|Year : 2022 | Volume
| Issue : 4 | Page : 653-658
Study the profile of some antioxidant markers in diabetic mellitus and non-diabetic patients with cardiovascular disease
Israa Ghassan Zainal
Department of Chemistry, College of Science, University of Kirkuk, Kirkuk, Iraq
|Date of Submission||22-Aug-2022|
|Date of Acceptance||08-Sep-2022|
|Date of Web Publication||09-Jan-2023|
Israa Ghassan Zainal
Department of Chemistry, College of Science, University of Kirkuk, Kirkuk
Source of Support: None, Conflict of Interest: None
Background: Cardiovascular diseases (CVDs) claim the lives of millions worldwide. Objective: Evaluate the levels of some antioxidant biomarkers in sera of patients with CVDs with and without diabetes mellitus type 2. Materials and Methods: Includes 100 samples in 68 patients (40 with CVDs and 28 CVDs with diabetic), and 32 healthy subjects. Results: Serum (Albumin, thiol, thiol/T.protein, amine, free amine/ T.protein, carbonyl, carbonyl/ T.protein, and Ischemia modified albumin (IMA)) showed a stronger response, a significant rise in carbonyl and carbonyl/TP, and a significant reduction in thiol and thiol/TP in the patients with CVDs with T2D compared to CVDs may be a good factor to differentiate them or predict more serious complications. Conclusions: Oxidation markers may be useful in monitoring CVDs with and without diabetes.
Keywords: Antioxidant markers, cardiovascular diseases, HAS, IMA, type 2 diabetes
|How to cite this article:|
Zainal IG. Study the profile of some antioxidant markers in diabetic mellitus and non-diabetic patients with cardiovascular disease. Med J Babylon 2022;19:653-8
|How to cite this URL:|
Zainal IG. Study the profile of some antioxidant markers in diabetic mellitus and non-diabetic patients with cardiovascular disease. Med J Babylon [serial online] 2022 [cited 2023 Feb 6];19:653-8. Available from: https://www.medjbabylon.org/text.asp?2022/19/4/653/367337
| Introduction|| |
Fatness, diabetes, too little exercise, smoking, and other variable lifestyle factors account for about 50% of the risk of “Cardiovascular diseases” CVDs. Death is the most dreaded complication of CVDs and remains one of the important global factors of mortality due to the alarming prevalence of CVDs in the population. The common complications of CVDs divided to several types including: Angina, cardiac arrest, atrial fibrillation, heart failure, Pulmonary embolism, Peripheral artery disease, heart attack, and Strokes. One of the major contributors to the growth and development of heart disease has been recognized as oxidative stress, Reactive oxygen species (ROS) have been identified to enhance the proliferation of cardiac fibroblasts. Decreased human serum albumin (HAS) concentrations are typically linked to an elevated risk of CVDs mortality; since it is the highest common extracellular type of protein, it performs a wide range of activities, such as transportation, controlling colloidal osmolality, and moderating sera redox homeostasis. Human serum albumin level decrease in chronic and acute illnesses, which provides accurate ideas on the early diagnosis of illnesses. Human serum albumin is a monomeric macromolecule having a molecular mass of about 66.5 kDa, HAS are a significant antioxidant source and are the biggest thiol group in the blood due to their high content. They have 35 cysteine residues that produce 17 disulfide bonds and just a single free cysteine at location 34. In normal persons, the Cys-34 is reduced by 70–80 percentage of HSA, which circulates as mono mercaptalbumin, while the Cys-34 is completely oxidized to sulfonic or sulfonic acid in 20–30% of HSA and linked to small molecule groups (cysteine, homocysteine, and glutathione) in the remaining five percentage of HSA moves as mercaptalbumin. Due to the limited half-life (20 days) for HAS molecular, it is a reliable redox status indicator of the level of limited time systemically oxidative stress. The far more common and widely employed indicator is “carbonyl stress” is protein carbonylation, which is believed to reflect carbonyl modification of amino residues. Carbonyl content concentration is perhaps the most typical and frequently used marker oxidation of proteins. IMA, which is changed in oxidative stress situations have been linked to endothelial L-arginine/nitric oxide pathway dysfunction and ischemia-reperfusion injury (affecting NO levels). As a result of a continuing ischemia event, IMA is HSA that is unable to connect with cobalt, it showed particularly effective in detecting acute myocardial ischemia. The purpose of this research was to determine the levels of many oxidative biomarkers in the serum of individuals with CVDs and CVDs with T2D, comprising whole protein content, HSA, globulin, A/G, free amino, carbonyl, thiol, and IMA compare with healthy people as control, in order to evaluate the possible change in the serum proteins of the studied patients and afterward, examining the association among biomarkers. in the patients’ groups.
| Materials and Methods|| |
From mid-January to the end of April 2022, the research performed in the Department of Chemistry at the University of Kirkuk, Iraq, in partnership with the Daquq general hospital.
