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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Payne, Deborah A. / Schlattmann, Peter / Tate, Jillian R.

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Plasma protein homocysteinylation in uremia

Alessandra F. Perna
  • 1First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Filomena Acanfora
  • 2First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Maria Grazia Luciano
  • 3First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Paola Pulzella
  • 4First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Rosanna Capasso
  • 5First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Ersilia Satta
  • 6First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Lombardi Cinzia
  • 7First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Rosa Maria Pollastro
  • 8First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Simona Iannelli
  • 9First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
/ Diego Ingrosso
  • 10Department of Biochemistry and Biophysics “F. Cedrangolo”, School of Medicine, Second University of Naples, Naples, Italy
/ Natale G. De Santo
  • 11First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy
Published Online: 2007-12-08 | DOI: https://doi.org/10.1515/CCLM.2007.336

Abstract

Protein homocysteinylation is proposed as one of the mechanisms of homocysteine toxicity. It occurs through various means, such as the post-biosynthetic acylation of free amino groups (protein-N-homocysteinylation, mediated by homocysteine thiolactone) and the formation of a covalent -S-S- bond found primarily with cysteine residues (protein-S-homocysteinylation). Both protein modifications are a cause of protein functional derangements. Hemodialysis patients in the majority of cases are hyperhomocysteinemic, if not malnourished. Protein-N-homocysteinylation and protein-S-homocysteinylation are significantly increased in hemodialysis patients compared to controls. Oral folate treatment normalizes protein-N-homocysteinylation levels, while protein-S-homocysteinylation is significantly reduced. Albumin binding experiments after in vitro homocysteinylation show that homocysteinylated albumin is significantly altered at the diazepam, but not at the warfarin and salicilic acid binding sites.

Clin Chem Lab Med 2007;45:1678–82.

Keywords: albumin; folate; hemodialysis; homocysteine; protein homocysteinylation; uremia

Corresponding author: Alessandra F. Perna, MD, PhD, Division of Nephrology/Department of Pediatrics, Second University of Naples, Via Pansini 5, Ed. 17, Naples, 80131 Italy Phone: +39-081-5666651, Fax: +39-081-5666655,


Received: 2007-06-19

Accepted: 2007-08-10

Published Online: 2007-12-08

Published in Print: 2007-12-01


Citation Information: Clinical Chemical Laboratory Medicine. Volume 45, Issue 12, Pages 1678–1682, ISSN (Online) 14374331, ISSN (Print) 14346621, DOI: https://doi.org/10.1515/CCLM.2007.336, December 2007

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