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PubMed2000

Photobiological properties of nabumetone (4-[6-methoxy-2-naphthalenyl]-2-butanone), a novel non-steroidal anti-inflammatory and analgesic agent.

The photolability of nabumetone (NB, 1, 4-[6-methoxy-2-naphthalenyl]-2-butanone) and its photobiological properties were studied under aerobic and anaerobic conditions using a variety of in vitro phototoxicity assays: photohemolysis, photoperoxidation of linoleic acid, and photosensitized degradation of histidine and thymine. The photodegradation rate of NB in methanol and phosphate buffered saline (PBS) was enhanced under oxygenated media. NB was phototoxic in vitro. The photohemolysis rate was enhanced by deuterium oxide and inhibited by the presence of 1,4-diazabicyclo[2.2.2]octane (DABCO), butylated hydroxyanisole (BHA), sodium azide (NaN3) and reduced gluthathione (GSH). The induced photoperoxidation of linoleic acid was inhibited significantly by sodium azide and reduced gluthathione. Histidine and thymine were photodegraded by a photosensitized reaction induced by NB. A mechanism involving singlet oxygen, radicals and photoproducts is suggested for the observed photoxicity.

Aerobiosis↗
PubMed1977

Bioproduction of rubratoxin in a glucose-mineral salts broth with nutritional supplements and metabolic inhibitors.

A sterile glucose-salts broth fortified with various metabolic inhibitors and nutritional supplements was inoculated with conidia of Penicillium rubrum P3290, and incubated quiescently at 28 degrees C for 14 days. Potassium sulfite and sodium metabisulfite at all test concentrations caused moderate reduction in rubratoxin formation; at high concentrations (greater than or equal to 2.7 X 10(-2)M) accumulation of fungal tissue was also retarded. Production of rubratoxin and cell mass was inhibited by p-aminobenzoic acid; syntheses of toxin were completely blocked by 7.5 X 10(-2)M of the vitamin. Effects of sodium fluoride on P. rubrum cultures grown on inorganic nitrogen sources varied from inhibition of mold growth and (or) rubratoxin A production to reduction in formation of rubratoxin B. With organic nitrogen sources, fluoride caused a 30 and 60% reduction in synthesis of rubratoxins A and B, respectively. Sodium acetate at all test concentrations enhanced formation of rubratoxin; mold growth was enhanced when acetate concentration was larger than or equal to 6.0 X 10(-2)M. A moderate reduction in mold growth was caused by lower acetate concentrations (1.2 X 10(-2)M or 2.4 X 10(-2)M). Sodium arsenite and iodoacetate at test concentrations blocked mold growth and toxin formation; sodium azide and 2,4-dinitrophenol caused a marked reduction in mold growth but inhibited toxin formation completely. However, sodium azide permitted slight growth and toxin formation when mold cultures were incubated for 28 days.

4-Aminobenzoic Acid↗
PubMed1991

Antimutagenicity of propionic acid bacteria.

The antimutagenic effect of dialysed cell extracts of 4 strains of propionic acid bacteria was examined against the mutagenicity of sodium azide in the TA1535 tester strain of Salmonella typhimurium using the Ames test. It was noted that dialysates of 2 strains of Propionibacterium shermanii, P. pentosaceum and P. acnes, significantly reduced sodium azide-induced revertants. The dialysate of propionic acid cocci did not show an antimutagenic effect. The inhibitory activity was enhanced if the mutagen and extract were coincubated for 20 min prior to performing the mutagenicity assay. Antimutagenicity of dialysates from P. shermanii VKM-103 against MNNG and 9-aminoacridine was shown in S. typhimurium strains TA1535 and TA97. The antimutagenic activity was found in the protein fraction of the cell extract of P. shermanii. The proteins of the dialysate of P. shermanii were separated using a Toyopearl gel column into 3 main peaks according to their molecular weights. The antimutagenic activity towards sodium azide was found in the second and the third peaks. We suggest that dialysates of the cells of propionic acid bacteria contain several kinds of antimutagenic substances with different molecular weights.

Aminacrine↗
PubMed1985

[Studies on the relationship between the oxygen uptake and the release of amylase and sialic acid].

