Alterations in conformational state of albumin in plasma in chronic hemodialyzed patients

Autor: Krzysztof Gwozdzinski, Anna Pieniazek, Zbigniew Zbrog, Lukasz Gwozdzinski
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Male
0301 basic medicine
Antioxidant
Protein Conformation
Physiology
medicine.medical_treatment
lcsh:Medicine
Biochemistry
chemistry.chemical_compound
tert-Butylhydroperoxide
Medicine and Health Sciences
Hydrogen peroxide
lcsh:Science
chemistry.chemical_classification
Multidisciplinary
biology
Organic Compounds
Fatty Acids
Chemical Reactions
Oxides
Middle Aged
Lipids
Peroxides
Body Fluids
Hydroperoxide
Chemistry
Blood
Nephrology
Physical Sciences
Iodoacetamide
Thiol
Anatomy
Oxidation-Reduction
Research Article
Serum albumin
Blood Plasma
03 medical and health sciences
Thiols
Renal Dialysis
Albumins
Medical Dialysis
Oxidation
medicine
Humans
Sulfhydryl Compounds
Serum Albumin
Aged
Reactive oxygen species
030102 biochemistry & molecular biology
Organic Chemistry
lcsh:R
Chemical Compounds
Albumin
Biology and Life Sciences
Proteins
Fatty acid
Hydrogen Peroxide
030104 developmental biology
chemistry
biology.protein
lcsh:Q
Zdroj: PLoS ONE, Vol 13, Iss 3, p e0192268 (2018)
PLoS ONE
ISSN: 1932-6203
Popis: Objective In chronic hemodialyzed (CH) patients the balance between production of reactive oxygen species and antioxidant defense system is disturbed and shifted towards oxidative conditions. The properties of albumin in CH patients were studied before hemodialysis (HD) and post-HD. Methods Two oxidants were applied, organic t-butyl hydroperoxide (t-BOOH) and inorganic hydroperoxide (H2O2), for oxidation of albumin molecules. By comparison, albumin from healthy donors was also modified by both oxidants. The thiol content in albumin was determined by the Ellman method. Albumin properties were evaluated with the spin labelling technique using two covalently bound spin labels, maleimide (MSL) and iodoacetamide (ISL), and fatty acid spin probe, 16-doxylstearic acid (16-DS). Results A decrease in thiols level in HD albumin was greater than in control albumin. The t-BOOH modified the microenvironment at the binding site of MSL and ISL in control albumin molecules to a greater extent than hydrogen peroxide. Control albumin treated with t-BOOH and H2O2 showed an increase in the mobility of 16-DS. However, no changes were observed in albumin from CH patients treated with either of the oxidizing agents. Conclusion Both oxidants induced strong conformational changes in albumin from healthy volunteers, but were less effective or ineffective in modification of albumin derived from CH patients. These results show that albumin from CH patients is highly modified in vivo and is not vulnerable to oxidation in the same way as normal albumin.
Databáze: OpenAIRE
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