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PubMed1980

Role of oxygen in antibody-dependent cytotoxicity mediated by monocytes and neutrophils.

The antibody-dependent cell-mediated cytoxicity (ADCC) by human monocytes and neutrophils was investigated by measuring the release of 51chromate from prelabeled erythrocytes coated with immunoglobulin G. ADCC was found to be positively correlated to phagocytosis of 51Cr-labeled erythrocytes and to the postphagocytic events of the effector cells, activation of the hexose monophosphate shunt, and degranulation. Exclusion of oxygen from the incubation media halved the ADCC by both cell types without affectijg phagocytosis or degranulation. Likewise, ADCC by cells from patients suffering from chronic granulomatous disease (CGD) was only half the intensity of ADCC by cells from normals. Inhibitors of mitochondrial respiration were without depressing effect of ADCC. Azide, which in addition to its blocking action on oxydative phosphorylation also inhibits catalase and myeloperoxidase, resulted in a approximately equal to 40% stimulation of ADCC by cells from normals but was without effect of ADCC by cells from CGD patients. The hydroxyl radical scavenger, mannitol, significantly depressed ADCC by cells from normals (P < 0.01) but was without effect on cells from CGD patients. Azide and mannitol also were without effect on ADCC by normal cells when oxygen was excluded. In a xanthine-xanthine oxidase system, erythrocytes were effectively lysed. This lysis was inhibited by catalase, superoxide dismutase, and mannitol. When comparable concentrations of glucose oxidase were used no lysis was observed. H2O2 either alone or in combination with azide did not lyse erythrocytes. It is suggested that ADCC by both monocytes and neutrophils is partly dependent on the generation of hydroxyl radicals by the effector cells.

Anaerobiosis↗
PubMed1993

Photografting of albumin onto dimethyldichlorosilane-coated glass.

4-Azido-2-nitrophenyl albumin (ANP-albumin) was prepared by displacing the fluoro group of 4-fluoro-3-nitrophenyl azide (FNPA) by an amino group of albumin. Photolysis of phenyl azides of ANP-albumin was studied by Fourier-transform infrared (FTIR) spectroscopy. The band of phenyl azide disappeared completely after a 12-min exposure to long wave UV light (366 nm), and the photolysis was first-order. Albumin was grafted onto dimethyldichlorosilane-coated glass (DDS-glass) by photolysis of the azido groups of ANP-albumin without any premodification of the surface. The albumin-grafted DDS-glass was characterized by determining the relative amount of nitrogen resulting from the grafted albumin on the surface using electron spectroscopy for chemical analysis (ESCA). The amount of nitrogen increased when the concentration of ANP-albumin in the adsorption solution increased up to 0.1 mg/ml. As the solution concentration increased above this value, the amount of nitrogen decreased. The platelet resistance of the albumin-grafted surfaces was evaluated by measuring the number of adherent platelets and the extent of activation that was quantitated by the area of platelets spread on the surfaces. The maximum platelet-resistant effect was observed when the ANP-albumin was adsorbed for more than 50 min at the solution concentration ranging from 0.05 to 10 mg/ml.

Adsorption↗
PubMed1979

Co-operativity of lectin binding to fibroblasts and its relation to cellular actomyosin.

