Characteristic of the Oxidative Stress in Blood of Patients in Dependence of Community-Acquired Pneumonia Severity

Larissa Muravlyova; Vilen Molotovâ€“Luchankiy; Ryszhan Bakirova; Dmitriy Klyuyev; Ludmila Demidchik; Valentina Lee

doi:10.3889/oamjms.2016.040

Authors

Larissa Muravlyova State Medical University, Biological Chemistry, Karaganda 100008
Vilen Molotovâ€“Luchankiy State Medical University, Propaedeutics of Internal Diseases, Karaganda 100008
Ryszhan Bakirova State Medical University, Propaedeutics of Internal Diseases, Karaganda 100008
Dmitriy Klyuyev State Medical University, Biological Chemistry, Karaganda 100008
Ludmila Demidchik State Medical University, Biological Chemistry, Karaganda 100008
Valentina Lee State Medical University, Propaedeutics of Internal Diseases, Karaganda 100008

DOI:

https://doi.org/10.3889/oamjms.2016.040

Keywords:

community-acquired pneumonia, modified proteins, malondialdehyde, blood plasma, erythrocytes

Abstract

BACKGROUND: At the present time the alternation of the oxidative metabolism is considered as one of the leading pathogenic mechanisms in the development and progression of community-acquired pneumonia (CAP). However the nature and direction of the oxidative protein changes in CAP patientâ€™s blood had been almost unexplored.

AIM: To define oxidative and modified proteins in erythrocytes and blood plasma of CAP patients.

MATERIAL AND METHODS: Blood plasma and erythrocytes obtained from: 42 patients with moderate severity pneumonia, 12 patients with grave severity pneumonia and 32 healthy volunteers. Content of advanced oxidation protein products, malondialdehyde and reactive carbonyl derivatives were estimated as indicators of the oxidative stress and oxidative damage of proteins.

RESULTS: In patients with grave severity the level of oxidative proteins and MDA in erythrocytes exceeded both: control values and similar meanings in CAP patients with moderate severity. The further growth of MDA in this group patientsâ€™ blood plasma was observed, but the level of oxidative proteins decreased in comparison with those in CAP patients with moderate severity.

CONCLUSION: To sum up, our derived data show, that injury of erythrocytesâ€™ redox-status and blood plasma components plays an essential role in development and progression CAP.

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

Plum Analytics Artifact Widget Block

References

Kalinina EP. Regulatory mechanisms of the immune response in men with community-acquired pneumonia and chronic obstructive pulmonary disease: Dissertation for the degree of candidate of medical sciences. Vladivostok, 2009: 1-49.

Trefler S, Rodriguez A, Martin-Loeches I, et al. Oxidative stress in immunocompetent patients with severe community-acquired pneumonia. A pilot study. Med Intensiva. 2014;38:73-82.

http://dx.doi.org/10.1016/j.medin.2013.01.004

PMid:23485500

Castillo RL, Carrasco RA, Alvarez PI, et al. Relationship between severity of adult community-acquired pneumonia and impairment of the antioxidant defense system. Biol Res. 2013;46:207-213.

http://dx.doi.org/10.4067/S0716-97602013000200013

PMid:23959020

Katsoulis K, Kontakiotis T, Baltopoulos G, et al. Total antioxidant status and severity of community-acquired pneumonia: are they correlated? Respiration. 2005;72:381-387.

http://dx.doi.org/10.1159/000086252

PMid:16088281

Pikuza OI, Zakirova AM, Rashitov LF, et al. Lipid peroxidation and serum zinc status of community-acquired pneumonia among schoolchildren. Pediatrics. 2012:91:30-32.

Majewska E, Kasielski M, Luczynski R, et al. Elevated exhalation of hydrogen peroxide and thiobarbituric acid reactive substances in patients with community acquired pneumonia. Respiratory Medicine. 2004;98:669-676.

http://dx.doi.org/10.1016/j.rmed.2003.08.015

PMid:15250234

Zhiyou C, Liang-Jun Y. Protein oxidative modifications: beneficial roles in disease and health. J Biochem Pharmacol Res. 2013;1:15-26.

