IMR Press / FBE / Volume 2 / Issue 4 / DOI: 10.2741/E199

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
RBC membrane damage and decreased band 3 phospho-tyrosine phosphatase activity are markers of COPD progression
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1 Departamento de Bioquimica y Biologia Molecular del Instituto Nacional de Perinatologia, Isidro Espinosa de los Reyes, Mexico
2 Departamento de Investigacion en Tabaquismo y EPOC, Instituto Nacional de Enfermedades Respiratorias (INER) “Ismael Cosio Villegas”, Mexico
Front. Biosci. (Elite Ed) 2010, 2(4), 1385–1393; https://doi.org/10.2741/E199
Published: 1 June 2010
Abstract

Injury to red blood cell (RBC) membrane by oxidative stress is of clinical importance in chronic obstructive pulmonary disease (COPD) which leads to oxidative stress (OE) during disease progression. Here, we studied the impact of this stress on injury to RBC membrane. Blood samples from both healthy volunteers (HV, n = 11) and controlled COPD patients (n=43) were divided according to their GOLD disease stage (I=7, II=21, III=10, IV=5). Plasma levels of paraoxonase (PON) activity, protein carbonyls (PC), conjugate dienes, lipohydroperoxides (LPH) and malondialdehyde (MDA) were determined and the PTPase, and the oxidative parameters were measured in RBC ghosts. Plasma from patients with COPD showed an increased oxidation of lipids and proteins, that correlated with the disease progression. PON activity decreased from GOLD stages II to IV and correlated with an increase in LPH (p < 0.0001, r = -0.8115). There was evidence of an increase in the oxidative biomarkers in RBCs, while the PTPase activity was diminished in stage III and IV of COPD. In conclusion, OE-induced injury associated with COPD is associated with an oxidative damage to the RBC membrane, with a concomitant decrease in the PTPase activity and altered function of anionic exchanger (AE1).

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