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PubMed1991

Chemoprotectants for cancer chemotherapy.

Maximal dosing of cytotoxic chemotherapy drugs is often limited by the development of severe nonmyelosuppressive toxicities. Numerous studies have demonstrated that sulfur-containing nucleophiles can antagonize the dose-limiting effects of alkylating agents on the genitourinary tract. Examples include the use of sodium thiosulfate to prevent cisplatin-induced renal tubular necrosis and the use of sulfhydryl-containing compounds like N-acetylcysteine and 2-mercaptoethanesulfonate (mesna) to block oxazophosphorine-induced bladder toxicity. Mesna does not block the antitumor action of oxazophosphorines due to its rapid formation of the inactive dimer dimesna in the bloodstream. The active monomer is selectively reduced from dimesna in renal tubule cells, thereby limiting the inactivation of toxins like acrolein to the genitourinary tract. Recent clinical trials suggest that oral mesna has adequate bioavailability (roughly 50% by urinary thiol measurements) to prevent urotoxicity in high-dose ifosfamide regimens. In addition, mesna is stable in aqueous oral formulations. This may facilitate more convenient oral mesna dosing in protocols using high-dose cyclophosphamide or ifosfamide. Whereas agents like mesna and sodium thiosulfate complex directly with activated (electrophilic) alkylator species, chemoprotectants for the anthracyclines appear to complex with metal cofactors like iron, which are required for the production of cardiotoxicity. Several ethylenediaminetetraacetic-like agents have been evaluated, and a water-soluble piperazinyl derivative, ICRF-187, is currently undergoing clinical evaluation in patients receiving large cumulative doxorubicin doses. An initial clinical trial suggests that ICRF-187 can prevent doxorubicin-induced cardiomyopathy. As with mesna, ICRF-187 does not block the myelosuppressive or the antitumor effects of doxorubicin. Overall, these studies show that site-selective chemoprotection is now feasible for at least two major classes of anticancer agents.

Antibiotics, Antineoplastic↗

PubMedDate not supplied

[The efficacy of water ozonation on the inactivation of oocysts of Cryptosporidium].

Cryptosporidium oocysts are currently found in surface waters. Their incomplete removal by sand filtration and their high resistance to chlorinated disinfectants make possible waterborne cryptosporidiosis outbreaks after drinking treated water. Because ozone is an alternative to chlorine for final drinking water disinfection the aim of our study was to determine the ozonation conditions able to eliminate the infectivity of oocysts. Feces from horses naturally infected by C. parvum were mixed with distilled water. The obtained suspension was clarified by passing through a graded series of four sieves (pore sizes, 315, 200, 125 and 63 microns). The clarified suspension was decontaminated by adding a 10% sodium hypochlorite solution. After a 10 minute contact time at room temperature, the chlorine residual was neutralised by the exactly requisite volume of a 0.01 N sodium thiosulfate solution. Oocysts in the suspension were purified by centrifugation and washing of pellets in distilled water. Oocysts in the finally obtained suspension were numerated by counting in a Malassez haemocytometer. Ozonated water containing dissolved ozone residuals ranging from 0.44 mg/l to 1.09 mg/l were inoculated with a number of oocysts ranging from 1.10(6) to 1.10(8). Contact times with ozone were 4.6 or 8 minutes. After destroying the ozone residual by sodium thiosulfate, ozonated oocysts were administered by oral route to male Sprague-Dawley rats weighing between 180 to 200 g and beforehand immunosuppressed by a regimen of 25 mg hydrocortisone acetate subcutaneously twice a week, 5 weeks before and 3 weeks after Cryptosporidium challenge. Oocyst shedding was daily controlled by phase contrast microscoy in smears of fecal suspension mixed with carbolfuchsine solution.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1986

Clinical features and management of cyanide poisoning.

