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PubMed2006

The effect of sulfite and chronic restraint stress on brain lipid peroxidation and anti-oxidant enzyme activities.

Sulfites are used as anti-microbial and anti-oxidant agents in a variety of drugs, and function as a preservative in many food preparations. In addition to these effects, sulfites oxidize to sulfite radicals initiating lipid peroxidation. The objective of our study was to investigate the effect of restraint stress and sulfite on brain lipid peroxidation and anti-oxidant enzyme activities. Forty male Wistar rats, aged three months, were randomized to one of the following groups: control, restraint stress, sulfite-treated and restraint stress + sulfite-treated. Chronic restraint stress was applied for 21 days (1 h/day) and sodium metabisulfite (520 mg/kg per day) was given by gavage for the same period. Lipid peroxidation was measured using the thiobarbituric acid (TBA) fluorometric assay. TBA-reactive substances (TBARS) were found increased in all treatment groups when compared to the control group. Spectrophotometric measurement of copper/zinc superoxide dismutase (Cu/Zn SOD) and catalase (CAT) revealed decreased enzyme activities in rats exposed to restraint stress compared to control and sulfite-treated rats. GSH-Px activities were significantly decreased in the restraint stress and sulfite-treated rats compared with the control rats. GSH-Px activity measured in restraint stress + sulfite-treated rats was significantly lower than in the other groups. The presented data confirms the pro-oxidant activity of restraint stress and establishes that decreased anti-oxidant enzyme activities in restraint stress-treated rats enhances brain lipid peroxidation caused via the ingestion of sulfites.

Animals↗
PubMed1985

Adverse reactions to sulfites.

Sulfites are widely used as preservatives in the food and pharmaceutical industries. In the United States more than 250 cases of sulfite-related adverse reactions, including anaphylactic shock, asthmatic attacks, urticaria and angioedema, nausea, abdominal pain and diarrhea, seizures and death, have been reported, including 6 deaths allegedly associated with restaurant food containing sulfites. In Canada 10 sulfite-related adverse reactions have been documented, and 1 death suspected to be sulfite-related has occurred. The exact mechanism of sulfite-induced reactions is unknown. Practising physicians should be aware of the clinical manifestations of sulfite-related adverse reactions as well as which foods and pharmaceuticals contain sulfites. Cases should be reported to health officials and proper advice given to the victims to prevent further exposure to sulfites. The food industry, including beer and wine manufacturers, and the pharmaceutical industry should consider using alternative preservatives. In the interim, they should list any sulfites in their products.

Anaphylaxis↗
PubMed1991

Oxidation of molybdopterin in sulfite oxidase by ferricyanide. Effect on electron transfer activities.

The attenuation of the sulfite:cytochrome c activity of sulfite oxidase upon treatment with ferricyanide was demonstrated to be the result of oxidation of the pterin ring of the molybdenum cofactor in the enzyme. Oxidation of molybdopterin (MPT) was detected in several ways. Ferricyanide treatment not only abolished the ability of sulfite oxidase to serve as a source of MPT to reconstitute the aponitrate reductase in extracts of the Neurospora crassa mutant nit-1 but also eliminated the ability of sulfite oxidase to reduce dichlorobenzenoneindophenol after anaerobic denaturation. Additionally, the absorption spectrum of anaerobically denatured ferricyanide-treated molybdenum fragment of rat liver sulfite oxidase was typical of fully oxidized pterins. Ferricyanide treatment had no effect on the protein of sulfite oxidase or on the sulfhydryl-containing side chain of MPT. Quantitation of the ferricyanide reaction showed that 2 mol of ferricyanide were reduced per mol of MPT oxidized, yielding a fully oxidized pterin. These results corroborate the previously reported conclusion that the native state of reduction of MPT in sulfite oxidase is at the dihydro level (Gardlik, S., and Rajagopalan, K.V. (1990) J. Biol. Chem. 265, 13047-13054). As a result of oxidation of the pterin ring, the affinity of MPT for molybdenum is decreased, leading to eventual loss of molybdenum. Because the loss of molybdenum is slow, a population of sulfite oxidase molecules can exist in which molybdenum is complexed to oxidized MPT. These molecules retain sulfite:O2 activity, a function apparently dependent solely on the molybdenum-thiolate complex, yet have greatly decreased sulfite:cytochrome c activity, a function requiring heme as well as the molybdenum center of holoenzyme. These observations suggest that the pterin ring of MPT participates in enzyme function, possibly in electron transfer, directly in catalysis, or by controlling the oxidation/reduction potential of molybdenum.

