4/2012
vol. 8
Letter to the Editor
Postep Kardiol Inter 2012; 8, 4 (30): 365
Online publish date: 2013/05/13
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Dear Editor,
We read the article “Paraoxonase-1 activity and the levels of lipids and lipid peroxidation markers in arterial versus venous blood samples in coronary angiography patients” written by Göçmen et al. with great interest [1]. The authors aimed to explore whether arterial blood samples withdrawn from femoral arteries can be used to determine some biochemical parameters.
Coronary artery disease (CAD) is the leading cause of death worldwide [2]. Oxidized low-density lipoprotein (ox-LDL) is accepted to be a key factor of initiating and accelerating atherosclerosis. High-density lipoprotein-associated proteins like paraoxonase 1 (PON1) enzyme prevent lipid oxidation. Paraoxonase 1 hydrolyzes lipid peroxides in atherosclerotic lesions, where they promote progression of atherogenesis. Coronary artery disease is associated with decreased plasma PON1 activity [3]. Göçmen et al. [1] showed that arterial blood samples can also be used to determine these parameters as well as venous samples. This is an interesting study. On the other hand, we would like to make a minor criticism about the methodological aspect.
Blood samples were withdrawn at 8 am, after 12 h of fasting, from the femoral artery and vena mediana cubiti at the same time. However, it is impossible to perform all the coronary angiographies at the same time. It would be better if the authors explained this issue.
References
1. Göçmen AY, Gűműșlű S, Gűnaydin I, Semiz E. Paraoxonase-1 activity and the levels of lipids and lipid peroxidation markers in arterial versus venous blood samples in coronary angiography patients. Postep Kardiol Inter 2012; 8: 199-204.
2. Zalewski J, Nycz K, Przewłocki T, et al. Conservative strategy in patients with non-ST-segment elevation acute coronary syndromes Postep Kardiol Inter 2010; 6: 147-153.
3. Sesal C, Ciloglu F, Peker I, Sayar N. Role of angiotensin converting enzyme, paraoxonase 155, 192 gene polymorphisms in syndrome X and coronary heart disease. Pak J Biol Sci 2009; 12: 46-51.
Dear Editor,
We read the article “Paraoxonase-1 activity and the levels of lipids and lipid peroxidation markers in arterial versus venous blood samples in coronary angiography patients” written by Göçmen et al. with great interest [1]. The authors aimed to explore whether arterial blood samples withdrawn from femoral arteries can be used to determine some biochemical parameters.
Coronary artery disease (CAD) is the leading cause of death worldwide [2]. Oxidized low-density lipoprotein (ox-LDL) is accepted to be a key factor of initiating and accelerating atherosclerosis. High-density lipoprotein-associated proteins like paraoxonase 1 (PON1) enzyme prevent lipid oxidation. Paraoxonase 1 hydrolyzes lipid peroxides in atherosclerotic lesions, where they promote progression of atherogenesis. Coronary artery disease is associated with decreased plasma PON1 activity [3]. Göçmen et al. [1] showed that arterial blood samples can also be used to determine these parameters as well as venous samples. This is an interesting study. On the other hand, we would like to make a minor criticism about the methodological aspect.
Blood samples were withdrawn at 8 am, after 12 h of fasting, from the femoral artery and vena mediana cubiti at the same time. However, it is impossible to perform all the coronary angiographies at the same time. It would be better if the authors explained this issue.
References
1. Göçmen AY, Gűműșlű S, Gűnaydin I, Semiz E. Paraoxonase-1 activity and the levels of lipids and lipid peroxidation markers in arterial versus venous blood samples in coronary angiography patients. Postep Kardiol Inter 2012; 8: 199-204.
2. Zalewski J, Nycz K, Przewłocki T, et al. Conservative strategy in patients with non-ST-segment elevation acute coronary syndromes Postep Kardiol Inter 2010; 6: 147-153.
3. Sesal C, Ciloglu F, Peker I, Sayar N. Role of angiotensin converting enzyme, paraoxonase 155, 192 gene polymorphisms in syndrome X and coronary heart disease. Pak J Biol Sci 2009; 12: 46-51.
Copyright: © 2013 Termedia Sp. z o. o. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) License ( http://creativecommons.org/licenses/by-nc-sa/4.0/), allowing third parties to copy and redistribute the material in any medium or format and to remix, transform, and build upon the material, provided the original work is properly cited and states its license.
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