The pathophysiology, clinical features, and management of cyanide toxicity are reviewed and sources of cyanide are listed. Cyanide is a deadly poison that is found in many foods and household and industrial products, including some that are readily available. Cyanide binds with cytochrome oxidase, the enzyme responsible for oxidative phosphorylation, and paralyzes cellular respiration. Because the tissues cannot use oxygen that is delivered, aerobic metabolism ceases. The signs and symptoms of cyanide poisoning reflect the extent of cellular hypoxia. Manifestations may include respiratory abnormalities (progressing from tachypnea and dyspnea to respiratory depression and apnea), hemodynamic instability, metabolic acidosis, and, possibly, local irritant effects after oral ingestion of cyanide. The mainstays of therapy are 100% oxygen and specific antidotes to cyanide. Sequential treatment with amyl nitrite by inhalation, intravenous sodium nitrite 3%, and intravenous sodium thiosulfate 25% is directed toward decreasing the amount of cyanide available for cellular binding. Nitrites convert hemoglobin to methemoglobin, which reacts with cyanide to form cyanomethemoglobin. Sodium thiosulfate serves as a source of sulfur groups, which are needed for conversion of cyanide to thiocyanate, a compound that is relatively less toxic and is excreted renally. Supportive care also is important. Cobalt EDTA, hydroxocobalamin, and aminophenols have also been used but are not considered standard treatments. Cyanide poisoning is a medical emergency that requires prompt recognition and immediate and aggressive treatment.

Antidotes↗

PubMed1985

The role of cyanide in fires.

Cyanide is a potent and rapidly lethal poison whose clinical and laboratory diagnosis is difficult. Cyanide is released in fire settings involving wool, silk and many synthetic polymers posing a definite risk. Interactions of carbon monoxide released in a fire and cyanide have important physiological consequences. Although the classic mechanisms for the toxicology and antagonism of cyanide have been studied for many years, recent studies have cast doubt as to the mechanism of some of these antagonists. In the fire setting it is not clinically acceptable to administer nitrites to create methemoglobinemia. Cobalt salts are currently too toxic. Oxygen should be administered but there is no proven benefit of hyperbaric oxygen. Oxygen, thiosulfate and hydroxycobalamin are probably the best and safest currently available antidotes to manage this difficult setting. In the future, encapsulated rhodanese enzyme may provide additional rapid therapeutic intervention. It is anticipated that oxygen, thiosulfate and hydroxycobalamin are a safer and more clinically acceptable antidotal combination in the management of cyanide exposure in the fire setting. Our current understanding of combustion toxicology should provide an opportunity to remove building materials and furnishings which pose a cyanide hazard in a fire setting.

Animals↗

PubMed1985

The protective effect of different drugs in rats poisoned by sulfur and nitrogen mustards.

Based on the recent pathognomic accomplishment in the mechanisms of toxic actions, the favorable degree of protection was achieved by several drugs in acute poisoning of rats with sulfur and nitrogen mustards. It has been established that dexamethasone, promethazine, vitamin E, heparin, and sodium thiosulfate (a) prolonged the survival time in animals poisoned by 3 LD50s of toxic agents, (b) diminished the lethalty (with the protective indices ranging from 1.5 to 2.7), (c) antagonized the decrease of body weight, and (d) lessened the degree of pathological organ changes. The simultaneous administration of two or three of the drugs mentioned, of which sodium thiosulfate as chemical inactivator of the toxic agents was basic and consonant component, led to the further increase in effectiveness. It is concluded that satisfactory results obtained in this study speak in favor of the basic pathological effects of mustard gases, as well as possible causes and their possible ways of action as postulated by Dannenberg (1983).

Animals↗

PubMed1984

Effect of gastrointestinal surgery and bacterial overgrowth on the urinary excretion of sulfur amino acids and their main degradation products.

