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PubMed2002

A neuropsychotoxicological assessment of workers in a sodium azide production plant.

OBJECTIVE: Despite its known toxicity and extensive current industrial use, the occupational neuropsychotoxicology of sodium azide has not yet been investigated. METHOD: Neuropsychological and psychological tests, a symptom self-report questionnaire and haematological and cardiac measurements were gathered from 41 exposed workers and 42 unexposed workers in a chemical production plant yearly for 3 years. RESULTS: The exposed workers presented significantly more acute symptoms of exposure (headache, vertigo, nausea, fatigue, cardiac palpitations, irritated or red eyes) than did the unexposed workers. However, only one chronic symptom was repeatedly and more significantly reported, namely trembling of the hands. No psychological or neuropsychological tests (reaction time, psychomotor, cognitive, chromatopsia, Profile of Mood States) differentiated the two groups. However, acute effects of exposure on plasma creatinine and on systolic pressure were noted. Low creatinine levels in the plasma of exposed workers correlated significantly with impairment of mood on the Profile of Mood States test, but not with any other measure. We recommend that workers exposed to sodium azide be assessed with tremometry, clinically and in a future field study.

Adult↗
PubMed1982

[A new test for hemolysis related to tocopherol deficiency: hemolysis caused by sodium azide (NaN3). Results in cholestasis in children].

In patients suffering from intra or extrahepatic biliary obstruction defective absorption of liposoluble vitamins results in tocopherol deficiency. Erythrocyte membranes thus have an increased susceptibility to various oxydants. Erythrocytes from 28 infants and children with biliary atresia have been studied. The usual peroxide hemolysis test (H2O2) was compared with a new method using sodium azide (NaN3), an inhibitor of intraerythrocytic catalase, as the hemolyzing agent. A much more significant correlation was found between plasma tocopherol levels and NaN3--induced hemolysis (R. coefficient = -0.872; P = 99.9%) than tocopherol levels and peroxyde hemolysis (RC = -0.477; P = 95-99%). In severely tocopherol-deficient patients (plasma levels below 0.15 mg/dl compared to normal of 0.5 mg/dl) sodium azide hemolysis is completed by the 5th hour of incubation at 37 degrees C. After the 5th hour, hemolysis begin to appear in the control media and when measured at 20 hrs is almost complete especially in the isotonic saline solution (NaCl 0.9 g/l). When abnormal red cells are incubated in their own tocopherol-supplemented plasma a complete normalization of hemolysis due to NaN3, H2O and control media is obtained. The sodium azide hemolysis test is proposed as a new and simple means of measuring tocopherol deficiency in erythrocyte membranes.

Azides↗
PubMed1962

Sodium azide selective medium for the primary isolation of anaerobic bacteria.

Forget, A. (University of Montreal, Montreal, Canada) and V. Fredette. Sodium azide selective medium for the primary isolation of anaerobic bacteria. J. Bacteriol. 83:1217-1223. 1962.-A selective medium has been devised for the primary isolation of anaerobic bacteria from a mixture of both aerobes and anaerobes. The solid medium contains 0.05% NaN(3), and the liquid medium has 0.2% NaN(3) in an identical base, namely, Trypticase soy broth. Addition of either 5% blood or 10% normal serum does not alter the selective action of sodium azide. The only defect which the medium exhibits is that it is unable to limit the growth of the facultative streptococci.

Azides↗
PubMed1996

Synergy between chronic corticosterone and sodium azide treatments in producing a spatial learning deficit and inhibiting cytochrome oxidase activity.

Previously, we developed a rat model of persistent mitochondrial dysfunction based upon the chronic partial inhibition of the mitochondrial enzyme cytochrome oxidase (EC 1.9.3.1). Continuous systemic infusion of sodium azide at approximately 1 mg/kg per hr inhibited cytochrome oxidase activity and produced a spatial learning deficit. In other laboratories, glucocorticoids have been reported to exacerbate neuronal damage from various acute metabolic insults. Therefore, we tested the hypothesis that corticosterone, the primary glucocorticoid in the rat, would potentiate the sodium azide-induced learning deficit. To this end, we first identified nonimpairing doses of sodium azide (approximately 0.75 mg/kg per hr) and corticosterone (100-mg pellet, 3-week sustained-release). We now report that chronic co-administration of these individually nonimpairing treatments produced a severe learning deficit. Moreover, the low dose of corticosterone, which did not elevate serum corticosterone, acted synergistically with sodium azide to inhibit cytochrome oxidase activity. The latter result represents a previously unidentified effect of glucocorticoids that provides a candidate mechanism for glucocorticoid potentiation of neurotoxicity induced by metabolic insult. These results may have the clinical implication of expanding the definition of hypercortisolism in patient populations with compromised oxidative metabolism. Furthermore, they suggest that glucocorticoid treatment may contribute to pathology in disease or trauma conditions that involve metabolic insult.

