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1.
Artif Cells Nanomed Biotechnol ; 46(sup2): 727-736, 2018.
Article in English | MEDLINE | ID: mdl-29873516

ABSTRACT

In the present research, we assumed that reducing the amounts of E6 and E7 oncoproteins by a specific siRNA sequence and recovering p53 and RB proteins, along with the recovery of the FOXO1 protein by applying anti-miR-182, would increase apoptosis and reduce proliferation rate in cancer cells. The HPV16-positive CaSki cervical cancer cell line was used. 48 hours after transfection of siRNA for targeting E6 and E7 oncoproteins and anti-miR-182, expression of its cellular targets p53, p21 and FOXO1 was assessed by real-time PCR, western blot analysis and immunocytofluorescence staining. In all treatments, apoptosis rate and viability were evaluated using Annexin-V-FITC apoptosis detection kits and MTT assays, respectively. Among the designed siRNAs, E6-1 and E7-2 proved the most effective in reducing E6 and E7 expressions by increasing the apoptotic rates to 12.4% and 16%, respectively, after 48 hours. Also, using anti-miR-182 increased apoptotic rate to 12.7% 48 hours after transfection of cervical cancer cells. The combinational use of either E6-1 or E7-2 siRNAs with anti-miR-182 resulted in a rise in apoptosis to 19.3% and 26%, respectively, higher than those obtained from the individual application of either without anti-miR-182. The simultaneous use of siRNA E6-1 and siRNA E7-2 with cisplatin increased sensitivity to cisplatin and reduced the viability of the cancer cells as compared to the use of cisplatin alone. The simultaneous use of cisplatin and anti-miR-182 had no considerable effect on viability or apoptosis rate compared to cisplatin alone.


Subject(s)
Apoptosis/genetics , Human papillomavirus 16/physiology , MicroRNAs/genetics , Oncogene Proteins, Viral/genetics , Papillomavirus E7 Proteins/genetics , RNA, Small Interfering/genetics , Repressor Proteins/genetics , Uterine Cervical Neoplasms/pathology , Cell Line, Tumor , Cell Proliferation/genetics , Cell Survival/genetics , Cisplatin/pharmacology , Female , Forkhead Box Protein O1/genetics , Gene Expression Regulation, Neoplastic/genetics , Gene Knockdown Techniques , Humans , Oncogene Proteins, Viral/deficiency , Papillomavirus E7 Proteins/deficiency , RNA Interference , Repressor Proteins/deficiency
2.
Biochim Biophys Acta ; 1851(10): 1383-93, 2015 Oct.
Article in English | MEDLINE | ID: mdl-26215076

ABSTRACT

Chronic obstructive pulmonary disease (COPD) is a heterogeneous and progressive inflammatory condition that has been linked to the dysregulation of many metabolic pathways including lipid biosynthesis. How lipid metabolism could affect disease progression in smokers with COPD remains unclear. We cross-examined the transcriptomics, proteomics, metabolomics, and phenomics data available on the public domain to elucidate the mechanisms by which lipid metabolism is perturbed in COPD. We reconstructed a sputum lipid COPD (SpLiCO) signaling network utilizing active/inactive, and functional/dysfunctional lipid-mediated signaling pathways to explore how lipid-metabolism could promote COPD pathogenesis in smokers. SpLiCO was further utilized to investigate signal amplifiers, distributers, propagators, feed-forward and/or -back loops that link COPD disease severity and hypoxia to disruption in the metabolism of sphingolipids, fatty acids and energy. Also, hypergraph analysis and calculations for dependency of molecules identified several important nodes in the network with modular regulatory and signal distribution activities. Our systems-based analyses indicate that arachidonic acid is a critical and early signal distributer that is upregulated by the sphingolipid signaling pathway in COPD, while hypoxia plays a critical role in the elevated dependency to glucose as a major energy source. Integration of SpLiCo and clinical data shows a strong association between hypoxia and the upregulation of sphingolipids in smokers with emphysema, vascular disease, hypertension and those with increased risk of lung cancer.