The urinary excretion of sulfur amino acids and their main degradation products was determined in patients subjected to various forms of gastrointestinal surgery or with bacterial overgrowth. A normal excretion of total sulfur and inorganic sulfate was found, indicating an adequate intake and maintained ability to absorb sulfur amino acids. An increased excretion of ester sulfate was observed in all groups except patients subjected to ileocecal resection or proctocolectomy, probably owing to bacterial overgrowth. A reduced excretion of methionine was observed in patients with gastric resection (Billroth I), ileocecal resection, and abnormal gut flora, whereas patients with jejunoileal bypass showed an increased excretion of methionine, probably a consequence of the impaired liver function. For cystathionine, a similar effect was found in patients with ileocecal resection and jejunoileal bypass. A reduced excretion of mercaptolactate was found in jejunoileal bypass patients. A low excretion of thiosulfate was seen in proctocolectomized patients, suggesting that the bacterial flora of the colon plays a role in the formation of thiosulfate. A low excretion of thiocyanate was found in gastric-resected patients, which may be due to a decreased ability to hydrolyze cyanogenic and/or thiocyanogenic glycosides or to a reduced intake of these compounds.

Adult↗

PubMedDate not supplied

[The possibility of using certain antioxidants for reducing ferriheme].

Kinetic parameters of the hemin spectral alterations occurred in reactions with sodium thiosulfate and sodium dithionite were studied depending on the reagents content as well as on the ratio between the antioxidant initial concentration and hemin. Simultaneous analysis of the kinetic parameters enabled one to suggest that hemin was reduced in reactions with sodium thiosulfate and sodium dithionite.

Antioxidants↗

PubMed1994

Electrogenic cotransport of Na+ and sulfate in Xenopus oocytes expressing the cloned Na+SO4(2-) transport protein NaSi-1.

The Na+/sulfate cotransporter cloned from rat kidney cortex (NaSi-1) has been expressed in oocytes of Xenopus laevis and subjected to electrophysiological analysis by current and voltage clamp methods. In current-clamped oocytes, superfusion with 1 mM sulfate resulted in a 12-mV depolarization of the cell membrane. Accordingly, in voltage-clamped oocytes sulfate induced an inward current IS, which was dependent on both the concentration of Na+ and sulfate in the superfusate. Half-maximal IS was observed at about 0.1 mM sulfate and 70 mM Na+. The Hill coefficients were 1 and 2.8 for sulfate and Na+, respectively. Thiosulfate and selenate created similar currents as sulfate with a similar Km. At saturating concentrations of thiosulfate and selenate, addition of sulfate could not induce an additive current. Phosphate (1 mM) did not inhibit sulfate-induced currents. Finally, IS was dependent on the holding potential being larger at more negative potentials. The results of this study strongly suggest an electrogenic cotransport of sulfate and Na+ with a stoichiometry of 1:3.

Animals↗

PubMedDate not supplied

Photostability profiles of minoxidil solutions.

Photostability profiles of minoxidil solutions exposed to fluorescent light, under the influence of several parameters like concentration, pH, buffer species, photostabilizers, container type, solvent system, and skin penetration enhancers were studied. The assay of minoxidil was done spectrophotometrically at 230 nm and 290 nm, using double beam UV-visible spectrophotometer. The results show that photodegradation of minoxidil solutions follows first order rate. Furthermore, minoxidil solution (4.5 micrograms/ml) was found to be more stable in phosphate buffer as compared to acetate buffer. Amber glass offered equivalent photoprotection as aluminum foil-covered glass. Minoxidil was found to be most stable in a solvent system of water or 25% v/v PEG300 and least stable in 25% v/v propylene glycol. Of the penetration enhancers studied dimethyl sulfoxide (DMSO) caused the least photodecomposition of minoxidil. The order of photoprotection of the five potential photostabilizers were as follows: sodium thiosulfate > EDTA > sodium benzoate approximately thiourea > sodium metabisulfite. Varying the concentration of sodium thiosulfate did not affect the minoxidil photostability. The study also indicates that minoxidil solution (4.5 micrograms/ml) is most photostable in pH 8 phosphate buffer. An increase in ionic strength had a photostabilizing effect until an optimum strength of 0.17, then further increase caused the rate of photodegradation to remain unchanged.

