| Erythrocyte glutathione transferase: a potential new biomarker in chronic kidney diseases which correlates with plasma homocysteine. | |
| | |
MedLine Citation:
|
PMID: 21984376 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
|
The erythrocyte glutathione S-transferase (e-GST) is a member of a superfamily of inducible enzymes involved in cell detoxification that shows an increased expression in chronic kidney disease (CKD) patients. We propose a new automated analysis procedure for e-GST activity that has been validated in 72 CKD patients and 62 maintenance hemodialysis patients (MHD). Regression analysis was carried out to assess association between e-GST activity data, main clinical variables, and plasma homocysteine (Hcy), a modified sulfur amino acid known as potential risk factor for cardiovascular disease that is increased above normal levels in more than 90% of the uremic patients. An increased e-GST activity was confirmed in MHD patients (N = 62; 10.2 ± 0.4 U/gHb) compared with healthy subjects (N = 80; 5.8 ± 0.4 U/gHb), and as an original finding, a significant increase of e-GST activity was observed in pre-dialysis CKD patients with a positive correlation with disease severity weighted according to the four stages of "Kidney Disease Outcomes Quality Initiative" classification (7.4 ± 0.5, 8 ± 1, 9.5 ± 0.6, 12 ± 1 U/gHb, respectively). No correlation was found between e-GST activity and hemoglobin, transferrin, blood iron and the markers of systemic inflammation and renal function such as alpha-1 acid glycoprotein and high-sensitive C-Reactive Protein, beta-2 microglobulin and the index of malnutrition-inflammation PINI, while a significant correlation was observed for the first time between plasma Hcy and e-GST activity (r (2) = 0.64, P < 0.0001) in MHD patients. Hcy, however, was not identified as an inhibitor of e-GST enzyme. The results in this study suggest the potential for automated e-GST analysis as a valuable tool to further explore phase II-related uremic toxicity in CKD and MHD patients. |
| | |
Authors:
|
Mariarita Dessì; Annalisa Noce; Kutayba F Dawood; Francesco Galli; Massimo Taccone-Gallucci; Raffaele Fabrini; Alessio Bocedi; Renato Massoud; Giorgio Fucci; Anna Pastore; Simone Manca di Villahermosa; Viviana Zingaretti; Giorgio Federici; Giorgio Ricci |
Related Documents
:
|
22744736 - A clinicopathological study of serotonin of sigmoid colon mucosa in association with ch... 22166506 - Adjuvant laboratory marker of kawasaki disease; nt-pro-bnp or hs-crp? 22772776 - Transcatheter aortic valve implantation in patients with and without concomitant corona... 21981606 - Peyronie's disease in teenagers. 19558966 - Hepatic anaplerotic outflow fluxes are redirected from gluconeogenesis to lactate synth... 17024796 - Risk factors for postoperative chest wound infections due to gram-negative bacteria in ... |
Publication Detail:
|
Type: JOURNAL ARTICLE Date: 2011-10-8 |
Journal Detail:
|
Title: Amino acids Volume: - ISSN: 1438-2199 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
|
Created Date: 2011-10-10 Completed Date: - Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 9200312 Medline TA: Amino Acids Country: - |
Other Details:
|
Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
|
Department of Laboratory Medicine, University of Rome 'Tor Vergata', Rome, Italy. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Biophysical functionality in polysaccharides: from Lego-blocks to nano-particles.
Next Document: Insulin resistance and the metabolism of branched-chain amino acids in humans.