Sixty-eight cases, depending on their age of 24–70 years, admitted to the Daquq general hospital were dedicated to the investigation. Cases were identified and categorized (40 samples as CVDs and 28 as CVDs with T2D) with of cardiac enzyme tests, X-rays, and results of the Electrocardiography when a patient is admitted. Thirty-two healthy people who had undergone a diagnostic test but showed no signs of cardiac disease were chosen as the control group. Specimens of serum were collected (5–6 ml) after 12 hours of fasting in gel tubes using a disposable syringe, and blood was taken by vein puncture without using the tourniquet. After 15 minutes at room temperature, centrifuged the gel tubes for (15) minutes at (2800 x g). The serum was collected and stored at deep freeze until utilizing it in experiments.
The collected samples are free from decomposition and turbidity to avoid any interference with the results, and patients do not suffer from other diseases outside the scope of the research topic.
Bromocresol green (BCG) is used to assess HSA. The concept is that HSA is bound with bromocresol color to create a chrysolite measured at 630 nm, with the amount of accessible HSA proportional to the rise in color. Lowry proposed a method in which bovine serum Albumin was employed as a control protein to calculate the total amounts of serum protein. The method proposed by Zaia, Barreto, and others was used to determine the free amino group spectrophotometrically. Elmman described a method for measuring total serum thiol concentration, the interaction between the thiol group and Ellman’s reagent (DTNB) results in the formation of a colored complex peak point at 412 nm. Calculated by utilizing the formula A = Ɛ. C. l. where: Ɛ=13,600 M-1cm-1.
The proteins’ carbonyl concentration was determined using the Levine, Garland procedure, utilizing the formula A = Ɛ. C. l, where: Ɛ=22,000 M-1cm-1. IMA level was determined in serum by Albumin Cobalt Binding Assay; Myocardial ischemia induces alterations in HSA, as seen by reduced exogenous cobalt (II) binding. According to the assay, there is an opposite correlation between the amount of albumin-bound cobalt and the level of color generation.
Graph Pad Prism V 9.0 (Graph Pad Software, San Diego, CA, USA) was utilized to do the statistical analysis, and the outcomes were presented as (mean ± SD). The independent t-test was used to compare the mean and standard deviation, and the correlation between the parameters and P ≤ 0.05 was used to assess statistical significance.
The study was conducted by the ethical principles that have their origin in the Declaration of Helsinki. It was carried out with patients verbal and analytical approval before sample was taken. The study protocol information and consent form were reviewed and approved by a local ethics committee according to document number 3/7/6141 (including the number and the date on (23/11/2021) to get this approval.
| Results|| |
The concentrations of T.protein, HSA, Globulin, Albumin/Globulin ratio A/G, Thiol, Free amine, Carbonyl, and IMA in the sera of all studied groups are shown in [Table 1].
|Table 1: Measurements of chemical parameters, that be expressed with (mean ± SD) for all groups under study|
Click here to view
The findings showed that there were no significant differences (P ≥ 0.05) for TP, globulin, and AGR levels in patients’ groups vs the control, HSA was significantly decreased (P ≤ 0.05) in patients with CVDs and CVDs with T2D compared with control, still their was a no discernible difference (P ≥ 0.05) among the two patient types. Both patients with CVDs and CVDs with T2D had a significant decrease for Thiol when vs the control, as well as a significant reduction (P ≤ 0.05) in CVDs with T2D patients when compared to CVD patients. A significant rise (P ≤ 0.05) in the concentrations of free amine, free amine/total protein, and IMA in patients’ groups compared to the control and a non-significant increase in it of cases with CVDs with T2D compared to CVDs. Finally, in both patient groups, there was a significant increase (P ≤ 0.05) for carbonyl, and carbonyl/TP when compared with control, also a significant rise (P ≤ 0.05) in the patient CVDs with T2D when compared with CVDs patients.