The relationship between the oxygen uptake and the release of amylase and sialic acid induced by pilocarpine was investigated in dog submandibular glands. Pilocarpine dose-dependently stimulated the oxygen uptake. The dose required for the maximal response was 10 microM. The release of amylase and sialic acid induced by pilocarpine was inhibited by the addition of iodoacetic acid, malonic acid, 2, 4-dinitrophenol, antimycin A or sodium azide. The oxygen uptake induced by pilocarpine was significantly inhibited by iodoacetic acid, malonic acid, antimycin A or sodium azide. On the other hand, 2, 4-dinitrophenol further stimulated the oxygen uptake by pilocarpine. The increase in the oxygen uptake or the release of amylase and sialic acid induced by pilocarpine was significantly inhibited by ouabain. The Na+, K+-ATPase activity ratio in the microsomal fraction of dog submandibular glands was dose-dependently increased by pilocarpine. The Na+, K+-ATPase activity ratio induced by pilocarpine was significantly inhibited by ouabain, antimycin A, oligomycin or 2, 4-dinitrophenol. The pilocarpine-induced Na+, K+-ATPase activity ratio was significantly inhibited by the removal Ca2+ from the medium or the addition of 2 mM EGTA. These results suggest that the increase in the oxygen uptake by pilocarpine is profoundly involved in the energy supply for the process of amylase and sialic acid release. In particular, the energy supply demanded for the activation of Na+ pump may play a role in the mechanism by which pilocarpine induces the oxygen uptake.

Amylases↗
PubMed2001

Characterisation of an ATP diphosphohydrolase (Apyrase, EC 3.6.1.5) activity in Trichomonas vaginalis.

In the present report the enzymatic properties of an ATP diphosphohydrolase (apyrase, EC 3.6.1.5) in Trichomonas vaginalis were determined. The enzyme hydrolyses purine and pyrimidine nucleoside 5'-di- and 5'-triphosphates in an optimum pH range of 6.0--8.0. It is Ca(2+)-dependent and is insensitive to classical ATPase inhibitors, such as ouabain (1 mM), N-ethylmaleimide (0.1 mM), orthovanadate (0.1 mM) and sodium azide (5 mM). A significant inhibition of ADP hydrolysis (37%) was observed in the presence of 20 mM sodium azide, an inhibitor of ATP diphosphohydrolase. Levamisole, a specific inhibitor of alkaline phosphatase, and P(1), P(5)-di (adenosine 5'-) pentaphosphate, a specific inhibitor of adenylate kinase, did not inhibit the enzyme activity. The enzyme has apparent K(m) (Michaelis Constant) values of 49.2+/-2.8 and 49.9+/-10.4 microM and V(max) (maximum velocity) values of 49.4+/-7.1 and 48.3+/-6.9 nmol of inorganic phosphate x min(-1) x mg of protein(-1) for ATP and ADP, respectively. The parallel behaviour of ATPase and ADPase activities and the competition plot suggest that ATP and ADP hydrolysis occur at the same active site. The presence of an ATP diphosphohydrolase activity in T. vaginalis may be important for the modulation of nucleotide concentration in the extracellular space, protecting the parasite from the cytolytic effects of the nucleotides, mainly ATP.

Adenosine Diphosphate↗
PubMed2000

Direct interaction of Na-azide with the KATP channel.

1. The effects of the metabolic inhibitor sodium azide were tested on excised macropatches from Xenopus oocytes expressing cloned ATP-sensitive potassium (KATP) channels of the Kir6.2/SUR1 type. 2. In inside-out patches from oocytes expressing Kir6.2 delta C36 (a truncated form of Kir6.2 that expresses in the absence of SUR), intracellular Na-azide inhibited macroscopic currents with an IC50 of 11 mM. The inhibitory effect of Na-azide was mimicked by the same concentration of NaCl, but not by sucrose. 3. Na-azide and NaCl blocked Kir6.2/SUR1 currents with IC50 of 36 mM and 19 mM, respectively. Inhibition was abolished in the absence of intracellular Mg2+. In contrast, Kir6.2 delta C36 currents were inhibited by Na-azide both in the presence or absence of intracellular Mg2+. 4. Kir6.2/SUR1 currents were less sensitive to 3 mM Na-azide in the presence of MgATP. This apparent reduction in sensitivity is caused by a small activatory effect of Na-azide conferred by SUR. 5. We conclude that, in addition to its well-established inhibitory effect on cellular metabolism, which leads to activation of KATP channels in intact cells, intracellular Na-azide has direct effects on the KATP channel. Inhibition is intrinsic to Kir6.2, is mediated by Na+, and is modulated by SUR. There is also a small, ATP-dependent, stimulatory effect of Na-azide mediated by the SUR subunit. The direct effects of 3 mM Na-azide on KATP channels are negligible in comparison to the metabolic activation produced by the same Na-azide concentration.