Subject(s)
Databases, Factual , Lipid Metabolism/genetics , Pulmonary Disease, Chronic Obstructive , Signal Transduction/genetics , Sphingolipids , Sputum/metabolism , Female , Humans , Male , Pulmonary Disease, Chronic Obstructive/genetics , Pulmonary Disease, Chronic Obstructive/metabolism , Smoking/adverse effects , Smoking/genetics , Smoking/metabolism , Sphingolipids/genetics , Sphingolipids/metabolism
3.
Iran J Basic Med Sci ; 18(2): 115-21, 2015 Feb.
Article in English | MEDLINE | ID: mdl-25810884

ABSTRACT

OBJECTIVES: Some pathologic situations such as diabetes and metabolic syndrome are associated with alternation in nitric oxide level. Incidence of these condition increases with aging. On the other hand, insulin secretion is modulated by nitric oxide, and nitric oxide synthase (NOS) activity is also altered in diabetes. In this study, modification in the enzyme activity associated with aging and also optimized procedure for islet NOS assay was investigated. MATERIALS AND METHODS: Male Wistar rats were randomly divided in two experimental groups: A: adult rats; were 4 month old and B: old rats; were 12 month old. In all groups, plasma glucose, insulin and NOX (nitrite + nitrate = NOX) were measured, and also insulin secretion in isolated pancreatic islet with or without L-NAME was investigated. Furthermore, the inducible NOS activity with L-citrulline measurement in islets was measured. RESULTS: L-citrulline was quantified using one step HPLC column. Aging induced hyperglycemia (P<0.05) and excess plasma NOX (17.74 ± 1.664 and 26.25 ± 2.166 µmol/l in A and B groups respectively, P<0.05) with unaltered plasma insulin. Islet insulin secretion was significantly reduced in aging rats. L-NAME induced islet insulin secretion especially in aging rats (P=0.003). Inducible NOS activity in islets of aging rats was significantly higher than adult rats (1.082 ± 0.084 and 6.277 ± 0.475 pmol/min per mg protein in adult and aging rats, respectively, P<0.001). CONCLUSION: These findings show that decreased in islet insulin secretion may be related to increase in iNOS activity in islets, which follows impaired carbohydrate metabolism in aging.

4.
J Immunotoxicol ; 12(2): 132-9, 2015.
Article in English | MEDLINE | ID: mdl-24852194

ABSTRACT

Respiratory disorders in sulfur mustard (SM)-exposed and chronic obstructive pulmonary disease (COPD) patients are mostly associated with neutrophilic inflammation, severe airflow limitation, and oxidative stress. The objective of this study was to establish whether neutrophil (PMN) proteomes in these diseases were similar or differed. Blood neutrophil proteomes from healthy, SM-exposed, and COPD subjects were analyzed using two-dimensional gel electrophoresis followed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI TOF MS). Elastase activity was determined kinetically. The results showed that levels of S100 calcium-binding protein (CBP) A12, S100 CBP A8, glyceraldehyde-3-phosphate dehy-drogenase, superoxide dismutase, and protein disulfide isomerase proteins - as well as elastase activity - were significantly increased in PMN from 'diseased' hosts compared to in cells from healthy controls. In contrast, coactosin-like protein, RhoGDP dissociation inhibitor, and actin isoforms were significantly decreased in diseased subjects' PMN compared to PMN of healthy controls. Moreover, serpin B1 and coronin-1A were expressed only in PMN of the healthy subjects. Lastly, S100 CBP A9, endoplasmic reticulum (ER)-60 protease, and glutathione-S-transferase isoforms were differentially expressed in the cells from the SM-exposed and COPD subjects. These results show that serpin B1, an efficient inhibitor of neutrophil serine proteases, was not detectable, and elastase activity significantly increased in PMN from both SM-exposed and COPD patients. It seems that, apart from inflammation and oxidative stress, a protease:anti-protease imbalance exists within PMN of both COPD and SM-exposed patients.


