Linked Life Data

15788230

Source:http://linkedlifedata.com/resource/pubmed/id/15788230

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-3-24
pubmed:abstractText
Oxidative stress is a major pathogenetic event occurring in several liver disorders and is a major cause of liver damage due to Ischemia/Reperfusion (I/R) during liver transplantation. While several markers of chronic oxidative stress are well known, early protein targets of oxidative injury are not well defined. In order to identify these proteins, we used a differential proteomics approach to HepG2 human liver cells treated for 10 min with 500 microM H(2)O(2). This dose was sufficient to induce a slight decrease of total GSH and total protein thiol content without affecting cell viability. By performing Differential Proteomic analysis, by means of two-dimensional gel electrophoresis and MALDI-TOF mass spectrometry, we identified four proteins which resulted sensitive to H(2)O(2) treatment. The main changes were due to post-translational modifications of native polypeptides. Three of these proteins belong to the Peroxiredoxin family of hydroperoxide scavengers, namely PrxI, PrxII and PrxVI, that showed changes in their pI as result of overoxidation. Mass mapping experiments demonstrated the specific modification of peroxiredoxins active site thiol into sulphinic and/or sulphonic acid, thus explaining the increase in negative charge measured for these proteins. The oxidation kinetic of all peroxiredoxins was extremely rapid and sensitive, occurring at H(2)O(2) doses unable to affect the common markers of cellular oxidative stress. Recovery experiments demonstrated a quite different behaviour between 1-Cys and 2-Cys containing Prxs as their retroreduction features is concerned, thus suggesting a functional difference between different class of Prxs. The in vivo relevance of our study is demonstrated by the finding that overoxidation of PrxI occurs during I/R upon liver transplantation and is dependent on the time of warm ischemia. Our present data could be of relevance in setting up more standardized procedures to preserve organs for transplantations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1071-5762
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
255-68
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15788230-Biological Markers, pubmed-meshheading:15788230-Carcinoma, Hepatocellular, pubmed-meshheading:15788230-Cysteine, pubmed-meshheading:15788230-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:15788230-Humans, pubmed-meshheading:15788230-Hydrogen Peroxide, pubmed-meshheading:15788230-Ischemia, pubmed-meshheading:15788230-Liver, pubmed-meshheading:15788230-Liver Neoplasms, pubmed-meshheading:15788230-Liver Transplantation, pubmed-meshheading:15788230-Oxidants, pubmed-meshheading:15788230-Oxidation-Reduction, pubmed-meshheading:15788230-Oxidative Stress, pubmed-meshheading:15788230-Peroxidases, pubmed-meshheading:15788230-Peroxiredoxins, pubmed-meshheading:15788230-Proteomics, pubmed-meshheading:15788230-Reperfusion Injury, pubmed-meshheading:15788230-Spectrometry, Mass, Matrix-Assisted Laser...
pubmed:year
2005
pubmed:articleTitle
Overoxidation of peroxiredoxins as an immediate and sensitive marker of oxidative stress in HepG2 cells and its application to the redox effects induced by ischemia/reperfusion in human liver.
pubmed:affiliation
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, 34127 Trieste, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't