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Part 2: Cellular and Molecular Biology of the Peritoneum and Peritoneal Dialysis |
Warwick Medical School, Clinical Sciences Research Institute, University of Warwick, University Hospital, Coventry, U.K.
Correspondence to: P.J. Thornalley, Clinical Sciences Research Institute, Warwick Medical School, University of Warwick, University Hospital, Clifford Bridge Road, Coventry CV2 2DX, U.K. P.J.Thornalley{at}warwick.ac.uk
Proteolysis products of proteins damaged by glycation, oxidation, and
nitration—glycated, oxidized, and nitrated amino acids (glycation,
oxidation, and nitration free adducts)—are waste products normally
excreted in urine and cleared in peritoneal dialysate. Glucose degradation
products in peritoneal dialysis (PD) fluids may increase protein damage,
giving rise to increased protein glycation, oxidation, and nitration adduct
residues of proteins and increased flux of glycation, oxidation, and nitration
free adducts. Increased protein damage has been linked to mortality in
end-stage renal disease. Reliable quantitation of markers for adducts of
protein glycation, oxidation, and nitration is required for mechanistic
studies and for morbidity and mortality risk analysis in PD patients. We
review the available analytical techniques for such quantitation. Stable
isotopic dilution analysis with tandem mass spectrometry is the "gold
standard." This method needs to be applied further in the study of PD
and to validate other techniques so that the effect of PD on the metabolism
and clearance of damaged proteins and related products can be quantified, and
so that best-practice fluid management can be established to minimize
cardiovascular risk.
KEY WORDS: Glycation; oxidative stress; nitrosative stress; tandem mass spectrometry; immunoassay; skin autofluorescence.
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