[Table 2] summarized the significant Pearson correlation (r) between the examined variables in the groups of individuals with CVDs and those who also had T2D and CVDs
|Table 2: The correlation between the parameters that were assessed in CVD patients with and without T2D|
Click here to view
According to the findings, there was a favorable positive between [TP-globulin, A/G-CO/TP, A/G-amino/TP, A/G-thiol/TP, CO-CO/TP, CO-CO/TP, CO/TP-amino/TP, amino-amino/TP and thiol-thiol/TP] and there were negative correlation coefficient between [TP-A/G, TP-CO/TP, TP-amino/TP, TP-thiol/TP, globulin-A/G, globulin-CO/TP, globulin-amino/TP, globulin-thiol/TP, CO-thiol, CO-thiol/TP and CO/TP – thiol], in both patients groups.
| Discussion|| |
Proteins are important targets for oxidation reactions described as a mismatch in how free radicals are formed and the antioxidant reaction within cells, because they are abundant in tissues, extracellular cells, and physiological fluids, as well as their quick reaction rates with oxidants, furthermore, oxidative stress can cause. Lipids and carbohydrates decompose into extremely reactive compounds that attack proteins in a variety of functional places. As a result, a wide range of proteins that modify non-reversible modifications contribute factors that speed up the development of many diseases. Because of the chemical stability of some protein oxidation products and produced in high quantities, they are attractive candidates as oxidative damage indicators. The current investigation demonstrates strong observational links between HSA and the likelihood of CVDs and CVDs with T2D when compared with control. In Comparison to the control, HSA concentrations in both groups decreased significantly (P ≤ 0.05) Andreas Ronit et al they found similar results, they also discovered a drop in HSA levels in individuals with CVDs. Several theories have been offered to clarify the mechanisms that may help to explain the link between a drop in HSA and an increased risk of CVDs, the most obvious mechanism is inflammation. The liver produces HSA, When there is widespread inflammation, several acute-phase proteins instead of HSA, which is a negative acute-phase reactant, are produced. Another explanation is that decreased HSA indicates increased vascular permeability in inflammatory conditions, whereas C-reactive protein (CRP) does not detect, as fluid redistribution to the intercellular can swiftly and greatly change HSA levels. Furthermore, in the case of patients who have diabetes in addition to CVDs, other mechanisms affect the decrease in HSA level. First, diabetes can cause a reduction in liver albumin production. Second, processes involved in the formation of glycated albumin (GA) may result in a reduction in HSA. GA functions as an intermediate for “advanced glycation end products” (AGE) which result in inflammation and have an aberrant capacity to bind various ligands. Furthermore, there is proof that GA causes an immunological reaction that causes HSA levels to drop much lower, and increased oxidative stress has been related to insulin resistance and diabetes development. Third, as previously state, inflammation has a role in the etiology of diabetes.
When comparing the patient groups with control the results of free amino concentrations showed a statistically significant rise (P ≤ 0.05) in the cases groups. These results are supported by Li, Tie et al they found that in CVDs, the concentration of free amino increased. Furthermore, the findings of this study contradicted those of Trifunovic-Macedoljan J et al, they showed a reduction in the amount of free amine in Diabetes Mellitus patients. This study’s findings people with higher free thiol levels exhibited better glycemic control than those with lower amounts, and patients with CVDs also had low levels compared with control. The findings showed a significant decline (P ≤ 0.05) in the free thiol amounts in the sera of CVDs with T2D compared to CVDs patients, there was also a significant decrease (P ≤ 0.05) in thiol amounts in patients with CVDs compared with control. These findings were consistent with those of Emmelien E.M. et al and Amaal E Abdulla et al they discovered that individuals with T2D and CVDs had significantly lower thiol concentrations in patients compared with control. The findings of the thiol levels contradicted those of Adnan Khalaf, M, et al, who found a significant rise (P ≤ 0.05) in thiol levels in diabetic patients compared to control. Diabetes results in metabolic pathway abnormalities, an increase in free radicals, and higher glucose levels due to the impaired antioxidant systems. Protein thiol groups are one of the antioxidant systems, when proteins are exposed to oxidative stress, the thiol groups decrease and functional problems occur. The significance of oxidative stress in CVDs has received more attention in recent decades, as it has been linked to endothelial dysfunction. Thiol