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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

Editorial Board Member: Gillery, Philippe / Kazmierczak, Steven / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Schlattmann, Peter / Whitfield, John B.

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Rank 5 out of 29 in category Medical Laboratory Technology in the 2013 Thomson Reuters Journal Citation Report/Science Edition

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Plasma protein homocysteinylation in uremia

Alessandra F. Perna1 / Filomena Acanfora2 / Maria Grazia Luciano3 / Paola Pulzella4 / Rosanna Capasso5 / Ersilia Satta6 / Lombardi Cinzia7 / Rosa Maria Pollastro8 / Simona Iannelli9 / Diego Ingrosso10 / Natale G. De Santo11

1First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

2First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

3First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

4First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

5First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

6First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

7First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

8First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

9First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

10Department of Biochemistry and Biophysics “F. Cedrangolo”, School of Medicine, Second University of Naples, Naples, Italy

11First Division of Nephrology, School of Medicine, Second University of Naples, Naples, Italy

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,

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

Publication History

Received:
2007-06-19
Accepted:
2007-08-10
Published Online:
2007-12-08

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

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