2017
DOI: 10.1016/j.bbrc.2017.03.147
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Pyridoxamine scavenges protein carbonyls and inhibits protein aggregation in oxidative stress-induced human HepG2 hepatocytes

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Cited by 12 publications
(4 citation statements)
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“…Protein carbonyls increase: Carbonyl stress; production of conformationally altered polypeptide chains, which contributes to cellular dysfunction; excessive aggregation of proteins by promoting unfolding and formation of noncovalent, as well as covalent bonds between proteins; increased toxicity; may lead to apoptotic cell death [154,155].…”
Section: Oxidative Nitrosative and Sulfuric Stress In Schizophreniamentioning
confidence: 99%
“…Protein carbonyls increase: Carbonyl stress; production of conformationally altered polypeptide chains, which contributes to cellular dysfunction; excessive aggregation of proteins by promoting unfolding and formation of noncovalent, as well as covalent bonds between proteins; increased toxicity; may lead to apoptotic cell death [154,155].…”
Section: Oxidative Nitrosative and Sulfuric Stress In Schizophreniamentioning
confidence: 99%
“…MDA, a common lipid peroxidation agent and an indicator for lipid peroxidation of the cell membrane, had certain cytotoxicity. PCO, a sign of oxidative damage of proteins, could cause conformational changes in the polypeptide chain, resulting in a loss of protein function . MPO produced by neutrophils could promote oxidative stress damage by activating chlorine molecules .…”
Section: Resultsmentioning
confidence: 99%
“…Oxidative stress leads to the non-enzymatic modification of specific amino acid residues, where aldehyde or ketone functional groups are introduced, this is known as carbonylation [21]. Protein carbonylation can have deleterious effects on cell function, since it can lead to protein dysfunction and to the production of potentially harmful protein aggregates [22]. In addition, Protein carbonyl groups can be used as biomarkers for oxidative damage to proteins [23].…”
Section: Introductionmentioning
confidence: 99%