Animals↗
PubMed1985

Effect of sulfite or nitrite on the ATP content and the carbohydrate metabolism in yeast.

Low concentrations of sulfite or nitrite (about 0.5 mmol) when applied at pH 3.6, caused a rapid and drastic decrease of the concentration of ATP in yeast cells. Under these conditions, alcoholic fermentation was inhibited by sulfite and to a lesser extent by nitrite. Ethanol consumption under aerobic conditions was shown to be more sensitive to nitrite than to sulfite. This indicates a higher sensitivity of respiratory processes to nitrite than to sulfite. Among 15 enzyme activities assayed in extracts from yeast cells after incubation with sulfite or nitrite, glyceraldehyde-3-phosphate dehydrogenase was shown to be the most sensitive. Analysis of the steady-state concentrations of intermediates of alcoholic fermentation in intact yeast cells also implies inhibition by sulfite or nitrite of the glyceraldehyde-3-phosphate dehydrogenase step of fermentation. In contrast to nitrite, sulfite had an additional effect by accumulating the intracellular steady state concentration of glyceraldehyde-3-phosphate 10 to 100-fold over the concentration in the absence of sulfite. In vitro studies on the equilibrium catalyzed by triosephosphate isomerase or aldolase confirmed the postulated shift of equilibrium concentrations by a formation of complex of glyceraldehyde-3-phosphate with sulfite.

Adenosine Triphosphate↗
PubMed1995

Sulfite sensitivity: significance in human health.

Endogenous sulfite is generated as a consequence of the body's normal processing of sulfur-containing amino acids. Sulfites occur as a consequence of fermentation and also occur naturally in a number of foods and beverages. As food additives, sulfiting agents were first used in 1664 and approved in the United States as long ago as the 1800s. With such long experience with their use, it is easy to understand why these substances have been regarded as safe. They are currently used for a variety of preservative properties, including controlling microbial growth, preventing browning and spoilage, and bleaching some foods. It is estimated that up to 500,000 (< .05% of the population) sulfite-sensitive individuals live in the United States. Sulfite sensitivity occurs most often in asthmatic adults--predominantly women; it is uncommonly reported in preschool children. Adverse reactions to sulfites in nonasthmatics are extremely rare. Asthmatics who are steroid-dependent or who have a higher degree of airway hyperreactivity may be at greater risk of experiencing a reaction to sulfite-containing foods. Even within this limited population, sulfite sensitivity reactions vary widely, ranging from no reaction to severe. The majority of reactions are mild. These manifestations may include dermatologic, respiratory, or gastrointestinal signs and symptoms. Severe nonspecific signs and symptoms occur less commonly. Broncho-constriction is the most common sensitivity response in asthmatics. The precise mechanisms of the sensitivity responses have not been completely elucidated. Inhalation of sulfur dioxide (SO2) generated in the stomach following ingestion of sulfite-containing foods or beverages, a deficiency in a mitochondrial enzyme, and an IgE-mediated immune response have all been implicated.(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Inhalation↗
PubMed1971

Characterization of a thermolabile sulfite reductase from Salmonella pullorum.