is an important component of redox signaling networks that are dynamic and complicated in the extracellular environment, where they have significant antioxidant action because of their ability to remove circulated reactive species quickly. Homocysteine, glutathione, and other small molecular weight thiols, account for a lesser percentage of extracellular thiols incorporated in plasma proteins. The most redox-active thiol groups are found in blood proteins. Because of its abundance and ability to transport thiols, experimentally HSA is this pool’s more significant component (Due to the presence of its lone free cysteine residue, Cys34). As a result of the preceding, serum levels of free thiol may be inversely connected to oxidative stress and the hazards it causes, such as CVDs and diabetes. Protein carbonyl production, which can result from direct free radical breakage of the side chains of amino acids is key evidence that proteins have oxidized. Protein oxidation was measured in this study by detecting protein carbonyl content. The outcomes showed a significantly rise (P ≤ 0.05) for carbonyl content in the sera of CVDs with T2D compared to CVDs and control, also revealed a significantly (P ≤ 0.05) higher carbonyl content in patients with CVDs compare with control. These findings were consistent with those of Abd I.K. and Sushmita Bora, et al they found that there was an increase in carbonyl levels in diabetes and CVDs patients respectively, however, this was in contrast to Adnan Khalaf, M. et al. findings. Platelets, which are circulating anucleate cells produced from megakaryocytes, play a critical role in the formation of CVDs. In prothrombotic cardiovascular events, ROS plays a significant part in platelet stress-induced signaling processes, platelet activation induces a pro-thrombotic phenotype and increases the risk of CVDs. IMA concentrations were found significantly rise (P ≤ 0.05) in CVDs with T2D and CVDs compared to control in this study. This result is confirmed by UVPU Sowjanya et al, and Amira Abdel Moneam Adly, et al they reported that the enhanced oxidative stress and free radical production resulted in wide vascular endothelial inflammation and the subsequent tissue hypoxia could be the causes of the strong correlation between higher serum IMA and HbA1c. For the generation of IMA, various mechanisms have been proposed. Acidosis, free iron, and copper ion release, hypoxia, rise free radical damaging, Na-Ca pump disruptions that depend on membrane energy are all possible consequences of cardiac ischemia, in each of which result in damage to the amino terminus of HSA.
For both patient groups, there was a significant inverse relationship between (Globulin-A/G, Carbonyl-Thiol, TP-A/G, and TP-Thiol/TP) and a significant positive correlation between (Carbonyl-Carbonyl/TP, and TP-Globulin). Current study outcomes were consistent with earlier investigations Adnan Khalaf, M, et al. This explains how a drop in HSA, which serves as an antioxidant in endothelial function and causes a relative rise in globulin levels, can result in a decrease in A/G (inverse relation), while also achieving (Positive association) between (TP-Globulin). Since protein thiol groups are one of the antioxidant systems, any increase in carbonyl content may result in a drop in thiol levels since protein carbonyl synthesis is a sign of dependent oxidative stress on the type of ROS (inverse relation).
| Conclusions|| |
The findings of this investigation showed that, in contrast to controls, oxidative protein markers increased in CVDs with T2D, it an increase in the patients with CVDs with T2D compared to CVDs. The aforementioned data could support a link between these
oxidation proteins and the aforementioned illnesses. Serum (HSA, thiol, thiol/T.protein, amine, free amine/ T.protein, carbonyl, carbonyl/ T.protein, and IMA) showed a stronger response, a significant rise in carbonyl and carbonyl/TP, and a significant reduction in thiol and thiol/TP in the patients with CVDs with T2D compared to CVDs may be a good factor to differentiate them or predict more serious complications. Patients with CVDs with T2D higher than patients with CVDs had more high correlations between biochemical markers. It’s possible that having T2D along with CVDs will enhance the likelihood that serious vascular problems. The correlation between (Carbonyl-Thiol/TP, and Thiol-Thiol/TP) is strong in Patients with CVDs but, is negligible in patients with CVDs with T2D this may serve as a good prognostic marker for patients with CVDs alone without T2D, whereas the strong correlation between (Globulin-amino/TP, and Carbonyl/TP-amino/TP) in patients with CVDs and T2D, and low correlation for same parameters in patients with CVDs may be referred to as significant indications of CVD patients with complication. Future research must confirm any possible associations between redox balance and the cardiovascular profile.