Analysis of Variance↗
PubMed2004

C-reactive protein-induced in vitro vasorelaxation is an artefact caused by the presence of sodium azide in commercial preparations.

OBJECTIVE: Although C-reactive protein (CRP) is increasingly recognized as an independent risk factor for acute myocardial events, recent evidence suggests that it can directly induce vasorelaxation. This study aimed to investigate the mechanism of this CRP-induced response. METHODS AND RESULTS: Isometric tension recordings were used to measure endothelium-dependent and endothelium-independent vascular smooth muscle relaxation in isolated rabbit aortic rings. CRP generated in-house by genetic engineering and expressed in Chinese hamster ovary cells, CRP purified from ascites, and CRP obtained from commercial sources were assessed for vasorelaxing properties. Only the commercial CRP preparation induced vasorelaxation; more than half maximal relaxation was observed at 0.025 microg/mL and maximum relaxation attained at 0.25 microg/mL. Commercial CRP contains high levels of sodium azide, a well-known vasorelaxant. Removal of this agent by dialysis abolished the vasodilatory effect of commercial CRP. Sodium azide alone at concentrations equivalent to that present in the commercial CRP produced a near-identical relaxation pattern to the undialyzed commercial product. CONCLUSIONS: CRP has no vasorelaxant properties per se, and the reported vasorelaxant ability of CRP is an artifact caused by sodium azide present in commercial preparations of this agent.

Animals↗
PubMed1999

Effects of in vivo sodium azide administration on the immunohistochemical localization of kynurenine aminotransferase in the rat brain.

Endogenous excitotoxins that act on receptors of cerebral excitatory amino acids play important roles in the pathogenesis of excitotoxic brain diseases. Activation of excitatory amino acid receptors results in neuronal death characteristic of these disorders. Kynurenic acid, a powerful endogenous excitatory amino acid receptor antagonist, which is therefore widely regarded as a potent neuroprotective agent, is produced from its biological precursor, L-kynurenine, by the action of the enzyme kynurenine aminotransferase-I. The chemical hypoxia induced by mitochondrial toxins produces a secondary excitotoxicity, leading to the activation of N-methyl-D-aspartate receptors. Accordingly, sodium azide, an inhibitor of cytochrome oxidase, induces the release of excitotoxins via an energy impairment and this, in turn, results in neurodegeneration. Since energy-dependent secondary excitotoxic mechanisms also account for the pathogenesis of neurodegenerative diseases, a study was made of the effects of sodium azide on the immunohistochemical localization of kynurenine aminotransferase-I. After in vivo administration of sodium azide for five days, a markedly decreased glial kynurenine aminotransferase-I immunoreactivity was found by immunohistochemical techniques in the glial cells of the striatum, hippocampus, dentate gyrus and temporal cortex; at the same time, kynurenine aminotransferase-I started to be expressed by nerve cells which had not been immunoreactive previously. The accumulation of kynurenine aminotransferase-I reaction product around the ribosomes of neuronal endoplasmic reticulum suggests de novo synthesis of kynurenine aminotransferase-I in the reactive nerve cells.

Animals↗
PubMed2006

Interactions of sodium azide with triazine herbicides: effect on sorption to soils.

Sodium azide (NaN(3)) is one of the biocides commonly used to inhibit microbial growth during sorption experiments. However, a few reports have suggested that NaN(3) can react with the analyte of interest. In this study, the interactions of NaN(3) with triazine herbicides were investigated and the effect of atrazine transformation on its sorption to soil was evaluated. The concentration of atrazine in the presence of NaN(3) decreased significantly over period of time. After 14 days, only 38% of the initial atrazine concentration (10 mg l(-1)) was detected in a solution containing 1,000 mg l(-1) NaN(3) at pH 5.5. The magnitude and the rate of atrazine transformation increased with increase in NaN(3) load and with decrease in pH. In contrast to atrazine behavior, the concentrations of prometon and ametryn did not change during the experiment. GC/MS analysis indicated that the chlorine atom of atrazine is replaced by the azide group yielding 2-azido-4-(ethylamino)-6-(isopropylamino)-s-triazine. Atrazine transformation by NaN(3) significantly affected sorption of herbicide to soil. The presence of NaN(3) affects indirectly the sorption of atrazine due to competitive effect of its derivative. Our results demonstrated that the application of NaN(3) as a biocide in sorption-desorption experiments must be carefully evaluated. This issue is vital for sorption experiments conducted over long periods of time or/and with concentration of NaN(3) higher than 100 mg l(-1).