The biochemical basis for sulfite accumulation by sulfate-using revertants of Salmonella pullorum was determined. All of the sulfate-using mutants isolated from wild-type S. pullorum accumulated sulfite when grown at 37 but not at 25 C. The specific activity of reduced nicotinamide adenine dinucleotide (NADPH)-dependent sulfite reductase (H (2)S-NADP oxidoreductase, EC 1.8.1.2) and of reduced methyl viologen (MVH)-dependent sulfite reductase (H (2)S-MV oxidoreductase), in extracts prepared from cells incubated at 37 C, declined as the incubation period lengthened. However, the specific activity of both reductases from cells incubated at 25 C did not decline. Thermolability of cell-free NADPH-dependent sulfite reductase from cells of S. pullorum incubated at 37 C was greater than the lability of this enzyme either from cells of S. typhimurium incubated at 37 C or from cells of S. pullorum incubated at 25 C. Cells cultured at 37 C continued to accumulate sulfite when the incubation temperature was shifted to 25 C; cells cultured at 25 C and shifted to 37 C accumulated no sulfite, whereas these cells shifted to 41 C accumulated sulfite. It was concluded that the configuration of the sulfite reductase of S. pullorum strain 6-18 is a function of the incubation temperature at which synthesis occurs.

Acyltransferases↗
PubMed1994

Effects of sulfite on the uptake and binding of benzo[a]pyrene diol epoxide in cultured murine respiratory epithelial cells.

Sulfur dioxide (SO2) may act as a cocarcinogen with benzo[a]pyrene (BaP) in the respiratory tract. We have modeled this effect by examining the interactions of 7r,8t-dihydroxy-9t,10t-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (anti-BPDE) with sulfite, the physiological form of SO2, in a murine respiratory epithelial cell line (C10). We exposed C10 cells to [3H]-anti-BPDE and determined the effects of 1 and 10 mM sulfite on the uptake and subcellular localization of labeled products. Autoradiographic analysis showed that sulfite doubled the nuclear localization of anti-BPDE-derived materials after a 4-hr incubation period. The net nuclear localization of anti-BPDE-derived materials was not affected by sulfite during the first 60 min, but nuclear localization continued to increase in the sulfite-containing incubations throughout the 4-hr incubation period. Little increase in nuclear localization of anti-BPDE-derived material was noted in the incubations without sulfite after 60 min. Subcellular fractionation was performed to determine the amount of label associated with cytosolic and nuclear fractions and to determine covalent binding to protein and DNA. Sulfite produced a modest increase in the amount of [3H]-anti-BPDE-derived products bound to protein; however, binding to nuclear DNA increased by more than 200% with 10 mM sulfite. Analysis of the supernatants from the cytosolic and nuclear fractions of cells exposed to anti-BPDE and sulfite demonstrated the presence of 7r,8t,9t-trihydroxy-7,8,9,10-tetrahydrobenzo[a]pyrene-10c-su lfonate (BPT-10-sulfonate). [3H]-BPT-10-sulfonate was unable to enter C10 cells, suggesting that it is formed intracellularly.(ABSTRACT TRUNCATED AT 250 WORDS)

7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide↗
PubMed1993

Sulfite both stimulates and inhibits the yeast vacuolar H(+)-ATPase.

The yeast vacuolar H(+)-ATPase (V-ATPase) exhibits nonlinear hydrolysis kinetics, i.e. an initial rapid rate followed by a slower, steadily declining rate. Sulfite (50-100 mM) stimulates the yeast V-ATPase specifically during the latter period. Sulfite activation has been observed for the F-ATPases and archaebacterial ATPases and is thought to be caused by the release of tightly bound nucleotide at the catalytic site. However, turnover-dependent inactivation of the yeast V-ATPase, and sulfite stimulation, were only observed at MgATP concentrations > 1.0 mM. Below 1.0 mM MgATP, the hydrolysis time course was linear, and sulfite was inhibitory. The inhibition during the initial phase and the stimulation during the later phase of the time course could be accounted for by a 5.5-fold sulfite-induced increase in the apparent Km, and a small increase in the apparent Vmax. Sulfite also protected the enzyme against inhibition by cold inactivation and by dicyclohexylcarbodiimide but not by bafilomycin. Sulfite stimulation during the later phase was antagonized by delta mu H+, particularly by delta pH. In contrast to its effects on hydrolysis, sulfite inhibited the formation of a pH gradient at all times and failed to enhance the membrane potential even when delta pH was collapsed by nigericin. These results indicate that sulfite partially uncouples hydrolysis from proton transport in a way that preserves regulation by delta mu H+.

