Oxidation of peroxiredoxins and carbonylation of class I histone deacetylases by arachidonic acid metabolites

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Publication Type dissertation
School or College College of Pharmacy
Department Medicinal Chemistry
Author Doyle, Kelly
Title Oxidation of peroxiredoxins and carbonylation of class I histone deacetylases by arachidonic acid metabolites
Date 2010
Description Redox signaling is a mechanism that facilitates homeostasis during redox insult resulting from cellular respiration, defense, and inflammation. Cellular perception of, and adaptation to redox stress requires a stratified response mediated by key regulatory proteins that utilize cysteine residues as redox switches in response to a broad range of inorganic and organic oxidants and electrophiles. Lipid peroxidation and metabolism are major sources of endogenous reactive oxygen-ipid species and reactive carbonyl species which act on membrane, nuclear, and cytosolic proteins to elicit changes in cell signaling and gene expression. Cyclooxygenase and lipoxygenase metabolism of arachidonic acid leads to the formation of these reactive lipid species, yet very little is known about how these enzymes might govern cellular redox processes. This dissertation provides biochemical and biological evidence demonstrating how cyclooxygenase- and lipoxygenase-derived lipid hydroperoxides (oxidants) and ?,?-unsaturated carbonyls (electrophiles) function as redox signaling mediators.
Type Text
Publisher University of Utah
Subject Cyclooxygenase; Cyclopentenone; Histone deacetylase; Lipoxygenase; Peroxiredoxin; Redox Biochemistry
Subject LCSH Oxidation-reduction reaction -- Physiological effect
Dissertation Institution University of Utah
Dissertation Name PhD
Language eng
Rights Management ©Kelly Doyle
Format Medium application/pdf
Format Extent 8,073,462 bytes
Source Original housed in Marriott Library Special Collections, QP6.5 2010 .D69
ARK ark:/87278/s6zg76sg
Setname ir_etd
ID 192982
Reference URL https://collections.lib.utah.edu/ark:/87278/s6zg76sg