Adenosine Triphosphate↗
PubMed1993

Iminium salt of copper benzochlorin (CDS1), a novel photosensitizer for photodynamic therapy: mechanism of cell killing.

The mechanism of cell killing by CDS1, an iminium salt of octaethylbenzochlorin with copper in the aromatic ring, in combination with light from a noncoherent light source was investigated. Using a standard clonogenic assay and the AY-27 FANFT tumor line, photoactivation of CDS1 was shown to be cytotoxic. The photodynamic cell killing ability of CDS1 required the presence of molecular oxygen. The reactive species generated by light activation of CDS1 were effectively quenched by N,N'-diphenyl-p-phenylenediamine. Additionally, the photodynamic effect of CDS1 was not enhanced by deuterium oxide. To characterize the reactive oxygen species generated by the photoactivation of CDS1 the well-characterized erythrocyte ghost model was used. Superoxide dismutase and catalase were potent inhibitors of CDS1-induced lipid peroxidation of erythrocyte membranes. Sodium azide only partially inhibited lipid peroxidation. These findings differed from the known singlet oxygen generator, tin (II) etiopurpurin dichloride (SnET2). Sodium azide was a potent inhibitor of SnET2-induced lipid peroxidation, whereas superoxide dismutase and catalase were totally ineffective. Based on these results, we conclude that CDS1 requires the presence of molecular oxygen for cell killing to occur but appears to act primarily through a non-singlet oxygen mechanism.

Animals↗
PubMed1988

Microcalorimetric studies of hybridoma cells.

In the present study, overall metabolism has been estimated in hybridoma cells by microcalorimetric measurement. Heat production rate was found to be 30-50 pW/cell at cell concentrations 0.65-4.5 x 10(5)/ml. High cell concentrations (1 x 10(6) cells/ml) caused unstable power-curves with an initial high peak and a rapid declining phase, whereas low cell concentrations (0.6-4.5 x 10(5) cells/ml) produced steady-state power-curves. Oxygen consumption was found to range between 1.5-6.1 x 10(-5) mol 02/cell/min, corresponding to about 80% of the total metabolic activity. The metabolic inhibitors sodium fluoride (50 nM), sodium azide (160 mM) and rotenone (0.1 mM) caused a reduction in overall cell metabolism of 60, 55 and 40% respectively.

Aerobiosis↗
PubMed1984

Cellular pathways of galactose-terminal ligand movement in a cloned human hepatoma cell line.

The intracellular pathways taken by galactose-terminal glycoproteins were examined following endocytosis by the asialoglycoprotein receptor in monolayers of the human hepatoma cell line, Hep G2. In addition to a pathway leading to lysosomal degradation, single cohort kinetics revealed that up to 28% of surface-bound and internalized 125I-asialoorosomucoid (ASOR) eventually returned undegraded to the extracellular medium over 6 hr in the presence or absence of free ASOR in the exocytosis medium. This reappearance of ligand in the exocytosis medium represented a constant fraction of surface bound and internalized 125I-ASOR, and followed pseudo-first order kinetics with t1/2 = 84 min (long transit pool). Under conditions of enhanced ligand-receptor dissociation (incubation with 100 mM N-acetylgalactosamine (GalNAc), at least 50% of initially internalized 125I-ASOR returned to the cell surface as ligand-receptor complexes, followed by dissociation of free ligand into the exocytosis medium. This rapid transit pool of ligand also displayed pseudo-first order kinetics with t1/2 = 24 min. Exocytosis of 125I-Gal-cytochrome c, a synthesized ligand displaying rapid dissociation from the asialoglycoprotein receptor (ASGP-R), paralleled the kinetics of the rapid transit pool of 125I-ASOR (t1/2 = 28 min). Furthermore, in addition to spontaneous dissociation from ASPG-R following return to the cell surface, studies conducted in saponin-permeabilized monolayers support the return of free intracellular 125I-Gal-cytochrome c to the cell surface during exocytosis. The rapid transit pool of ligand was insensitive to inhibition by 10 mM sodium azide or 0.1 mM primaquine. In contrast, the long transit pool destined for exocytosis was inhibited 50% by 10 mM sodium azide, but insensitive to inhibition by 0.1 mM primaquine. These data suggest that, following internalization by the ASGP-R, a major pathway of ligand movement includes the rapid return of ligand-receptor complexes and/or free ligand to the cell surface. Return of ligand-receptor complexes or free ligand to the cell surface occurs prior to an acidic sorting compartment, can involve multiple cycles of return to the cell surface, and may involve passage through other nonlysosomal intracellular organelles.