Adenosine Triphosphate↗
PubMedDate not supplied

Effects of sodium sulfite on recovery and composition of detergent fiber and lignin.

Use of sodium sulfite to reduce nitrogenous contamination in fiber analysis was evaluated. The effects of sodium sulfite on analytical accuracy and precision were examined for amylase-treated neutral detergent fiber (aNDF), sequentially determined acid detergent fiber (sADF), and acid detergent lignin (sADL) in animal feeds. In one experiment, 0.5 g sodium sulfite was added per sample during neutral detergent (ND) extraction. The treatment consistently reduced aNDF, sADF, and sADL values of 180 alfalfa samples and improved precision (decreased within-sample variance of replicated analyses). The greatest effect was on precision of sADL analysis, with within-sample variance reduced by more than 50%. In a second experiment, 24 animal feeds were analyzed for a aNDF, sADF, and sADL with and without addition of 0.5 g sodium sulfite per sample during ND extraction. Nitrogen contents of the recovered fiber fractions were determined. Sodium sulfite reduced fiber and lignin values and decreased nitrogen concentration in residues. Within-sample variance was lower in all analyses. In a third experiment, 23 animal feeds were analyzed for aNDF with sodium sulfite at 0, 0.25, 0.5, and 1.0 g per sample. Average aNDF of feeds was reduced by each additional increment of sodium sulfite; however, 1.0 g sodium sulfite resulted in only a slight reduction in aNDF compared with 0.5 g. Therefore, 0.5 g sodium sulfite per sample should be added to samples prior to aNDF analysis.

Amylases↗
PubMed2001

Six-membered cyclic sulfites derived from glucofuranose and 1,2,4-butanetriol.

Six-membered cyclic sulfites derived from glucofuranose derivatives 5, 6 and from 1-O-tert-butyldimethylsilil-1,2,4-butanetriol 12 were synthesized and separated into pure diastereomers which were in turn subjected to the sequence of reactions leading to the introduction of the terminal vinyl ether fragment. Reactivity and applicability of cyclic sulfites as intermediates in [2+2]cycloaddition of chlorosulfonyl isocyanate (CSI) to vinyl ethers were studied. The cycloaddition to vinyl ethers 19 and 20 proceeded in low yield and low asymmetric induction, in the case of the former, and moderate yield and pronounced asymmetric induction, in the case of the latter. The (1)H-NMR spectra of sulfites 13-16 reveal a preference of the sulfite oxygen atom for the axial position. Thus, well-defined conformation in solution for compounds 13 and 15 and a mixture of the two possible chair forms for sulfites 14 and 16 could be assigned. The stretching frequency of the S-->O bond in stable conformation with an axial sulfite oxygen occurs in the range 1,160-1,210 cm(-1), whereas conformationally mobile sulfites exhibit corresponding absorption above 1,220 cm(-1). The absolute configuration assignments of sulfites 7, 8, 15, 16 and 25-28 were done empirically based on the combined analysis of the NMR, IR, X-ray, and dichroic data. It was demonstrated that the sign of the Cotton effect around 194 nm correlated with the absolute stereochemistry at the sulfur atom in a sulfite chromophore.

Journal Article↗
PubMed2005

Structural insights into sulfite oxidase deficiency.