Adsorption↗
PubMed1983

Effects of sodium azide on phototaxis of the blue-green alga Anabaena variabilis and consequences to the two-photoreceptor systems-hypothesis.

Experiments with sodium azide support the earlier report that two different photoreceptor systems participate in the absorption of the phototactically active light in Anabaena variabilis. The one of them, represented by the phycobiliproteins and chlorophyll a, is responsible for positive and negative phototaxis around 440 nm and between 580 and 700 nm. This system is sensitive to sodium azide which is able to reverse the negative reaction at high fluence rates to a positive one. The second one which absorbs light between 500 and 560 nm and above 700 nm is insensitive to azide. It triggers only negative responses in absence and presence of azide as well. P750 is obviously not a photoreceptor pigment of this system, since there is no indication for its occurrence in Anabaena. Even photobleaching of the photosynthetic pigments at high fluence rates is prevented by azide. The noncyclic photosynthetic electron transport is not severely inhibited by azide because photokinesis is only in part impaired. Therefore, the hypothesis is suggested that the phototactic reaction-sign reversal generator of Anabaena is controlled by the level of an active oxygen species, probably singlet oxygen, which is quenched by azide.

Azides↗
PubMed2000

Effects of sodium azide on the secretion of soluble amyloid-beta precursor protein and the accumulation of beta-amyloid(1-40) in cultured chick neurons.

Sodium azide has been reported in the literature to reduce the release of secreted amyloid beta-precursor protein (AbetaPPs) and to produce a large increase in the cellular level of an 11.5 kDa C-terminal AbetaPP derivative containing the beta-amyloid (Abeta) sequence. Here we report that 1 mM of sodium azide, reduced the constitutive AbetaPPs secretion from cultured embryonic chick neurons after 12 h of incubation. After 24 h of incubation there was a modest increase in lactate dehydrogenase (LDH) release and no change in MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) reduction, suggesting that the reduced AbetaPPs secretion was not due to the cell toxic effects of NaN(3). However, NaN(3) reduced the accumulation of Abeta(1-40) in the cell lysates and decreased the acetylcholine esterase activity both in cell culture media and in cell lysates. It is concluded that the effect of NaN(3) upon AbetaPP metabolism in the chick cultured neurons may be a rather non-specific effect.

Amyloid beta-Peptides↗
PubMedDate not supplied

[Study of kinetic parameters of singlet molecular oxygen in aqueous porphyrin solutions. Effect of detergents and the quencher sodium azide].

The kinetic parameters of porphyrin-photosensitized formation and deactivation of singlet molecular oxygen (1O2) and their dependence on the concentration of the 1O2 quencher sodium azide were investigated in air-saturated water, ethanol, and aqueous micellar solutions of detergents using time-resolved measurements of oxygen phosphorescence under pulsed laser excitation. The lifetimes of 1O2 formation and deactivation and the rate constants of 1O2 quenching by sodium azide were determined. It was shown that, with no azide in the solutions, the rise in phosphorescence intensity after the laser flash corresponded to the kinetics of energy transfer from the porphyrin triplet molecules to oxygen, while the decay kinetics corresponded to the kinetics of 1O2 deactivation. In the presence of detergent, a considerable increase in the 1O2 lifetime was observed, which is likely due to the localization of 1O2 molecules mostly in lipophilic micelles and not in the water phase. If relatively high azide concentrations were used, the lifetime of the porphyrin triplet state did not change but the 1O2 lifetime decreased to values similar to those in living cells. In this case, the inversion of the phosphorescence kinetic phases was observed. The rise corresponded to 1O2 deactivation, and the decay, to the energy transfer from triplet porphyrin to oxygen. The data suggest that, in living cells, 1O2 molecules are also located mainly in lipophilic structures and the 1O2 lifetime determines the kinetics of the phosphorescence rise after the laser pulse.

Detergents↗
PubMed1992

Cytogenetic effects of sodium azide encapsulated in liposomes on heteroploid cell cultures.

Lipid vesicles (liposomes) have been shown to be a useful vehicle for the delivery of a variety of compounds to cultured cells. Using multilamellar vesicles (MLV) and small unilamellar vesicles (SUV) we were able to deliver the classical mutagen, sodium azide, into human heteroploid HEp-2 cells. With this method sodium azide is not diluted in culture medium, but it is 'focused' into cells, producing chromosomal aberrations and other major genetic damages. Our results indicate that liposomes are suitable vectors for introducing clastogenic substances into cultured human cells.