Asialoglycoprotein Receptor↗
PubMed1976

Effect of some inhibitors on kanamycin formation by Streptomyces kanamyceticus.

The formation of kanamycin is markedly inhibited by mercuric chloride, sodium iodoacetate, 2,4-dinitrophenol, sodium arsenite and sodium azide particularly when these are added at the start of fermentation. Less inhibition of kanamycin synthesis is observed in case of sodium 5,5-diethylbarbiturate, malonic acid, sodium arsenate and sodium fluoride. Inhibition of kanamycin synthesis is associated with growth inhibition in case of 2,4-dinitrophenol, sodium arsenite and sodium azide. Bacitracin and D-cycloserine have a stimulatory effect on kanamycin synthesis with slight inhibition of cellular growth. This stimulation might be due to accumulation of cell wallintermediates--aminosugar and sugar--which are shunted to the pathway of kanamycin synthesis. Penicillin lowers kanamycin synthesis by 65 percent as compared with 19 percent reduction of cellular growth. Chloramphenicol has a stimulatory effect at lower concentration (20 mug/ml), when it is added at 24 h of fermentation. At higher concentration (50 mug/ml) chloramphenicol shows marked inhibition of both cellular growth and antibiotic biosynthesis.

Arsenic↗
PubMed2006

Mixed guanidinato/alkylimido/azido tungsten(VI) complexes: synthesis and structural characterization.

A series of structurally characterized new examples of pentacoordinated heteroleptic tungsten(VI)-guanidinates complexes are described. Starting out from [WCl(2)(Nt-Bu)(2)py(2)] (1) (py = pyridine) and the guanidinato transfer reagents (TMEDA)Li[(Ni-Pr)(2)CNi-Pr(2)] (2a) (TMEDA = N,N,N',N'-tetramethylethylendiamine) and [Li(NC(NMe(2))(2))](x) (2b), the title compounds [WCl(Nt-Bu)(2)[(Ni-Pr)(2)CNi-Pr(2)]] (3) and [W(Nt-Bu)(2)Cl{NC(NMe(2))(2)]](2) (6) were selectively formed by the elimination of one mole equivalent of lithium chloride. The isopropyl-substituted guanidinato ligand [(Ni-Pr)(2)CNi-Pr(2)} of monomeric 3 is N(1),N(3)-bonded to the tungsten center. The introduction of the sterically less-demanding tetramethyl guanidinato ligand [NC(NMe(2))(2)] expectedly leads to dimeric 6 exhibiting a planar W(2)N(2) ring with the guanidinato group bridging the two tungsten centers via the deprotonated imino N-atom. The remaining chloro ligand of 3 is labile and can be substituted by sterically less-crowded groups such as dimethylamido or azido that yield the presumably monomeric compounds 4 and 5, respectively. A similar treatment of 6 with sodium azide yields the dimeric azido derivative 7. Reacting [WCl(2)(Nt-Bu)(2)py(2)] directly with an excess of sodium azide leads to the dimeric bis-azide species [[W(Nt-Bu)(2)(N(3))(mu(2)-N(3))py](2)]. The new compounds were fully characterized by single-crystal X-ray diffractometry (except 2, 4, and 5), NMR, IR, and mass-spectroscopy as well as elemental analysis. Compound 5, [W(N(3))(Nt-Bu)(2)[(Ni-Pr)(2)CNi-Pr(2)]], can be sublimed at 80 degrees C, 1 Pa.

