ORIGINAL PAPER Oxidative stress in human in sustained and white coat hypertension

• Published in: International journal of clinical practice (Esher) Vol. 60; no. 12; p. 1565
• Main Authors: Caner, M, Karter, Y, Uzun, H, ÇURGUNLU, A, VEHID, S, Balci, H, Yucel, R, GÜNER, I, Kutlu, A, YALDIRAN, A, ÖZTÜRK, E
• Format: Journal Article
• Language: English
• Published: London Hindawi Limited 01.12.2006
• Subjects: Hypertension; Kinetics; Oxidation; Proteins; Stress
• ISSN: 1368-5031; 1742-1241
• DOI: 10.1111/j.1742-1241.2006.00959.x

Oxidative stress is thought to play a critical role in the pathogenesis of hypertension. Protein oxidation is defined here as the covalent modification of a protein induced either directly by reactive oxygen species or indirectly by reaction with secondary by-products of oxidative stress. The aim of our study was to evaluate the protein oxidation and to examine the function of the antioxidative system in sustained and white coat hypertensives (WCH) and compare with normotensives. This study was designed to investigate the protein oxidation parameters [protein carbonyls (PCOs)] in sustained hypertensives (17 males and 20 females) and WCH (18 males and 19 females). PCO and the endogenous antioxidant components protein thiol (P-SH), CuZn-superoxide dismutase (CuZn-SOD) and glutathione (GSH) were analysed using spectrophotometric and kinetic methods. Sustained hypertensive and WCH groups exhibited higher protein oxidation and lower P-SH, CuZn-SOD and GSH activities than normotensives. With regard to these parameters, there was no significant difference between sustained hypertensive and WCH groups. Blood pressure correlates positively with PCO groups and negatively with others. There exists an imbalance between oxidants and antioxidants in WCH because of the increase of oxidants associated with the decrease of antioxidant capacity. This may cause endothelial dysfunction just like in sustained hypertension. It may be necessary to add antioxidants to conventional antihypertensive therapy to balance the oxidative status in WCH. [PUBLICATION ABSTRACT]