We have investigated the binding of 125I-concanavalin A (125I-Con A) and 125I-succinyl concanavalin A (125I-s-Con A) to rat fibroblasts (16C line) as a function of the concentration of added lectin, and the alterations to this binding behaviour caused by drugs which modify the cytoskeleton. The changes in cell behaviour which occur at different levels of binding have also been studied. As shown previously for some other systems, the binding of Con A is complex and partly co-operative. Three phases can be distinguished in our system: (i) pre-nucleation binding, (ii) binding which shows a small positive slope in a Scatchard plot and a Hill coefficient greater than unity, and which therefore is incipiently co-operative, and (iii) post-co-operative binding. The co-operative phase of binding is paralleled by progressive inhibition of EGTA-mediated cell detachment from substrata, with inhibition being complete when this phase of binding is complete. Likewise, the phagocytosis of latex spheres is progressively inhibited up to a threshold which coincides with the completion of co-operative binding. Thirdly, cells pretreated with Con A round up with colchicine (10(-5) M) if co-operative finding is complete, but adopt broad epithelial shapes if it is not. s-Con A does not show cooperative binding, and correspondingly does not inhibit EGTA-mediated cell detachment, or show a distinct threshold in the inhibition of phagocytosis, or promote the 2 types of shape change with colchicine. The pattern of Con A binding is drastically altered by pretreatment of cells with cytochalasin B or azide. The Scatchard and Hill plots show that the co-operative phase remains and is complete at about the same level of binding, but that it is more readily nucleated and takes place against a changed number and/or distribution of receptors. Pretreatment of cells with colchicine causes changes in the pattern of binding which are different from those observed with cytochalasin B or azide and are more difficult to interpret. We conclude that a reciprocal relationship exists between the cellular actomyosin and the state of cell surface receptors. Perturbation of actomyosin by cytochalasin B or azide can enhance the freedom of some receptors to participate in a co-operative rearrangement which facilitates the binding of further molecules of lectin. Vice versa, the co-operative event has a feedback influence on the cellular actomyosin to cause alterations of cellular response.

Actomyosin↗
PubMed1994

Oxygen radical formation in well-washed rat liver microsomes: spin trapping studies.

The generation of hydroxyl radicals by rat liver microsomes was monitored by spin trapping with 5,5-dimethylpyrroline N-oxide (DMPO). The results confirm and extend previous data which demonstrated that hydroxyl radicals are produced by microsomes in the presence of NADPH and O2, and without the exogenous addition of iron. No EPR signals could be detected unless catalase activity which was associated with the microsomes could be substantially diminished. Addition of azide was the most effective means of eliminating catalase activity, but azide also reacted rapidly with hydroxyl radicals, forming azidyl radicals which were in turn trapped by DMPO. Extensive washing and preincubation of microsomes with 3-amino-1,2,4-triazole in the presence of H2O2 were evaluated as alternative methods of decreasing the catalase contamination of microsomes. Although neither method completely eliminated microsomal catalase activity, addition of azide was no longer necessary for hydroxyl radical detection with DMPO. When highly washed microsomal preparations were tested, weak signals of the superoxide radical adduct of DMPO could also be detected. These data indicate that the sensitivity of spin trapping in microsomal systems can be improved substantially when care is taken to eliminate cytosolic contaminants such as catalase.

Animals↗
PubMed2006

High level expression of a protein precursor for functional studies.

In vitro analyses of type I signal peptidase activities require protein precursors as substrates. Usually, these pre-proteins are expressed in vitro and cleavage of the signal sequence is followed by SDS polyacrylamide gel electrophoresis coupled with autoradiography. Radioactive amino acids have to be incorporated in the expressed protein, since the amount of the in vitro expressed protein is usually very low and processing of the signal peptide cannot be followed by SDS polyacrylamide gel electrophoresis alone. Here we describe a rapid and simple method to express large amounts of a protein precursor in E. coli. We have analyzed the effect of ionophors as well as of azide on the accumulation of expressed protein precursors. Azide blocks the function of SecA and the ionophors dissipate the electrochemical gradient across the cytoplasmic membrane of E. coli. Addition of azide ions resulted in the formation of inclusion bodies, highly enriched with pre-apo-plastocyanine. Plastocyanine is a soluble copper protein, which can be found in the periplasmic space of cyanobacteria as well as in the thylakoid lumen of cyanobacteria and chloroplasts, and the pre-protein contains a cleavable signal sequence at its N-terminus. After purification of cyanobacterial preapo-plastocyanine, its signal sequence can be cleaved off by the E. coli signal peptidase, and protein processing was followed on Coomassie stained SDS polyacrylamide gels. We are optimistic that the presented method can be further developed and applied.