Subject(s)
Neutrophils/metabolism , Proteome/analysis , Serpins/metabolism , Blood Circulation , Calgranulin A/genetics , Calgranulin A/metabolism , Gene Expression Regulation , Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)/genetics , Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)/metabolism , Humans , Male , Microfilament Proteins/genetics , Microfilament Proteins/metabolism , Middle Aged , Mustard Gas/administration & dosage , Pancreatic Elastase/genetics , Pancreatic Elastase/metabolism , Protein Disulfide-Isomerases/genetics , Protein Disulfide-Isomerases/metabolism , Pulmonary Disease, Chronic Obstructive , Respiration Disorders/chemically induced , S100A12 Protein/genetics , S100A12 Protein/metabolism , Serpins/genetics , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Superoxide Dismutase/genetics , Superoxide Dismutase/metabolism , rho Guanine Nucleotide Dissociation Inhibitor alpha/genetics , rho Guanine Nucleotide Dissociation Inhibitor alpha/metabolism
5.
Immunopharmacol Immunotoxicol ; 35(3): 419-25, 2013 Jun.
Article in English | MEDLINE | ID: mdl-23672526

ABSTRACT

Late respiratory complications in patients suffering from pulmonary lesions due to sulfur mustard (SM) gas are asthma, chronic obstructive pulmonary disease and bronchiectasis. Recently PON1 antioxidant activity draws attention as the enzyme which prevents the oxidation of lipoproteins during oxidative stress. In this study we aimed to investigate PON1 192 polymorphisms and paraoxonase and arylesterase activity in the serum of SM-exposed lung disease patients. Also, we examined the detection of PON1 and apoA1 proteins in BAL fluid. 101 male patients were included who were categorized to three groups of mild, moderate and severe suffering from pulmonary lesions due to SM. Significant reduction in paraoxonase activity [Healthy: 412.46 ± 89.1 U/L, Severe: 89.66 ± 20.7 U/L] (p < 0.0001) and arylesterase activity [Healthy: 25826.4 ± 4425.23 U/L, Severe: 16760.43 ± 3814.9 U/L] (p < 0.0001) with increase in severity of disease was demonstrated statistically. With respect to the distribution of the PON1 polymorphism, the RR genotype was more frequent in severe patients [37.2%] than healthy group [10%] (p < 0.05) and no significant regression was found between genotype and PON1 activity. On the other hand, the results of PON1 and apoA1 detection illustrated that only apoA1 protein was found in BAL fluid. According to our findings it seems that increase in the stress oxidative in chemical injured veterans with pulmonary complications comes with reduction in PON1 enzyme activity and appearance of RR genotype rises up with the increase in disease severity. Since a significant correlation between enzyme activity and genotype was not observed altering these two variables with each other requires more studies.


Subject(s)
Aryldialkylphosphatase/genetics , Chemical Warfare Agents/toxicity , Lung Diseases/genetics , Mustard Gas/toxicity , Polymorphism, Genetic , Severity of Illness Index , Adult , Apolipoprotein A-I/analysis , Aryldialkylphosphatase/blood , Bronchoalveolar Lavage Fluid/chemistry , Case-Control Studies , Cholesterol, HDL/blood , Cholesterol, LDL/blood , Humans , Lipid Peroxidation/genetics , Lung Diseases/chemically induced , Lung Diseases/enzymology , Male , Middle Aged , Oxidative Stress/genetics , Respiratory Function Tests , Triglycerides/blood
6.
Clin Proteomics ; 8(1): 2, 2011 Jan 07.
Article in English | MEDLINE | ID: mdl-21906349

ABSTRACT

INTRODUCTION: Sulfur mustard "bis (2-chlroethyl) sulphide" (SM) is a chemical warfare agent that remains a threat to human health. The aim of this study was to identify protein expression signature or biomarkers that reflect chronic lung damages induced by SM exposure. METHODS: Prior to analysis, plasma was fractionated using ethanol precipitation. Using two dimensional SDS-PAGE; fractionated protein profiles of 20 healthy and 20 exposed patients with lung diseases were established. Selected protein spots were successfully identified with MALDI TOF MS/MS. RESULTS: The results show that α1 haptoglobin isoforms were detected in plasma of the all lung disease patients but none of the healthy controls. Amyloid A1 isoforms was also detected in plasma of the lung disease patients but none of the healthy controls. Moreover, low molecular weight proteins were enriched in ethanol supernatant compared to ethanol precipitate. CONCLUSION: Our present results and previous studies suggest that ongoing tissue remodeling is involved in SM exposed lung damage patients. These finding might improve patient care and suitable therapies.