Sulfite oxidase deficiency is a lethal genetic disease that results from defects either in the genes encoding proteins involved in molybdenum cofactor biosynthesis or in the sulfite oxidase gene itself. Several point mutations in the sulfite oxidase gene have been identified from patients suffering from this disease worldwide. Although detailed biochemical analyses have been carried out on these mutations, no structural data could be obtained because of problems in crystallizing recombinant human and rat sulfite oxidases and the failure to clone the chicken sulfite oxidase gene. We synthesized the gene for chicken sulfite oxidase de novo, working backward from the amino acid sequence of the native chicken liver enzyme by PCR amplification of a series of 72 overlapping primers. The recombinant protein displayed the characteristic absorption spectrum of sulfite oxidase and exhibited steady state and rapid kinetic parameters comparable with those of the tissue-derived enzyme. We solved the crystal structures of the wild type and the sulfite oxidase deficiency-causing R138Q (R160Q in humans) variant of recombinant chicken sulfite oxidase in the resting and sulfate-bound forms. Significant alterations in the substrate-binding pocket were detected in the structure of the mutant, and a comparison between the wild type and mutant protein revealed that the active site residue Arg-450 adopts different conformations in the presence and absence of bound sulfate. The size of the binding pocket is thereby considerably reduced, and its position relative to the cofactor is shifted, causing an increase in the distance of the sulfur atom of the bound sulfate to the molybdenum.

Amino Acid Sequence↗
PubMed1989

Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.

The hemoprotein component of Salmonella typhimurium sulfite reductase (NADPH) (EC 1.8.1.2) was purified to homogeneity from cysJ266, a mutant strain lacking sulfite reductase flavoprotein. The siroheme- and Fe4S4-containing enzyme was isolated as a monomeric 63-kDa polypeptide and consisted of a mixture of unligated enzyme and a complex with sulfite. Following reduction with 5'-deazaflavin-EDTA and reoxidation, the complex was converted to the uncomplexed, high spin ferri-siroheme state seen previously with Escherichia coli sulfite reductase hemoprotein preparations. The S. typhimurium hemoprotein exhibited catalytic and physical properties identical to the hemoprotein prepared by urea dissociation of E. coli sulfite reductase holoenzyme and was fully competent in reconstituting NADPH-sulfite reductase activity when combined with excess purified sulfite reductase flavoprotein. The DNA sequences of cysI and cysH from S. typhimurium and E. coli B were determined and, together with previously reported data, confirmed the organization of this region as promoter-cysJ-cysI-cysH with all three genes oriented in the same direction from the promoter. Molecular weights deduced for the cysI-encoded sulfite reductase hemoprotein and for the cysH-encoded 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase were approximately 64,000 and 28,000, respectively. Comparison of the deduced amino acid sequence of sulfite reductase hemoprotein with that of spinach nitrite reductase (Back, E., Burkhart, W., Moyer, M., Privalle, L., and Rothstein, S. (1988) Mol. Gen. Genet. 212, 20-26), which also contains siroheme and an Fe4S4 cluster, showed two groups of cysteine-containing sequences with the structures Cys-(X)3-Cys and Cys-(X)5-Cys, which are homologous in the two enzymes and are postulated to provide the ligands of the Fe4S4 cluster in both proteins. From these sequences and from crystallographic (McRee, D. E., Richardson, D. C., Richardson, J. S., and Siegel, L. M. (1986) J. Biol. Chem. 261, 10277-10281) and spectroscopic data in the literature, a model is proposed for the structure of the active center of these two enzymes.

Amino Acid Sequence↗
PubMed1983

Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum.

Sulfite oxidase from Thiobacillus novellus has been purified 206-fold. The enzyme reduced both ferricyanide and cytochrome c. The ferricyanide activity was 3-5% of the cytochrome c activity. During purification, the absorbance ratio of A413 nm/A280 nm showed a continual increase, suggesting the presence of heme in the T. novellus sulfite oxidase molecule. The absorption spectrum of the enzyme is very similar to that of rat liver sulfite oxidase which contains cytochrome b5 type heme. Gel electrophoresis of the purified protein in the presence of sodium dodecyl sulfate revealed a protein staining band of approximately 41,000 Da. Gel filtration chromatography of the enzyme in aqueous media indicated a molecular weight of 38,000. These results suggest that T. novellus sulfite oxidase is a monomer of approximately 40,000 Da. Moreover, analysis of the visible absorption spectrum of the purified enzyme and the co-elution of 413 and 280 nm absorbing material during high pressure liquid chromatography gel chromatography provided clear evidence for the presence of heme in T. novellus sulfite oxidase. EPR spectroscopy of the enzyme revealed a characteristic molybdenum spectrum, which was observed only in the presence of sulfite. Analysis of the T. novellus sulfite oxidase molybdenum cofactor showed a fluorescence spectrum indistinguishable from that displayed by the molybdenum cofactor of chicken liver sulfite oxidase. Therefore, it is concluded that T. novellus sulfite oxidase is a monomeric (Mr approximately 40,000) molybdohemoprotein.

