Hyperhomocysteinemia, paraoxonase activity and risk of coronary artery disease

Kerkeni, Mohsen; Addad, Faouzi; Chauffert, M; Chuniaud, Laurence; Miled, A.; Trivin, F; Maaroufi, Khira

doi:10.1016/j.clinbiochem.2006.05.010

Cited by 58 publications

(34 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Overall, the findings of the present study confirm the observations by Sakuta et al, though we extended the analysis on both genders. Moreover, we also ruled out any potential confounding influence from the concentration of folic acid and B12, which are recognized as major determinants of plasma homocysteine concentrations (8 (10).…”

Section: Discussionmentioning

confidence: 99%

Plasma .GAMMA.-glutamyl Transferase Activity Predicts Homocysteine Concentration in a Large Cohort of Unselected Outpatients

et al. 2008

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Plasma .GAMMA.-glutamyl Transferase Activity Predicts Homocysteine Concentration in a Large Cohort of Unselected Outpatients

et al. 2008

View full text Add to dashboard Cite

show abstract

“…Cystatin C level has been shown to reflect subtle decreases in renal funcion that independently predicts total homocysteine level among stable renal transplant recipients [17]. A negative correlation have been found between PON1 activity and homocysteine level in patients with coronary artery disease [18]. However, the relationship between cystatin C and PON1 acivity has not been investigated.…”

Section: Introductionmentioning

confidence: 96%

Serum Cystatin C Is a Determinant of Paraoxonase Activity in Hemodialyzed and Renal Transplanted Patients

et al. 2009

View full text Add to dashboard Cite

Abstract.Background: Human paraoxonase-1 (PON1) inhibits LDL-oxidation and atherogenesis, and possesses lactonase activity. Decreased PON1 activity was found in hemodialyzed and renal transplanted patients. Cystatin C plays a protective role in atherosclerosis, and is a new, sensitive marker of renal function. The relationship between these two markers in renal failure has not been investigated. Aims: The goal of this study was to clarify the relationship between PON1 activity, cystatin C and homocysteine in chronic renal failure. We also determined the levels of oxidatively modified LDL (oxLDL) and thiobarbituric acid reactive substances (TBARS) to characterize lipid peroxidation. Patients and methods: 74 hemodialized (HD), 171 renal transplanted patients (TRX), and 110 healthy controls (C) were involved in the study. PON1 activity and TBARS levels were measured spectrophotometrically. OxLDL level was determined with sandwich ELISA. Results: There was a negative correlation between PON1 activity and cystatin C level. Homocysteine level correlated negatively with PON1 activity, and positively with cystatin C level. OxLDL and TBARS levels were significantly higher in the HD and TRX groups compared to C. Conclusions: Cystatin C may be a good predictive factor not only for homocysteine levels but for the antioxidant status in patients with renal failure and renal transplantation.

show abstract

“…[179][180][181] Other studies have focused on whether polymorphisms in the PON genes may predispose to stroke. PON promoter and coding region polymorphisms were shown to be associated with increased stroke and coronary artery disease risk in several studies, 175,[182][183][184] but a recent study of the polymorphisms in PON I, PON II, and PON III in ischemic stroke patients showed no association with an increased risk of ischemic stroke. 185 …”

Section: Paraoxonase (Pon)mentioning

confidence: 99%

“…174 Additional studies showed that PON I also reduces homocysteine thiolactone in human blood, while an increase in homocysteine levels lowers PON I activity. 175 Transgenic and knockout studies show that PON I deficiency results in oxidative stress in macrophages, as well as in serum, [176][177][178] suggesting a protective effect for this enzyme. Both HDL and PON are also found in the interstitial fluid where they can exert their antioxidant effects.…”

Section: Paraoxonase (Pon)mentioning

confidence: 99%

Redox Regulation in the Extracellular Environment

Ottaviano

Handy

Loscalzo

2008

Circ J

128

100

View full text Add to dashboard Cite

Molecular oxygen is involved in the oxidation of substrates used to produce energy; however, normal metabolism can also generate harmful (bio)chemical byproducts. These deleterious products are partially reduced forms of oxygen, and include free radicals such as superoxide anion radical, hydroxyl radical, or highly oxidizing non-radical species such as hydrogen peroxide (H2O2) and lipid peroxides, which are collectively known as ROS. 1 ROS typically derive from normal metabolism, activated leukocytes, and ambient oxygen in the environment. The production and accumulation of ROS and their downstream effects can be controlled or attenuated by antioxidants. When the ability of antioxidants to eliminate harmful cellular and extracellular ROS is compromised, the balance between ROS generation and antioxidant function to eliminate ROS is shifted in favor of an accumulation of oxidants, which defines the state of oxidative stress in a cell or organism. Oxidative damage can affect DNA, lipids, and proteins, and eventually compromise cell integrity. Many studies have implicated ROS in the pathological processes leading to heart disease, cancer, aging, AIDS, and inflammatory and autoimmune diseases.Oxidants, especially free radicals, are highly reactive. Superoxide can react within milliseconds with nitric oxide (NO) to produce peroxynitrite (ONOO -), a reactive nitrogen species (RNS). The nitrosium cation and nitroxyl anion are other RNS derived from NO. 2 Peroxynitrite is a strong oxidant involved in the nitrosative modification of proteins and lipids. Owing to its rapid reaction with NO, superoxide may modulate NO bioavailability and, subsequently, regulate vascular function. 3 Circulation Journal Vol.72, January 2008The cytosol, mitochondria, peroxisomes, and plasma are all potential sites of ROS formation. 4 The major sources of ROS are enzymatic via nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (Nox), xanthine oxidase, myeloperoxidase, endothelial NO synthase (eNOS), or as a consequence of normal mitochondrial respiration. In vascular cells, other enzymatic sources of ROS include cytochrome P450 isoenzymes, lipoxygenase, cyclooxygenase, heme oxygenase, and glucose oxidase. 1,3,[5][6][7] Most reviews to date have focused on the role of intracellular antioxidants that eliminate ROS from the intracellular environment. There are, however, several extracellular antioxidants that also play an equally important role in limiting ROS accumulation in the extracellular environment. Along with limiting ROS accumulation, extracellular redox status is essential for maintaining protein stability and function.The major enzymes important for the elimination of extracellular H2O2 are glutathione peroxidase-3 (GPx-3) and peroxiredoxin IV (Prx IV). Other extracellular antioxidants involved in ROS elimination include paraoxonase (PON), thioredoxin (Trx), Trx reductase (TrxR), glutaredoxin (Grx), extracellular superoxide dismutase (EC-SOD), and extracellular glutathione (GSH).Some of these antioxidants, notably glutathione...

show abstract

Hyperhomocysteinemia, paraoxonase activity and risk of coronary artery disease

Cited by 58 publications

References 43 publications

Plasma .GAMMA.-glutamyl Transferase Activity Predicts Homocysteine Concentration in a Large Cohort of Unselected Outpatients

Plasma .GAMMA.-glutamyl Transferase Activity Predicts Homocysteine Concentration in a Large Cohort of Unselected Outpatients

Serum Cystatin C Is a Determinant of Paraoxonase Activity in Hemodialyzed and Renal Transplanted Patients

Redox Regulation in the Extracellular Environment

Contact Info

Product

Resources

About