaldehyde metabolism were measured and compared with the adduct level, Immunoblot analysis revealed that the 37-kDa adduct, absent in the pair-fed control, was evident in alcohol-fed rats but markedly reduced by YH439 treatment. Immunohistochemical analysis also showed that the 37-kDa adduct is predominantly localized in the pericentral region of the liver where CYP2E1 protein is mainly expressed. This staining disappeared in the pericentral region after YH439 treatment. The levels of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase isozymes were unchanged after YH439 treatment. However, the level of the 37-kDa protein adduct positively correlated with the hepatic content of P4502E1, These data indicate that the 37-kDa adduct could be produced by CYP2E1-mediated ethanol metabolism in addition to the ADH-dependent formation. (C) 2000 Academic Press.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1006/abbi.2000.2119" target="_blank" rel="noreferrer noopener">10.1006/abbi.2000.2119</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2000
acetaldehyde
acetaldehyde-protein adduct
Alcohol
alcohol metabolism
aldehyde
Archives of biochemistry and biophysics
Biochemistry & Molecular Biology
Biophysics
CYP2E1
CYP2E1 inhibitor
dehydrogenase
ETHANOL
expression
Felder M R
Hardwick J P
hepatocytes
hydroxyethyl radical adducts
induction
Jeng J
Jeong K S
Journal Article or Conference Abstract Publication
lipid-peroxidation
plasma-membrane
Soh Y
Song B J