Heme↗
PubMed2005

A biocatalyst for the removal of sulfite from alcoholic beverages.

The presence of sulfites in alcoholic beverages, particularly in wines, can cause allergic responses with symptoms ranging from mild gastrointestinal problems to life threatening anaphylactic shock in a substantial portion of the population. We have developed a simple and inexpensive biocatalytic method that employs wheatgrass (Triticum aestivum) chloroplasts for the efficient oxidation of sulfites in wines to innocuous sulfates. A sufficiently high rate of sulfite oxidation was obtained in the presence of ethanol at concentrations commonly found in most wines. Crude chloroplast preparations at a concentration as low as 5 mg/mL were capable of reducing sulfite in commercial white wines from 150 ppm to under 7.5 ppm within 3 hours. A 93% removal of sulfite in commercial red wines was observed with 1 mg/mL chloroplasts within 45 min. Optimal sulfite removal efficiency was observed at pH 8.5 and was promoted by illumination, indicating the participation of light-induced photosynthetic electron transport processes in sulfite oxidation. Overall, this work indicates that biocatalytic oxidation using wheatgrass chloroplasts can be employed to remove sulfites from beverages prior to consumption.

Alcoholic Beverages↗
PubMed1986

Covalent reactions in the toxicity of SO2 and sulfite.

Toxic effects of SO2 and sulfite such as bronchitis and bronchoconstriction have been well documented. SO2 has also been suggested to potentiate carcinogenic effects of PAH. However, the molecular basis of these toxic effects is unclear. We have examined the covalent reaction of SO2 and sulfite with cellular proteinacious and nonproteinaceous sulfhydryl compounds using rat liver, and lung and human lung derived A549 cells. Reactions of sulfite and protein in rat and human lung cells reveals at least three proteins with sulfite-reactive disulfide bonds. Besides fibronectin and serum albumin, which had been reported to contain sulfonated products following exposure to sulfite, we have found one other protein with sulfite-binding capabilities. Since the integrity of disulfide bonds is crucial to the tertiary structure and thus protein function, the disruption of protein structure by sulfitolysis may result in altered cellular activities leading to biochemical lesions. Using carefully controlled conditions, reproducible GSH contents can be found in cultured cells and used as an experimental basis for studying alterations in the GSH and GSSG content of cells. Sulfitolysis of GSSG results in the formation of GSSO3H in A549 cells, and possibly in the lung. GSSO3H can be reduced enzymatically by GSSG reductase. However, the Km of GSSO3H is high compared to that of GSSG, suggesting the existence of a transient concentration of GSSO3H once it is formed. Cysteine S-sulfonate is, however, not reduced by cytosolic extracts in the presence of NADPH and would have to be eliminated from the cell by other means. GSSO3H is a strong competitive inhibitor of GST in rat liver and lung and A549 cells, using 1-chloro-2,4-dinitrobenzene as a substrate. It also inhibits the formation of GSH conjugates of BP 4,5-oxide, anti and syn BPDE, but to a lesser extent. These results suggest that SO2 may affect the detoxification of xenobiotic compounds by inhibiting, via formation of GSSO3H, the enzymatic conjugation of GSH and reactive electrophiles. Since GSH conjugation represents the major pathway of elimination of BP epoxides in the lung, our results offer a possible explanation for the cocarcinogenicity of SO2 with PAHs. These data suggest that the sulfitolysis reaction of sulfite is the common reaction mechanism mediating the underlying biochemical reactions leading to both the toxic and cocarcinogenic properties of SO2. Quantitation of sulfitolysis products and their interaction with cellular processes should provide a coherent scheme relating SO2 and sulfite toxicity among animal species and humans.