7.
Ren Fail ; 31(6): 514-21, 2009.
Article in English | MEDLINE | ID: mdl-19839829

ABSTRACT

BACKGROUND: Pre-exposure to hyperoxic gas (>or= 95%) has been shown to protect the heart and central nervous system from ischemia-reperfusion injury. In the present study, we investigated whether oxygen pretreatment induces delayed renal protection in rats. The possible role of some renal antioxidant agents was also investigated. MATERIALS AND METHODS: Adult male Wistar rats were kept in a hyperoxic (HO) (>or= 95% O(2)) environment for 0.5 h, 1 h, 2 h, 3 h, 6 h, and 2 h/day for three consecutive days and 4 h/day for six consecutive days, and control group (IR) animals were kept in the cage with no HO, one day before subjecting their kidney to 40 minutes of ischemia and 24h of reperfusion. Renal function was assessed by comparing plasma creatinine (Cr), blood urea nitrogen (BUN), creatinine clearance (CLCr), and fractional excretion of sodium (FENa%). Histopathological injury score was also determined according to the Jablonski method. To examine the antioxidant system induction by hyperoxia, we measured renal catalase and superoxide dismutase activity, and renal glutathione and malondialdehyde content. RESULTS: Our data demonstrated that only in 4 h/day HO for six consecutive days, the renal function tests (Cr, CLCr, BUN, and FENa%) and Jablonski histological injury were better than control group (p < 0.05). The beneficial effect of oxygen pretreatment in this group was associated with increased renal catalase activity compared with those obtained from control group (p < 0.05). CONCLUSION: The present study demonstrates that repeated exposure to hyperoxic (>or= 95% O(2)) environment can reduce subsequent rat's renal ischemia-reperfusion damage. Induction of endogenous antioxidant system may partially explain this beneficial effect of hyperoxic preconditioning.


Subject(s)
Hyperoxia , Kidney Diseases/prevention & control , Oxidative Stress/physiology , Oxygen/administration & dosage , Reperfusion Injury/prevention & control , Analysis of Variance , Animals , Catalase/metabolism , Creatinine/metabolism , Disease Models, Animal , Immunohistochemistry , Ischemic Preconditioning/methods , Kidney/blood supply , Kidney Diseases/pathology , Kidney Function Tests , Male , Malondialdehyde/metabolism , Probability , Random Allocation , Rats , Rats, Wistar , Reactive Oxygen Species/metabolism , Regional Blood Flow , Reperfusion Injury/pathology , Time Factors
8.
Proteomics Clin Appl ; 3(10): 1191-200, 2009 Oct.
Article in English | MEDLINE | ID: mdl-21136943

ABSTRACT

Sulfur mustard is an alkylating agent that reacts with ocular, respiratory, cutaneous, and bone marrow tissues. Main late respiratory complications are chronic obstructive pulmonary disease, bronchiectasis, asthma, and bronchiolitis obliterans. The aim of the present study was to identify differentially expressed proteins in bronchoalveolar lavage (BAL) fluid of control healthy and sulfur mustard-exposed lung disease patients. The BAL protein profile of ten healthy and 30 exposed patients with mild, moderate, and severe conditions (ten males in each group) were separated with 2-D SDS-PAGE and differentially expressed protein spots were successfully identified with MALDI TOF TOF MS. Among the differentially expressed proteins we observed a significant increase in vitamin D binding protein isoforms, haptoglobin isoforms, and fibrinogen especially in exposed moderate and severe lung diseases patients (p<0.01). Moreover, compared with healthy controls, significant decreases was noted in calcyphosine, surfactant protein A, and transthyretin in these patients (p<0.01). Apolipoprotein A1 was detected in all patients' BAL fluid but none of the healthy controls. Furthermore, S100 calcium-binding protein A8 was only detected in BAL fluid of moderate and severe groups. These findings will be useful to improve current methods of monitoring and helps to identify new therapeutic targets for treatment of this complicated illness.