Journal Article↗
PubMed2005

Photosensitizing properties of 6-methoxy-2-naphthylacetic acid, the major metabolite of the phototoxic non-steroidal anti-inflammatory and analgesic drug nabumetone.

The photobiological properties of 6-methoxy-2-naphthylacetic acid (6-MNAA) were studied using a variety of in vitro phototoxicity assays: photohemolysis, photoperoxidation of linoleic acid, photosensitized degradation of histidine and thymine and the Candida phototoxicity test. 6-MNAA was phototoxic in vitro. 6-MNAA reduced nitro blue tetrazolium (NBT) when irradiated with lambda > or = 300 nm in deoxygenated aqueous buffer solution (pH 7.4). NBT can be reduced by reaction with the excited state of 6-MNAA subject to interference with molecular oxygen. The photohemolysis rate was inhibited by the presence of 1,4-diazabicyclo[2.2.2]octane (DABCO), sodium azide (NaN3) and reduced glutathione (GSH). Photoperoxidation of linoleic acid and photosensitized degradation of histidine and thymine were significantly inhibited by sodium azide and reduced glutathione. 6-MNAA was phototoxic to C. albicans, C. lipolytica and C. tropicalis. A mechanism involving singlet oxygen, radicals, and electron transfer reactions is suggested for the observed phototoxicity.

Aerobiosis↗
PubMed2001

[Synthesis of phosphoramide mustard analogues belonging to the L-sugar series].

During the past decades numerous cyclophoshamide (mustard) derivatives of nucleosides and aminodeoxy sugars have been prepared for investigating their antitumor activities. The cyclophosphamide analogues of aminotrideoxy hexoses belonging to the D-series of sugars have been prepared by Monneret et al. The present paper reports the synthesis of the new phosphoramide mustards 16-17 from 12 and 15 (belonging to the L-sugar series). First compound 10 was synthesized from the L-rhamnose (9). Methyl 3-azido-2,3,6,-trideoxy-alpha-L-ribo-hexopyranoside (11) was obtained by the replacement of the 3-O-p-toluene-sulfonyl group of 10 with sodium azide. Methyl 3-azido-2,3,6,-trideoxy-alpha-L-arabino-hexopyranoside (14) was synthesized by rign opening of 13 with sodium azide. The corresponding amino sugars (12, 15) were obtained by catalytic hydrogenation (over palladium on carbon) of 11 and 14. Our compounds 12 and 15 were transformed into the cyclophosphamide derivatives 16a,b-17a,b upon treatment with bis(2-chloroethyl)phoshoramidic dichloride in the presence of triethylamine (36 h, r.t.). The approximately 1:1 mixtures of isomers (due to the different steric position of the P=O group) could be readily separated by chromatography. The 1H NMR assignments of compounds 16a, 16b, 17a and 17b, were based on one-dimensional selective decoupling experiments or two-dimensional chemical shift-correlated spectroscopy (COSY-60). The assignment of configuration to the isomeric phosphoramidates was based on the magnetic anisotropy of the P=O bond. The distinctly different chemical shift patterns of sugar protons observed for the two isomers allowed the unambiguous assignment of the P=O stereochemistry. The compounds 16a,b-17a,b (mixture of isomers) were tested for inhibitory activity using L1210 and HT29 cell lines.

Antineoplastic Agents, Alkylating↗
PubMed2003

ATP and ADP hydrolysis in brain membranes of zebrafish (Danio rerio).

Nucleotides, e.g. ATP and ADP, are important signaling molecules, which elicit several biological responses. The degradation of nucleotides is catalyzed by a family of enzymes called NTPDases (nucleoside triphosphate diphosphohydrolases). The present study reports the enzymatic properties of a NTPDase (CD39, apyrase, ATP diphosphohydrolase) in brain membranes of zebrafish (Danio rerio). This enzyme was cation-dependent, with a maximal rate for ATP and ADP hydrolysis in a pH range of 7.5-8.0 in the presence of Ca(2+) (5 mM). The enzyme displayed a maximal activity for ATP and ADP hydrolysis at 37 degrees C. It was able to hydrolyze purine and pyrimidine nucleosides 5'-di and triphosphates, being insensitive to classical ATPase inhibitors, such as ouabain (1 mM), N-ethylmaleimide (0.1 mM), orthovanadate (0.1 mM) and sodium azide (0.1 mM). A significant inhibition of ATP and ADP hydrolysis (68% and 34%, respectively) was observed in the presence of 20 mM sodium azide, used as a possible inhibitor of ATP diphosphohydrolase. Levamisole (1 mM) and tetramisole (1 mM), specific inhibitors of alkaline phosphatase and P1, P(5)-di (adenosine 5'-) pentaphosphate, an inhibitor of adenylate kinase did not alter the enzyme activity. The presence of a NTPDase in brain membranes of zebrafish may be important for the modulation of nucleotide and nucleoside levels, controlling their actions on specific purinoceptors in central nervous system of this specie.