Wall SB, Oh JY, Diers AR, et al. Oxidative modification of proteins: an emerging mechanism of cell signaling. Front Physiol. 2012;14:369.

http://dx.doi.org/10.3389/fphys.2012.00369

Yan LJ. Protein redox modification as a cellular defense mechanism against tissue ischemic injury. Oxid Med Cell Longev. 2014;Article ID 343154.

Grimsrud PA, Xie H, Griffin TJ, et al. Oxidative stress and covalent modification of protein with bioactive aldehydes. J Biol Chem. 2008;32:21837-21841.

http://dx.doi.org/10.1074/jbc.R700019200

PMid:18445586 PMCid:PMC2494933

Semchyshyn HM. Reactive carbonyl species in vivo: generation and dual biological effects. The Scientific World Journal. 2014;Article ID 417842.

Piwowar A. Advanced oxidation protein products. Part I. Mechanism of the formation, characteristics and property. Pol Merkur Lekarski. 2010;28:166-169.

Piwowar A, Knapik-Kordecka M, Warwas M. AOPP and its relations with selected markers of oxidative/antioxidative system in type 2 diabetes mellitus. Diabetes Research and Clinical Practice. 2007;77:188-192.

http://dx.doi.org/10.1016/j.diabres.2006.12.007

PMid:17335928

Tiwar BK, Pandey KB, Abidi AB, et al. Markers of oxidative stress during diabetes mellitus. Journal of Biomarkers. 2013;Article ID 378790.

Mohanty JG, Nagababu E, Rifkind JM. Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging. Front Physiol. 2014;5:84.

http://dx.doi.org/10.3389/fphys.2014.00084

PMid:24616707 PMCid:PMC3937982

Rifkind JM, Nagababu E. Hemoglobin redox reactions and red blood cell aging. Antioxid Redox Signal. 2013;18:2274-2283.

http://dx.doi.org/10.1089/ars.2012.4867

PMid:23025272 PMCid:PMC3638511

Witko-Sarsat V, Frielander M, Capeillere-Blandin C, et al. Advanced oxidation protein products as a novel marker of oxidative stress in uremia. Kidney Int. 1996;49:1304-1313.

http://dx.doi.org/10.1038/ki.1996.186

PMid:8731095

Korobeinikova EN. Modification of the definition of lipid peroxidation products in the reaction with thiobarbituric acid. Lab Work. 1989;7:8-10.

Goncharenko MS, Latinova AM. Method of assessment of peroxide oxidation of lipids. Lab Case. 1985;1:60-61.

Levine RL, Garland D, Oliver CN, et al. Determination of carbonyl content in oxidatively modified proteins. Method Enzymol. 1990;186:464-478.

http://dx.doi.org/10.1016/0076-6879(90)86141-H

Steel C, Cockeran R, Anderson R, et al. Overview of community-acquired pneumonia and the role of inflammatory mechanisms in the immunopathogenesis of severe pneumococcal disease. Mediators of Inflammation. 2013; Article ID 490346.

Rahman I. Oxidative stress in pathogenesis of chronic obstructive pulmonary disease: cellular and molecular mechanisms. Cell Biochem Biophys. 2005;43(1):167-188.

http://dx.doi.org/10.1385/CBB:43:1:167

Xiang W, Weisbach V, Sticht H, et al. Oxidative stress-induced posttranslational modifications of human hemoglobin in erythrocytes. Arch Biochem Biophys. 2013;529(1):34-44.

http://dx.doi.org/10.1016/j.abb.2012.11.002

PMid:23201302

Huertas A, Das SR, Emin M, et al. Erythrocytes induce proinflammatory endothelial activation in hypoxia. Am J Respir Cell Mol Biol. 2013;48:78-86.

http://dx.doi.org/10.1165/rcmb.2011-0402OC

PMid:23043086 PMCid:PMC3547079

Michelis R, Kristal B, Zeitun T, et al. Albumin oxidation leads to neutrophil activation in vitro and inaccurate measurement of serum albumin in patients with diabetic nephropathy. Free Radic Biol Med. 2013;60:49-55.

http://dx.doi.org/10.1016/j.freeradbiomed.2013.02.005

PMid:23429046

Selmeci L, SzÐµkely M, Soos P, et al. Human blood plasma advanced oxidation protein products (AOPP) correlates with fibrinogen levels. Free Radic Res. 2006;40:952-958.

http://dx.doi.org/10.1080/10715760600818789

PMid:17015275