Antihypertensive Agents↗

PubMed1998

A fatal case of hydrogen sulfide poisoning in a geothermal power plant.

An adult man entered an oil separator room to remove waste oil from a vacuum pump in a geothermal power plant. He suddenly collapsed and died soon after. Since hydrogen sulfide gas was detected in the atmosphere at the scene of the accident, poisoning by this gas was suspected and toxicological analysis of sulfide and thiosulfate in blood, brain, lung, femoral muscle was made using the extractive alkylation technique combined with gas chromatography/mass spectrometry (GC/MS). The concentrations of sulfide in these tissues were similar to those previously reported for fatal cases of hydrogen sulfide gas. The concentration of thiosulfate in the blood was at least 48 times higher than the level in control samples. Based on these results, the cause of death was attributed to hydrogen sulfide gas poisoning.

Accidents, Occupational↗

PubMed1999

Alkali metal ions protect mitochondrial rhodanese against thermal inactivation.

Incubation of bovine liver mitochondrial rhodanese in dilute, reducing solutions at temperatures ranging between 30 and 45 degreesC conduced to a rapid loss of enzymatic activity. This inactivation was substantially reduced in the presence of millimolar concentrations of alkali metal ions, divalent cations (including Mg2+, Ca2+, and Ba2+) were ineffective. The extent of protection afforded by monovalent cations was highly dependent on their ionic radii, with K+ and Na+ ions being the most effective protective agents. The protection afforded by a number of anions, including thiosulfate, could be totally ascribed to the presence of the accompanying monovalent cation. The overall results indicate that K+ and Na+, at concentrations and temperatures within the physiological range, substantially contribute to the stabilization of the functional structure of rhodanese.

Animals↗

PubMed2000

Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate.

ThiI is an enzyme common to the biosynthetic pathways leading to both thiamin and 4-thiouridine in tRNA. Comparison of the ThiI sequence with protein sequences in the data bases revealed that the Escherichia coli enzyme contains a C-terminal extension displaying sequence similarity to the sulfurtransferase rhodanese. Cys-456 of ThiI aligns with the active site cysteine residue of rhodanese that transiently forms a persulfide during catalysis. We investigated the functional importance of this sequence similarity and discovered that, like rhodanese, ThiI catalyzes the transfer of sulfur from thiosulfate to cyanide. Mutation of Cys-456 to alanine impairs this sulfurtransferase activity, and the C456A ThiI is incapable of supporting generation of 4-thiouridine in tRNA both in vitro and in vivo. We therefore conclude that Cys-456 of ThiI is critical for activity and propose that Cys-456 transiently forms a persulfide during catalysis. To accommodate this hypothesis, we propose a general mechanism for sulfur transfer in which the terminal sulfur of the persulfide first acts as a nucleophile and is then transferred as an equivalent of S(2-) rather than S(0).

Amino Acid Sequence↗

PubMed2005

Identification of putative sulfurtransferase genes in the extremophilic Acidithiobacillus ferrooxidans ATCC 23270 genome: structural and functional characterization of the proteins.

Eight nucleotide sequences containing a single rhodanese domain were found in the Acidithiobacillus ferrooxidans ATCC 23270 genome: p11, p14, p14.3, p15, p16, p16.2, p21, and p28. Amino acids sequence comparisons allowed us to identify the potentially catalytic Cys residues and other highly conserved rhodanese family features in all eight proteins. The genomic contexts of some of the rhodanese-like genes and the determination of their expression at the mRNA level by using macroarrays suggested their implication in sulfur oxidation and metabolism, formation of Fe-S clusters or detoxification mechanisms. Several of the putative rhodanese genes were successfully isolated, cloned and overexpressed in E. coli and their thiosulfate:cyanide sulfurtransferase (TST) and 3-mercaptopyruvate/cyanide sulfurtransferase (MST) activities were determined. Based on their sulfurtransferase activities and on structural comparisons of catalytic sites and electrostatic potentials between homology- modeled A. ferrooxidans rhodaneses and the reported crystal structures of E. coli GlpE (TST) and SseA (MST) proteins, two of the rhodanese-like proteins (P15 and P16.2) could clearly be defined as TSTs, and P14 and P16 could possibly correspond to MSTs. Nevertheless, several of the eight A. ferrooxidans rhodanese-like proteins may have some different functional activities yet to be discovered.