Azides↗
PubMed1998

Determining sodium azide concentration in blood by ion chromatography.

We describe a simple method for measuring sodium azide concentrations in aliquots of blood and other tissues. Aliquots are acidified, converting azide to volatile hydrazoic acid (HN3) which is then trapped in sodium hydroxide. We analyze the resulting aliquots by ion chromatography, using a sodium tetraborate eluent and suppressed conductivity detection. The method is sensitive to at least 100 ng/mL.

Azides↗
PubMed1985

Sodium azide preservation of faecal specimens for Kato analysis.

The modified Kato technique has the advantages of reproducibility, simplicity and economy: the disadvantage is that it cannot be used in conjunction with traditional faecal preservatives. Sodium azide has been evaluated as a preservative for human faeces for subsequent Kato analysis. More than 400 faecal samples (from normal and malnourished children, and from mixed-age participants in a field survey of the Turks and Caicos Islands) were each mixed with 2-5 mg of sodium azide powder and stored in 2 or 4 ml autoanalyser cups at ambient tropical temperature. At intervals up to 30 weeks, aliquots were prepared for Kato analysis. Trichuris trichiura, Ascaris lumbricoides and Necator americanus eggs were well preserved without degenerative or developmental changes in morphology. Quantitative analyses of 18 samples indicated that the mean egg count/sample did not change significantly after storage for 1, 2, 4, 8, 12 and 16 weeks in preservative. The use of azide preservative extends the applications of the Kato technique to field and clinical studies in which delays may occur between specimen collection and examination. The direct costs of azide preservation are substantially lower than for traditional methods and the preserved specimens are more compact and resistant to leakage.

Ascaris↗
PubMed1987

Growth inhibitory effect of sodium azide in chemosensitivity assays.

In vitro chemosensitivity assays based on colony counting are plagued by persistent incidence of false-negative results. To avoid serious predictive errors, some investigators have utilized positive controls (known toxic compounds) as a quality control measure. Sodium azide (NaN3) at 6 mg/ml failed to inhibit colony formation in 17/35 (49%) assays; while in the thymidine incorporation assay, sodium azide was effective in inhibiting 124/131 (95%) specimens. Positive control substances for use in chemosensitivity assays must be carefully selected to insure accurate results.

Azides↗
PubMed1981

Effect of sodium azide on sister-chromatid exchanges in human lymphocytes and Chinese hamster cells.

Previous reports from this laboratory and others indicate that sodium azide is a unique mutagen. It is highly mutagenic in S. typhimurium TA1530 as well as in barley, rice, peas, yeast and Chinese hamster V79 cells. However, azide apparently does not produce chromosome breaks in barley, Vicia or human lymphocytes. Therefore, a study of the effects of azide on sister-chromatid exchanges (SCE) appeared warranted. Human whole blood and Chinese hamster K1 cell line were exposed for 4 and 2 h resp. to various concentrations of sodium azide ranging from 10(-3) to 10(-7) M. Cells were harvested and chromosomes stained by the FPG technique. In human lymphocytes, concentrations above 10(-4) induced lethality whereas the K1 cell line was sensitive to concentrations above 10(-5) M. The lower concentrations of azide produced no significant increase in SCE frequency above controls. Concurrent mitomycin C treatments produced significant increases in SCE levels. This apparent lack of induction of SCEs above background combined with previous data demonstrating negative clastogenic but very positive mutagenic activity of azide confirms the uniqueness of this mutagen. It would appear that azide is one of the few known potent mutagens that does not increase SCEs and/or break chromosomes.

Animals↗
PubMed2005

Cyclic GMP, sodium nitroprusside and sodium azide reduce aqueous humour formation in the isolated arterially perfused pig eye.