9.
Toxicol In Vitro ; 22(5): 1257-63, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18513920

ABSTRACT

Effects of diazoxon on the gene and protein expression of nicotinic acetylcholine receptors (nAChR) were evaluated in PC12 cells. Cells were exposed to 100 microM diazoxon for 48 h in the presence versus absence of nAChR agonists or antagonists. Diazoxon significantly inhibited AChE activity in the cells. At the mRNA level, transcripts of the alpha4 and beta2 subunits of nAChR were significantly reduced in cells exposed to diazoxon, but there was no change in alpha7 subunit mRNA content. Diazoxon exposure also significantly reduced the protein levels of both alpha4 and beta2 nAChR subunits. Treatment with nicotine (10 microM) or with the nicotinic receptor antagonists, mecamylamine (10 microM) or dihydro-beta-erythroidine (DHbetaE) (5 microM) efficiently prevented the diazoxon-induced reduction in alpha4 and beta2 nAChR mRNA and protein in PC12 cells, but carbamaylcholine, a weak nAChR agonist, was ineffective. These data suggest that alpha4beta2 nAChRs are involved in diazoxon-related toxicity and that nicotinic receptor antagonists could play a protective role against organophosphate-related damage.


Subject(s)
Gene Expression/drug effects , Organophosphorus Compounds/toxicity , RNA, Messenger/metabolism , Receptors, Nicotinic/drug effects , Animals , Dihydro-beta-Erythroidine/pharmacology , Dose-Response Relationship, Drug , Drug Combinations , Mecamylamine/pharmacology , Nicotine/pharmacology , PC12 Cells/drug effects , PC12 Cells/metabolism , Rats , Receptors, Nicotinic/genetics , Receptors, Nicotinic/metabolism
10.
J Biochem Biophys Methods ; 70(6): 1037-42, 2008 Apr 24.
Article in English | MEDLINE | ID: mdl-17928061

ABSTRACT

Human paraoxonases-1 is one of the most important detoxifying enzymes. In this study using simple chromatographic procedures human paraoxonases-1 was purified from human pooled plasma. The enzyme was purified using DEAE Sephadex an anion exchanger and G-200 a gel filtration chromatographic media. Results showed a single band of approximately 43 KD proteins in SDS-PAGE, corresponding to the human PON1. Using paraoxon as the substrate the activity was related to the concentration of calcium and sodium ions (Km=1.2+/-0.2 mM). Phenyl acetate hydrolyzing activity was independent of sodium and calcium ions (Km=0.78+/-0.08 mM). Keeping at 25 degrees C for 20 days 75% of the enzyme original activity was restored in 20% (v/v) glycerol. EDTA and zinc chloride both inhibited the enzyme activity. In conclusion the applied procedures can be used for large scale purification. It would greatly facilitate their structural and functional characterization and permit examination of their weak, yet potentially most biologically relevant activities, in the complete absence of other serum proteins.


Subject(s)
Aryldialkylphosphatase/isolation & purification , Aryldialkylphosphatase/metabolism , Aryldialkylphosphatase/antagonists & inhibitors , Edetic Acid/pharmacology , Enzyme Inhibitors/pharmacology , Enzyme Stability , Hot Temperature , Humans , Hydrogen-Ion Concentration , Kinetics
11.
Environ Toxicol Pharmacol ; 26(1): 22-9, 2008 Jul.
Article in English | MEDLINE | ID: mdl-21783883

ABSTRACT

Chronic and acute exposure to organophosphate pesticides may lead to persistent neurological and neurobehavioral effects, which cannot be explained by acetylcholinesterase (AChE) inhibition alone. In an attempt to elucidate the mechanism by which paraoxon affects the nicotinic receptors gene expression, the effects of exposure of PC12 cells to 100µM concentrations of paraoxon for 48h in the presence and the absence of nicotinic acetylcholine receptors (nAChRs) agonists and antagonists were characterized. Paraoxon at 100µM significantly inhibited AChE activity. On the mRNA level, the α(4) and ß(2) subunits of nAChR mRNA were significantly decreased in the cells exposed to paraoxon. On the protein level, α(4) and ß(2) subunits of nAChR protein were also significantly reduced. Mecamylamine (10µM), dihydro-ß-erythroidine (DHßE) (5µM) and nicotine (10µM) efficiently prevented the decrease of α(4) and ß(2) nAChR mRNA and protein in PC12 cells, but carbamaylcholine a weak agonist of nAChR was not efficient. These observations suggest that α(4)ß(2) nAChRs are involved in paraoxon related toxicity and nicotinic receptors antagonists could play some protective role against organophosphate related damages.