Animals↗
PubMed1993

Sulfite stimulates NADPH oxidase of human neutrophils to produce active oxygen radicals via protein kinase C and Ca2+/calmodulin pathways.

The effect of sulfite on the oxidative metabolism of human neutrophils was studied in vitro. Superoxide anion production of PMN was determined using superoxide dismutase-inhibitable lucigenin-dependent CL. The addition of sulfite in concentrations of 0.01 mM-1 mM results in an up to 6-fold increase in CL of nonstimulated neutrophils at 37 degrees C and pH 7. Neutrophils stimulated with zymosan or PMA have an additional 2-fold stimulation when sulfite is added. Higher sulfite concentrations (2 mM-10 mM) decrease the CL of both nonstimulated and stimulated cells. The activity of NADPH oxidase, responsible for O2.- production, is significantly increased in neutrophils incubated with 1 mM sulfite. Neutrophils from patients with chronic granulomatous disease, which are cytochrome b558 negative or have p47phox deficiency, exhibit no significant NADPH oxidase activity and show no increase in CL by sulfite. Inhibitors of protein kinase C, H7, and calphostin C, as well as inhibitors of Ca(2+)- and calmodulin-dependent processes, W7, and R 24 571, completely inhibited the increased CL of sulfite-treated neutrophils. These findings indicate that sulfite in low concentrations stimulates neutrophils to produce superoxide anions by activation of NADPH oxidase through a signal transduction pathway involving protein kinase C and Ca2+/calmodulin.

Calcium↗
PubMed2005

Sulfite facilitates LDL lipid oxidation by transition metal ions: a pro-oxidant in wine?

Lipid oxidation in LDL may play a role in atherogenesis. It has been shown that sulfite - a compound in the aqueous fraction of wine - could inhibit free radical (AAPH) mediated oxidation of plasma. Thus, sulfite has been proposed as an antioxidant. In contrast, the aqueous phase of wine has recently been shown to contain not fully identified compounds promoting transition metal ion (Cu(2+)) initiated LDL oxidation. As transition metal ions can catalyse the auto-oxidation of sulfite, we studied the influence of sulfite on Cu(2+) initiated LDL oxidation. The results show that sulfite at concentrations found in vivo strongly facilitated LDL oxidation by Cu(2+). The LDL-oxidase activity of ceruloplasmin was also stimulated by sulfite. ROS formation by Cu(2+)/SO(3)(2-) was not inhibited by SOD but by catalase. We propose that formation of Cu(+), sulfite radicals (SO(3)*(-)) and hydroxyl radicals (OH(*)) is a mechanism by which sulfite could act as a pro-atherogenic agent in presence of transition metal ions.

Amidines↗
PubMed2000

Picomolar quantitation of free sulfite in foods by means of [57Co]hydroxocobalamin and radiometric chromatography of [57Co]sulfitocobalamin. Method, applications and significance of coexisting sulfides.

The concentration dependent reaction of sulfite with 57Co-labeled hydroxocobalamin (OH57CoCbl) to produce a sulfitocobalamin (SO(3)57CoCbl) adduct served as a quantification strategy for foodborne sulfite residues freely extracted into pH 5.2, 0.05 M acetate buffer. SO(3)57CoCbl was then resolved using SP-Sephadex C-25 gel chromatography and its radiometric detection allowed calculation of a standard logit plot from which unknown sulfite concentrations could be determined. The sulfite detection range was 6.0 nM-0.3 pM with respective relative standard deviations of 4.4-29.4% for 50-microl samples. Individual incidences of foodborne sulfite intolerances provoked by L-cysteine or sulfite additive use in bakery products, which remained undetected using conventional sulfite analytical methods, underscored the quantitative value of the method. The analytical significance and occurrences of detectable sulfides coexisting with foodborne sulfite residues was also addressed.

Chromatography, Gel↗