Acidithiobacillus↗

PubMed1964

THE GENUS VEILLONELLA. 3. HYDROGEN SULFIDE PRODUCTION BY GROWING CULTURES.

Rogosa, Morrison (National Institute of Dental Research, Bethesda, Md.), and Ferial S. Bishop. The genus Veillonella. III. Hydrogen sulfide production by growing cultures. J. Bacteriol. 88:37-41. 1964.-The conditions necessary for H(2)S production by 105 strains of Veillonella, from a variety of sources and comprising seven anti-genic groups, are presented and discussed. All strains, during 1 to 2 days of growth, produced H(2)S in a defined medium supplemented with proper amounts of l-cysteine, l-cystine, reduced glutathione, thiosulfate, thiocyanate, or thioglycolate. Erratic or negative results were obtained with some commonly used media containing yeast extract and casein digest, but which were not supplemented with appropriate substrates for H(2)S production. Previous literature descriptions of V. alcalescens as not producing H(2)S are incorrect; H(2)S production, or the previously presumed lack of it, cannot be used as a criterion differentiating V. alcalescens from V. parvula.

Culture Media↗

PubMed1964

EFFECT OF CATALASE AND CULTURAL CONDITIONS ON GROWTH OF BEGGIATOA.

Burton, Sheril D. (Oregon State University, Corvallis), and Richard Y. Morita. Effect of catalase and cultural conditions on growth of Beggiatoa. J. Bacteriol. 88:1755-1761. 1964.-The addition of catalase to culture medium increased the period of viability of Beggiatoa from 1 week to 2 months. Addition of catalase also produced a marked increase in cell yield and enzyme activity. Cultures grown without catalase exhibited an absorption peak characteristic of peroxides. This absorption peak was removed by addition of catalase during or after growth. Oxygen was required for growth, but carbon dioxide was not produced. Malate and acetate stimulated growth at low concentrations. Glucose and thiosulfate were not oxidized, and cytochromes were not detectable by spectrophotometric analysis.

Acetates↗

PubMed1999

Nitric oxide stimulates growth hormone secretion in vitro through a calcium- and cyclic guanosine monophosphate-independent mechanism.

In the last years, nitric oxide (NO) has emerged as an important intra- and intercellular transmitter involved in the control of the hypothalamic-pituitary axis, and NO synthase (NOS) has been identified in pituitary cells. To determine the role of NO in the control of GH secretion acting directly at the pituitary level, we have studied GH release by hemipituitaries incubated in the presence of different concentrations (10(-7)-10(-3) M) of sodium nitroprusside (SNP), a potent NO donor. We found that SNP (10(-4)-10(-3) M) stimulated GH release. This effect was mediated by the release of NO since it was abolished in the presence of hemoglobin, a scavenger of NO, but preserved in the presence of rhodanese + sodium thiosulfate (inactivators of cyanides generated from SNP). To analyze the participation of cyclic guanosine monophosphate (cGMP), the second messenger for a wide range of NO actions, in SNP-stimulated GH secretion, hemipituitaries were incubated in the presence of 8-bromo-cGMP (8-Br-cGMP; 10(-7)-10(-3) M). In addition, hemipituitaries were stimulated with SNP plus oxadiazoloquinoxaline (OQD) or LY 83,583 (inhibitors of guanylyl cyclases). We found that 8-Br-cGMP was ineffective in eliciting GH release, and that the stimulatory effect of SNP was maintained in presence of OQD and LY 83,583. Finally, to analyze calcium dependence, the SNP effect was studied in hemipituitaries incubated in free medium calcium, in the presence of nifedipine and verapamil (blockers of calcium channels) and after depletion of intracellular Ca(2+) stores with caffeine. We found that the SNP-induced GH secretion is also detected after incubation of hemipituitaries in free calcium medium, in the presence of nifedipine and verapamil, and after caffeine preincubation. We conclude that NO stimulates GH secretion in vitro through a specific calcium-cGMP-independent mechanism. Copyrightz1999S.KargerAG,Basel

Animals↗

PubMed2004

Nitric oxide donor sodium nitroprusside dilates rat small arteries by activation of inward rectifier potassium channels.