12.
Environ Toxicol Pharmacol ; 26(2): 247-54, 2008 Sep.
Article in English | MEDLINE | ID: mdl-21791372

ABSTRACT

Chronic and acute exposure to organophosphate pesticides or related nerve agents may lead to persistent neurological and neurobehavioral effects, which cannot be explained by acetylcholinesterase (AChE) inhibition alone. In the present study, the effects of mecamylamine (2mg/kg), or atropine (10mg/kg) alone, or in combination, on the expression of nicotinic acetylcholine receptors (nAChRs) subunits, functional signs of toxicity and lethality in paraoxon-treated rats were investigated. Surviving animals were sacrificed after 48h of paraoxon administration. Paraoxon, at dosage of 1× LD50, significantly reduced expression of α(4) and ß(2) nAChR subunits mRNA and protein in rat brain homogenates. Mecamylamine, efficiently prevented reduction of the α(4) and ß(2) nAChR mRNA and protein in paraoxon exposed rat brains, but atropine was not efficient. Concurrent treatment with mecamylamine and atropine restored nAChRs mRNA and protein level and prevented lethality and severe involuntary movements induced by paraoxon. Nicotinic receptors antagonists may be included in the cocktail of therapeutic agents targeting the various mechanisms for neuronal injury by organophosphates.

13.
J Neurochem ; 101(6): 1527-38, 2007 Jun.
Article in English | MEDLINE | ID: mdl-17286584

ABSTRACT

Accumulation of the amyloid protein (Abeta) in the brain is an important step in the pathogenesis of Alzheimer's disease. However, the mechanism by which Abeta exerts its neurotoxic effect is largely unknown. It has been suggested that the peptide can bind to the alpha7 nicotinic acetylcholine receptor (alpha7nAChR). In this study, we examined the binding of Abeta1-42 to endogenous and recombinantly expressed alpha7nAChRs. Abeta1-42 did neither inhibit the specific binding of alpha7nAChR ligands to rat brain homogenate or slice preparations, nor did it influence the activity of alpha7nAChRs expressed in Xenopus oocytes. Similarly, Abeta1-42 did not compete for alpha-bungarotoxin-binding sites on SH-SY5Y cells stably expressing alpha7nAChRs. The effect of the Abeta1-42 on tau phosphorylation was also examined. Although Abeta1-42 altered tau phosphorylation in alpha7nAChR-transfected SH-SY5Y cells, the effect of the peptide was unrelated to alpha7nAChR expression or activity. Binding studies using surface plasmon resonance indicated that the majority of the Abeta bound to membrane lipid, rather than to a protein component. Fluorescence anisotropy experiments indicated that Abeta may disrupt membrane lipid structure or fluidity. We conclude that the effects of Abeta are unlikely to be mediated by direct binding to the alpha7nAChR. Instead, we speculate that Abeta may exert its effects by altering the packing of lipids within the plasma membrane, which could, in turn, influence the function of a variety of receptors and channels on the cell surface.


