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Comparison of homocitrulline and carbamylated albumin as biomarkers of carbamylation reactions in hemodialyzed patients. | LitMetric

AI Article Synopsis

  • - The study examined the link between homocitrulline (HCit) levels and albumin carbamylation in hemodialyzed patients participating in the NICOREN trial, using specialized testing methods.
  • - Results revealed that HCit concentrations were significantly correlated with the degree of albumin carbamylation, showing that higher HCit levels indicate more carbamylation in patients.
  • - Importantly, neither sevelamer nor nicotinamide treatments reduced HCit or carbamylated albumin levels after 24 weeks, suggesting that HCit could serve as a useful biomarker for protein carbamylation in clinical settings.

Article Abstract

To describe the association between levels of homocitrulline (HCit) and the degree of albumin carbamylation in a cohort of hemodialyzed patients. Plasma total and protein-bound HCit concentrations in samples from hemodialyzed patients included in NICOREN trial were determined by LC-MS/MS at baseline and after 24 weeks of treatment with either sevelamer or nicotinamide. HCit concentrations at all timepoints and in both groups were positively and significantly correlated with the degree of albumin carbamylation. Plasma concentrations of total HCit, protein-bound HCit and carbamylated albumin did not decrease after 24 weeks of treatment with either sevelamer or nicotinamide. The present results demonstrate that plasma total and protein-bound HCit concentrations were closely associated with albumin carbamylation in hemodialyzed patients. Therefore, total and protein-bound HCit concentrations might be valuable biomarkers of the overall intensity of protein carbamylation in this context. Given the less complex and time-consuming analytical methods required, these markers should be favored in future clinical studies of carbamylation reaction.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10689527PMC
http://dx.doi.org/10.1007/s00726-023-03306-0DOI Listing

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