Financial support and sponsorship
Conflicts of interest
There are no conflicts of interest.
| References|| |
Khot UN, Khot MB, Bajzer CT, Sapp SK, Ohman EM, Brener SJ, et al
. Prevalence of conventional risk factors in patients with coronary heart disease. Jama 2003;290:898-904.
Shao C, Wang J, Tian J, Tang YD Coronary artery disease: From mechanism to clinical practice. Adv Exp Med Biol 2020;1177:1-36.
Cheng TH, Cheng PY, Shih NL, Chen IB, Wang DL, Chen JJ Involvement of reactive oxygen species in angiotensin II-induced endothelin-1 gene expression in rat cardiac fibroblasts. J Am Coll Cardiol 2003;42:1845-54.
Brioschi M, Gianazza E, Mallia A, Zoanni B, Altomare A, Fernandez AM, et al
. S-thiolation targets albumin in heart failure. Antioxidants 2020;9:1-13.
Kleinova M, Belgacem O, Pock K, Rizzi A, Buchacher A, Allmaier G Characterization of cysteinylation of pharmaceutical-grade human serum albumin by electrospray ionization mass spectrometry and low-energy collision-induced dissociation tandem mass spectrometry. Rapid Commun Mass Spectrom 2005;19:2965-73.
Kurano M, Yasukawa K, Ikeda H, Aoki J, Yatomi Y Redox state of albumin affects its lipid mediator binding characteristics. Free Radic Res 2019;53:892-900.
Adnan Khalaf M, Ghassan Zainal I Investigation of antioxidant markers in diabetic patients. Arch Razi Inst 2021;76:1453-60.
Kamel HH, Mostafa AHM, AL-Salahy MB, Walaa MS, WAHBA AA Protein carbonyl, oxidative stress, anemia, total free amino acids and sheep haemonchosis relationship. J Egypt Soc Parasitol 2018;48:21-30.
Mahmoud Saleh OF, Said NHE, Youssef Bahgat HM, El Ghaffar Mohamed NA, Fishawy HSE Serum ischemia modified albumin as a marker of complications in patients with type 2 diabetes mellitus. Endocrinol Diabetes Res 2019;13:2.
Shevtsova A, Gordiienko I, Tkachenko V, Ushakova G Ischemia-modified albumin: Origins and clinical implications. Dis Markers 2021;2021:9945424.
Shannon CM, Ballew SH, Daya N, Zhou L, Chang AR, Sang Y, et al
. Serum albumin and risks of hospitalization and death: Findings from the atherosclerosis risk in communities study. J Am Geriatr Soc 2021;69:2865-76.
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ Protein measurement with the folin phenol reagent. J Biol Chem 1951;193:265-75.
Zaia DAM, Barreto WJ, Santos NJ, Endo AS Spectrophotometric method for the simultaneous determination of proteins and amino acids with p-benzoquinone. Anal Chim Acta 1993;277:89-95.
Ellman GL Tissue sulfhydryl groups. Arch Biochem Biophys 1959;82:70-7.
Levine RL, Garland D, Oliver CN, Amici A, Climent I, Lenz AG, et al
. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 1990;186:464-78.
Oran I, Oran B Ischemia-modified albumin as a marker of acute coronary syndrome: The case for revising the concept of “N-terminal modification” to “fatty acid occupation” of albumin. Dis Markers 2017;2017:5692583.
Kehm R, Baldensperger T, Raupbach J, Höhn A Protein oxidation - formation mechanisms, detection and relevance as biomarkers in human diseases. Redox Biol 2021;42:101901.
Ronit A, Kirkegaard-Klitbo DM, Dohlmann TL, Lundgren J, Sabin CA, Phillips AN, et al
. Plasma albumin and incident cardiovascular disease: Results from the CGPS and an updated meta-analysis. Arterioscler Thromb Vasc Biol 2020;40:473-82.
Kaptoge S, Seshasai SR, Gao P, Freitag DF, Butterworth AS, Borglykke A, et al
. Inflammatory cytokines and risk of coronary heart disease: New prospective study and updated meta-analysis. Eur Heart J 2014;35:578-89.
