Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist gegebenenfalls nur via VPN oder Shibboleth (DFN-AAI) möglich. mehr Informationen...
Ergebnis 7 von 217

Details

Autor(en) / Beteiligte
Titel
Cys34-cysteinylated human serum albumin is a sensitive plasma marker in oxidative stress-related chronic diseases
Ist Teil von
  • PloS one, 2014-01, Vol.9 (1), p.e85216-e85216
Ort / Verlag
United States: Public Library of Science
Erscheinungsjahr
2014
Quelle
MEDLINE
Beschreibungen/Notizen
  • The degree of oxidized cysteine (Cys) 34 in human serum albumin (HSA), as determined by high performance liquid chromatography (HPLC), is correlated with oxidative stress related pathological conditions. In order to further characterize the oxidation of Cys34-HSA at the molecular level and to develop a suitable analytical method for a rapid and sensitive clinical laboratory analysis, the use of electrospray ionization time-of-flight mass spectrometer (ESI-TOFMS) was evaluated. A marked increase in the cysteinylation of Cys34 occurs in chronic liver and kidney diseases and diabetes mellitus. A significant positive correlation was observed between the Cys-Cys34-HSA fraction of plasma samples obtained from 229 patients, as determined by ESI-TOFMS, and the degree of oxidized Cys34-HSA determined by HPLC. The Cys-Cys34-HSA fraction was significantly increased with the progression of liver cirrhosis, and was reduced by branched chain amino acids (BCAA) treatment. The changes in the Cys-Cys34-HSA fraction were significantly correlated with the alternations of the plasma levels of advanced oxidized protein products, an oxidative stress marker for proteins. The binding ability of endogenous substances (bilirubin and tryptophan) and drugs (warfarin and diazepam) to HSA purified from chronic liver disease patients were significantly suppressed but significantly improved by BCAA supplementation. Interestingly, the changes in this physiological function of HSA in chronic liver disease were correlated with the Cys-Cys34-HSA fraction. In conclusion, ESI-TOFMS is a suitable high throughput method for the rapid and sensitive quantification of Cys-Cys34-HSA in a large number of samples for evaluating oxidative stress related chronic disease progression or in response to a treatment.
Sprache
Englisch
Identifikatoren
ISSN: 1932-6203
eISSN: 1932-6203
DOI: 10.1371/journal.pone.0085216
Titel-ID: cdi_plos_journals_1476179784
Format
Schlagworte
Aged, Albumin, Alternations, Amino acids, Amino Acids, Branched-Chain - administration & dosage, Analysis, Bilirubin, Bilirubin - chemistry, Biology, Biomarkers - blood, Biomedical laboratories, Chain branching, Chromatography, Chronic Disease, Chronic diseases, Chronic illnesses, Cirrhosis, Correlation, Cysteine - chemistry, Cysteine - metabolism, Development and progression, Diabetes, Diabetes mellitus, Diabetes Mellitus - blood, Diabetes Mellitus - diagnosis, Diabetes Mellitus - drug therapy, Diazepam, Diazepam - chemistry, Drugs, Ethics, Female, Gastroenterology, Glycation End Products, Advanced - blood, Hepatology, High performance liquid chromatography, Hospitals, Human serum albumin, Humans, Ionization, Kidney diseases, Kidney transplantation, Laboratories, Liquid chromatography, Liver, Liver cirrhosis, Liver Cirrhosis - blood, Liver Cirrhosis - diagnosis, Liver Cirrhosis - diet therapy, Liver diseases, Male, Mass spectrometry, Medical treatment, Medicine, Middle Aged, Models, Molecular, Nephrology, Oxidation, Oxidation-Reduction, Oxidative Stress, Patients, Pharmaceutical sciences, Physiological aspects, Plasma levels, Protein Binding, Proteins, Renal Insufficiency - blood, Renal Insufficiency - diagnosis, Renal Insufficiency - diet therapy, Serum albumin, Serum Albumin - chemistry, Serum Albumin - metabolism, Signal transduction, Spectrometry, Mass, Electrospray Ionization, Studies, Supplements, Tryptophan, Tryptophan - chemistry, Type 2 diabetes, Warfarin, Warfarin - chemistry

Weiterführende Literatur

Empfehlungen zum selben Thema automatisch vorgeschlagen von bX