Acid Anhydride Hydrolases↗
PubMed1998

Characterization of laccases and peroxidases from wood-rotting fungi (family Coprinaceae).

Panaeolus sphinctrinus, Panaeolus papilionaceus, and Coprinus friesii are described as producers of ligninolytic enzymes. P. papilionaceus and P. sphinctrinus both produced a laccase. In addition, P. sphinctrinus produced a manganese peroxidase. C. friesii secreted a laccase and two peroxidases similar to the peroxidase of Coprinus cinereus. The purified laccases and peroxidases were characterized by broad substrate specificities, significant enzyme activities at alkaline pH values, and remarkably high pH optima. The two peroxidases of C. friesii remained active at pH 7.0 and 60 degrees C for up to 60 min of incubation. The peroxidases were inhibited by sodium azide and ethylene glycol-bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA), whereas the laccases were inhibited by sodium azide and N,N-diethyldithiocarbamic acid. As determined by native polyacrylamide gel electrophoresis and isoelectric focusing, all three fungi produced laccase isoenzymes.

Amino Acid Sequence↗
PubMed1975

Pediococcus cerevisiae mutant with altered transport of folates.

A Pediococcus cerevisiae mutant that actively accumulated folate (PteGlu), in contrast to the wild-type, was also found to exhibit changes in the pattern of uptake of 5-methyl-tetrahydrofolate (5-CH3-H4PteGlu) and amethopterin. Most of the 5-CH3-H4PteGlue accumulated through a glucose- and temperature-dependent process, and a concentrative uptake was also found in gluocse-starved cells and in cells incubated at OC. About 75% of the accumulated 5-CH3-H4PteGlu exchanged with amethopterin. In contrast to the wild type, the mutant accumulated both diastereoisomers of 5-CH3-H4PteGlue by glucose-dependent and glucose-independent processes. Amethopterin and PteGlue competitively inhibited the uptake in both processes, with an apparent lower affinity of the carrier for PteGlu than for the analogue. p-Chloromercuribenzoate strongly inhibited the uptake (75%). The p-chloromercuribenzoate-nonsusceptible and temperature-independent uptake was also competed by amethopterin. Metabolic poisons like sodium azide, potassium fluoride, iodoacetate, and 2,4-dimitrophenol inhibited the glucose-dependent process. Uptake, in the absence of glucose, was enhanced by sodium azide and potassium fluoride.

Azides↗
PubMed1993

Fluence-rate-dependent photosensitized oxidation of NADH.

The photosensitizing activity of dimethoxyhaematoporphyrin, excited by a laser pulse at 532 nm (YAG-Nd3+), was investigated using reduced nicotinamide adenine dinucleotide (NADH) as a substrate. The photo-oxidative modification of NADH was monitored by measuring the absorbance at 340 nm. The use of nanosecond pulses (15 and 0.5 ns) resulted in photosensitized NADH oxidation which depended on the fluence but not on the fluence rate up to a peak fluence rate of 10(7) W cm-2. At higher fluence rates a decrease in NADH photo-oxidation was observed, as well as on irradiation with picosecond pulses (35 ps). Stern-Volmer assay of the quenching by sodium azide revealed a decrease in quenching efficiency with increasing peak fluence rate. Oxidation of NADH was not suppressed by the addition of 20 mM sodium azide at peak fluence rates above 6 x 10(9) W cm-2. This observation, as well as the significant bleaching of dye absorption, indicates excitation of the photosensitizer into higher lying excited singlet states and the involvement of processes other than photodynamic action.

Hematoporphyrin Derivative↗