The role of vascular smooth muscle inward rectifier K+ (K(IR)) channels in the mechanisms underlying vasodilation is still unclear. The hypothesis that K(IR) channels are involved in sodium nitroprusside (SNP)-induced dilation of rat-tail small arteries was tested. SNP relaxed tail small arteries with an EC50 of 2.6x10(-8) mol/L. Endothelium removal did not attenuate this effect. Vessel pretreatment with hydroxocobalamin, a nitric oxide (NO) scavenger, but not with rhodanese and sodium thiosulfate, inactivators of cyanide (CN), abolished the SNP effect. Vessel pretreatment with 10(-5) mol/L Ba2+, a specific blocker of K(IR) channels at micromolar concentrations, reduced the SNP effect. Low concentrations of K+ dilated the vessels; this effect was attenuated largely after pretreatment with 3x10(-5) mol/L Ba2+. In freshly isolated smooth muscle cells, a barium-sensitive current was observed at potentials negative to the potassium equilibrium potential. Application of 10(-4) mol/L SNP increased the barium-sensitive current 1.79+/-0.23-fold at -100 mV and hyperpolarized the membrane potential by 8.6+/-0.5 mV. In tissue from freshly dissected vessels, transcripts for K(IR) 2.1 and 2.2, but not for K(IR) 2.3 and 2.4, were found. However, only K(IR) 2.1 antibodies immunostained the tunica media of the vessel. These data suggest that vascular smooth muscle K(IR) 2.1 channels are involved in the SNP-induced dilation of rat-tail small arteries.

Animals↗

PubMed1989

Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation.

Controlled conditions have been found that give complete reactivation and long term stabilization of rhodanese (EC 2.8.1.1) after oxidative inactivation by hydrogen peroxide. Inactivated rhodanese was completely reactivated by reductants such as thioglycolic acid (TGA) (100 mM) and dithiothreitol (DTT) (100 mM) or the substrate thiosulfate (100 mM) if these reagents were added soon after inactivation. Reactivability fell in a biphasic first order process. At pH 7.5, in the presence of DTT inactive rhodanese lost 40% of its reactivability in less than 5 min, and the remaining 60% was lost more gradually (t 1/2 = 3.5 h). TGA reactivated better than DTT, and the rapid phase was much less prominent. If excess reagents were removed by gel filtration immediately after inactivation, there was time-independent and complete reactivability with TGA for at least 24 h, and the resulting samples were stable. Reactivable enzyme was resistant to proteolysis and had a fluorescence maximum at 335 nm, just as the native protein. Oxidized rhodanese, Partially reactivated by DTT, was unstable and lost activity upon further incubation. This inactive enzyme was fully reactivated by 200 mM TGA. Also, the enzyme could be reactivated by arsenite and high concentrations of cyanide. Addition of hydrogen peroxide (40-fold molar excess) to inactive rhodanese after column chromatography initiated a time-dependent loss of reactivability. This inactivation was a single first order process (t 1/2 = 25 min). Sulfhydryl titers showed that enzyme could be fully reactivated after the loss of either one or two sulfhydryl groups. Irreversibly inactivated enzyme showed the loss of one sulfhydryl group even after extensive reduction with TGA. The results are consistent with a two-stage oxidation of rhodanese. In the first stage there can form sulfenyl and/or disulfide derivative(s) at the active site sulfhydryl that are reducible by thioglycolate. A second stage could give alternate or additional oxidation states that are not easily reducible by reagents tried to date.

Arsenic↗