DeFronzo RA, Reeves WB, Awad AS Pathophysiology of diabetic kidney disease: Impact of SGLT2 inhibitors. Nat Rev Nephrol 2021;17:319-34.
Trifunović-Macedoljan J, Pantelić N, Damjanović A, Rašković S, Nikolić-Đurović M, Pudar G, et al
. LC/DAD determination of biogenic amines in serum of patients with diabetes mellitus, chronic urticaria or Hashimoto’s thyroiditis. J Serbian Chem Soc 2016;81:487-98.
Rabbani G, Ahn SN Review: Roles of human serum albumin in prediction, diagnoses and treatment of COVID-19. Int J Biol Macromol 2021;193:948-55.
Li T, Luo HH, Feng XF, Bai Y, Fang ZZ, Wu GG, et al
. Plasma free amino acids and risk of cardiovascular disease in chinese patients with type 2 diabetes. Front Endocrinol (Lausanne) 2020;11:519923.
Schillern EEM, Pasch A, Feelisch M, Waanders F, Hendriks SH, Mencke R, et al
. Serum free thiols in type 2 diabetes mellitus: A prospective study. J Clin Transl Endocrinol 2019;16:100182.
Abdulle AE, Bourgonje AR, Kieneker LM, Koning AM, la Bastide-van Gemert S, Bulthuis MLC, et al
. Serum free thiols predict cardiovascular events and all-cause mortality in the general population: A prospective cohort study. BMC Med 2020;18:130.
Balali-Mood M, Naseri K, Tahergorabi Z, Khazdair MR, Sadeghi M Toxic mechanisms of five heavy metals: Mercury, lead, chromium, cadmium, and arsenic. Front Pharmacol 2021;12:643972.
Cervantes Gracia K, Llanas-Cornejo D, Husi H CVD and oxidative stress. J Clin Med 2017;6:22.
Turell L, Radi R, Alvarez B The thiol pool in human plasma: The central contribution of albumin to redox processes. Free Radic Biol Med 2013;65:244-53.
Lee JO, Choi N, Lee JW, Song S, Kim YP Rapid electrokinetic detection of low-molecular-weight thiols by redox regulatory protein-DNA interaction in microfluidics. Sensors Actuators B Chem 2021;336:129735.
Ichihara S, Suzuki Y, Chang J, Kuzuya K, Inoue C, Kitamura Y, et al
. Involvement of oxidative modification of proteins related to ATP synthesis in the left ventricles of hamsters with cardiomyopathy. Sci Rep 2017;7:9243.
Abd IK, Zainal IG Assessment of biochemical parameters and study its correlation in ß-Thalassemia major patients and healthy controls in Kirkuk City, Iraq. Med J Babylon 2020; 17:172.
Bora S, Shankarrao Adole P Carbonyl stress in diabetics with acute coronary syndrome. Clin Chim Acta 2021;520:78-86.
Jain K, Tyagi T, Patell K, Xie Y, Kadado AJ, Lee SH, et al
. Age associated non-linear regulation of redox homeostasis in the anucleate platelet: Implications for CVD risk patients. Ebiomedicine 2019;44:28-40.
Sowjanya U, Sridevi C, Rajkumari DMM, Kasibabu A Study of ischemia modified albumin in type 2 diabetes as a marker of severity. J Dent Med Sci 2015;14:14-7.
Adly AAM, ElSherif NHK, Ismail EAR, Ibrahim YA, Niazi G, Elmetwally SH Ischemia-modified albumin as a marker of vascular dysfunction and subclinical atherosclerosis in β-thalassemia major. Redox Rep 2017;22:430-8.
Mishra B, Pandey S, Niraula SR, Rai BK, Karki P, Baral N, et al
. Utility of ischemia modified albumin as an early marker for diagnosis of acute coronary syndrome. J Nepal Health Res Counc 2018;16:16-21.
Kut K, Bartosz G, Soszyński M, Sadowska-Bartosz I Antioxidant properties of hispidulin. Nat Prod Res2022;36:6401-4.
Song YR, Kim JK, Lee HS, Kim SG, Choi EK Serum levels of protein carbonyl, a marker of oxidative stress, are associated with overhydration, sarcopenia and mortality in hemodialysis patients. BMC Nephrol 2020;21:281.
[Table 1], [Table 2]