Subject(s)
Amyloid beta-Peptides/metabolism , Membrane Lipids/metabolism , Receptors, Nicotinic/metabolism , Aconitine/analogs & derivatives , Aconitine/metabolism , Animals , Bungarotoxins/metabolism , Cell Line, Tumor , Cell Membrane/metabolism , Female , Fluorescence Polarization , Hippocampus/metabolism , Humans , Membrane Fluidity/drug effects , Neuroblastoma/metabolism , Oocytes/metabolism , Rats , Rats, Sprague-Dawley , Surface Plasmon Resonance , Transfection , Xenopus laevis , alpha7 Nicotinic Acetylcholine Receptor , tau Proteins/metabolism
14.
Clin Biochem ; 37(3): 241-4, 2004 Mar.
Article in English | MEDLINE | ID: mdl-14972648

ABSTRACT

OBJECTIVES: The aim of this study was to screen newborns in Tehran for glucose-6-phosphate dehydrogenase (G6PD) deficiency in relation to hyperbilirubinemia and jaundice. DESIGN AND METHODS: We performed quantitative and qualitative red blood cell (RBC) G6PD assays in cord blood of 2000 male and female at-term neonates. Observations for jaundice and bilirubin determination were made in G6PD-deficient and normal groups. Those with severe jaundice were treated with phototherapy or exchange transfusion. RESULTS: Our results showed that 2.1% (3.6% of males and 0.6% of females) was G6PD-deficient. Those with severe jaundice and hyperbilirubinemia (160 normal and 17 G6PD-deficient) were hospitalized and treated with phototherapy or exchange transfusion. Bilirubin levels in G6PD-deficient neonates were somewhat higher compared to G6PD-normal babies (18.8 +/- 2.4 mg/dl [321.5 +/- 41 micromol/l] vs. 15.7 +/- 3.2 mg/dl [268.5 +/- 54.7 micromol/l]; P < 0.05). G6PD activity was significantly lower in G6PD-deficient group than in the normal group (2.1 +/- 0.7 vs. 12.5 +/- 5.0 U/g Hb; P < 0.001). CONCLUSION: This study shows that the incidence of G6PD deficiency in newborns of Tehran is 2.1%, which is relatively high, and also hyperbilirubinemia and jaundice are approximately 3-fold higher in G6PD-deficient group than in the G6PD-normal group (51% vs. 16%). This emphasizes the necessity of neonatal screening on cord blood samples of both sexes for G6PD deficiency and the need to watch closely for development of hyperbilirubinemia.


Subject(s)
Glucosephosphate Dehydrogenase Deficiency/epidemiology , Glucosephosphate Dehydrogenase/blood , Jaundice, Neonatal/epidemiology , Chi-Square Distribution , Exchange Transfusion, Whole Blood/methods , Female , Glucosephosphate Dehydrogenase Deficiency/blood , Humans , Infant, Newborn , Iran/epidemiology , Jaundice, Neonatal/blood , Jaundice, Neonatal/therapy , Male , Prevalence
15.
Environ Toxicol Pharmacol ; 16(3): 179-85, 2004 Apr.
Article in English | MEDLINE | ID: mdl-21782705

ABSTRACT

Organophosphates (OP) are used in large quantities around the world as agricultural insecticides. Exposure to these toxic chemicals is a serious global health problem. Human plasma butyrylcholinesterase is known to be a good scavenger of organophosphorus pesticides and chemical warfare agents. In this study, purified human plasma butyrylcholinesterase (HuBChE) from pooled outdated human plasma, was immobilized onto the polyurethane foam. The immobilized enzyme showed greater stability at and above room temperature (up to 55°C), compared to the enzyme in solution. Scavenger properties of immobilized enzyme were tested in vitro with parathion and its active metabolite paraoxon. In, in vitro experiments polyurethane foam with immobilized active enzyme removed 40% of parathion and 50% of paraoxon inhibitory effect (based on cholinesterase inhibition). In, in vivo experiments groups of rats inhaled parathion through filters with immobilized active enzyme (Group I), immobilized inactivated enzyme (Group II), and control group (Group III) inhaled solvent only without any parathion or filter. In the Group II animals, activity of plasma and red blood cells cholinesterase was significantly decreased (30 and 28%, respectively) compared to Groups I and III animals. In other tissues such as brain, skeletal muscle and lung, activity of the acetylcholinesterase (AChE) in the Group II animals, was decreased significantly (29, 28, and 22%, respectively). There was no significant differences between Groups I and III animals enzyme activities. In conclusion, immobilized butyrylcholinesterase (BChE) may be useful in scavenging and detoxifying organophosphate compounds both for medical protection and decontamination procedures.

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