The effect of nitric oxide (NO) on aqueous humour formation (AHF) and intraocular pressure (IOP) was studied using NO donors, sodium azide (AZ) and sodium nitroprusside (SNP). Using the porcine arterially perfused eye preparation, drug effects on AHF and IOP were measured by fluorescein dilution and manometry, respectively. Perfusion pressure of the ocular vasculature was also monitored using digital pressure transducer and pen recorder. L-Arginine (1.0 mM), a precursor of NO, but not D-arginine (1.0 mM), the inactive analogue, produced a significant reduction in AHF (28.5%) and IOP (21.1%). L-NAME (L-nitro-L-arginine) (10-100 microM), an NO synthase inhibitor, had no effect on AHF and IOP. However, L-NAME (100 microM) completely reversed L-arginine's effect. AZ and SNP reduced the AHF and IOP dose-dependently. AZ at 100 nM, 1 and 10 microM reduced AHF by 26.0, 39.7 and 51.7% and IOP by 10.8, 17.3 and 24.0%, respectively. SNP at 1, 10 and 100 microM reduced the AHF by 6.0, 24.2 and 35.4% and IOP by 3.5, 9.5 and 15.5%, respectively. 8-pCPT-cGMP (8-para-chlorophenyl-thioguanosine-3',5'-cyclic guanosine monophosphate, 10 microM), a cGMP analogue, also reduced the AHF (34.9%) and IOP (15.9%). The effects of AZ and SNP on the AHF and IOP were blocked by a soluble guanylate cyclase inhibitor ODQ (10 microM), whereas ODQ alone or combined with 8-pCPT-cGMP had no effect on the AHF and IOP. None of the drugs had any significant effect on ocular vasculature. The reduction of the AHF and IOP in the arterially perfused pig eye by nitrovasodilators is likely to involve the NO-cGMP pathway.

Animals↗
PubMed1983

Lack of correlation between cyclic GMP elevation and relaxation of nonvascular smooth muscle by nitroglycerin, nitroprusside, hydroxylamine and sodium azide.

Recent reports have suggested that the smooth muscle relaxant effects of drugs such as nitroprusside and nitroglycerin are mediated by increases in tissue levels of cyclic GMP. This hypothesis was examined by comparing the effects of nitroprusside, nitroglycerin, hydroxylamine and sodium azide on tension and cyclic GMP levels in rat vas deferens, rat myometrium and guinea-pig taenia coli. All four of the agents were capable of increasing cyclic GMP levels in these tissues but there did not appear to be a good correlation between cyclic GMP elevation and muscle relaxation in any of the tissues studied. For example, nitroprusside markedly elevated cyclic GMP levels in rat vas deferens and myometrium but had no relaxant effect on either tissue. Nitroglycerin was less effective than nitroprusside in elevating cyclic GMP levels, but was an effective relaxant in both tissues. Significant increases in myometrial cyclic GMP were seen with 0.1, 1 and 5 mM concentrations of hydroxylamine but only the highest concentration had a definite relaxant effect on the muscles. A similar concentration of nitroprusside produced a greater elevation of cyclic GMP than did hydroxylamine, but had no relaxant effect in this preparation. In guinea-pig taenia coli, significant increases in cyclic GMP levels were obtained with concentrations of sodium azide and hydroxylamine which had no effect on the contractile activity of the preparations. These results, together with previous results from this laboratory, suggest that the relaxant effects of this group of drugs in rat vas deferens, rat myometrium and guinea-pig taenia coli are not mediated by increases in tissue levels of cyclic GMP. Further experiments are necessary to determine whether a causal relationship exists between cyclic GMP elevation and relaxation in other types of smooth muscle.

Animals↗
PubMed1984

In vivo and in vitro effects of sodium azide on mouse complement.

A microtiter hemolytic assay was utilized to determine sodium azide (NaN3) modulation of B6C3F1 and C3H mouse serum complement levels in vivo and in vitro. Functional complement was expressed in CH50 units per milliliter. Experiments were performed to determine the in vitro effect of NaN3 on complement mediated lysis of IgM sensitized rabbit erythrocytes. Concentrations of 5, 10, 20, 30, 40, 60, and 80 mM NaN3 were added to microtiter wells containing Tris buffer, IgM sensitized rabbit erythrocytes, and serum complement from naive female C3H mice. Although NaCl and KCl controls had an inhibitory effect, NaN3 demonstrated a significant dose-dependent inhibition of complement-mediated lysis. In the three in vivo experiments, female B6C3F1 mice were exposed to NaN3 and physiological saline (vehicle control). Complement hemolytic ability was evaluated after a 1-day, single iv injection of 0.2, 2.0, and 20.0 mg/kg NaN3; at Days 1, 2, 3, 4, and 6 of a 6-day time course study after ip administration of 20 mg/kg NaN3; and at the end of an 11-day study involving daily injections of 10, 15, and 20 mg/kg NaN3 given ip. No significant changes in complement-mediated hemolysis were observed in the in vivo experiments. These studies indicate that NaN3 does not affect mouse complement levels in vivo. However, NaN3 suppresses in vitro complement hemolytic ability.

Animals↗