Amino Acid Sequence↗
PubMedDate not supplied

Effects of anoxia and metabolic inhibitors on reaction of the fast sodium system.

The effects of anoxia and metabolic inhibitors on inactivation and reactivation of the fast Na system of dog ventricular muscle fibers were studied by examining (dV/dt)max of the action potential upstroke. Anoxia for 60 min, dinitrophenol (DNP) (2.0 mM), and sodium azide (2.0 mM) depressed markedly steady-state (dV/dt)max at each membrane potential produced by changing [K]o. Anoxia tended to prolong recovery slightly, but DNP and azide changed little the time course of recovery of the (dV/dt)max, which was studied by applying double pulses to elicit action potential at different intervals. It is concluded that anoxia, DNP, and azide caused prominent depression of the maximum Na conductance but had less influence on its recovery kinetics.

Animals↗
PubMed1975

Transport of sugars and amino acids in bacteria. XV. Comparative studies on the effects of various energy poisons on the oxidative and phosphorylating activities and energy coupling reactions for the active transport systems for amino acids in E. coli.

The effects of various energy poisons on oxidation of respiratory substrate, synthesis of cellular ATP, and energy transformation reaction in intact Escherichia coli cells were studied systematically. Various mutants were, therefore, used in which specific functions in the energy-transducing reactions were defective or altered. The energy poisons examined were: sodium azide. DPPA and azidebenzenes which are inhibitors of respiratory-chain phosphorylation, SF6847, and CCCP which are known to be uncouplers, zinc sulfate which is an inhibitor for certain dehydrogenases, and sodium arsenate and sodium fluoride which are inhibitors of glycolytic synthesis of ATP. The preferential inhibitions occurred in the oxidation reactions with certain respiratory substrates by energy poisons used. DPPA inhibited glycerol oxidation much more strongly than succinate oxidation. However, DPPA could inhibit the oxidation of both glycerol 3-phosphate and succinate by membrane fraction strongly while the oxidation of NADH and D-lactate slightly. It inhibited glycerol 3-phosphate dehydrogenase [EC 1.1.2.1] strongly as well as succinate dehydrogenase [EC 1.3.99.1],.but not D-lactate dehydrogenase of membrane fraction. MAB and other azidebenzene derivatives inhibited succinate oxidation preferentially. SF6847 and CCCP inhibited succinate oxidation strongly, while sodium azide inhibited it weakly and these three poisons were less inhibitory for glycerol oxidation. DPPA, sodium azide, SF6847, and CCCP inhibited the synthesis of ATP coupled with respiration but not with glycolysis. Zinc sulfate inhibited the cellular ATP synthesis coupled with either respiration or glycolysis.

Adenosine Triphosphate↗
PubMed2001

Antimutagenic potential of extracts isolated from Terminalia arjuna.

Terminalia arjuna is an important medicinal plants widely used in the preparation of Ayurvedic formulations used against several ailments. The present investigation was aimed at the fractionation of crude extracts from the bark of T. arjuna in order to isolate and purify the antimutagenic factors present. The antimutagenicity assay was performed to check the modulatory effect of these fractions against NPD, sodium azide, and 2AF, using the Ames Salmonella his+ reversion assay. Most of the phenolic fractions exhibited mutagen specificity against direct-acting mutagens, being effective in suppressing the frameshift mutagen NPD but failing to inhibit sodium azide (base pair substitution)-induced his+ revertants. ET-1 fraction triterpenoid diglycoside showed a marked effect against sodium azide but was ineffective against NPD. In the case of the indirect-acting mutagen 2AF, all the fractions were found to be quite potent in modulating its mutagenicity in both TA98 and TA100 tester strains of Salmonella typhimurium. The results indicate that the bark of T. arjuna harbors constituents with promising antimutagenic/anticarcinogenic potential that should be investigated further.

Antimutagenic Agents↗
PubMed1992

Uptake of the noncytotoxic transport probe procainamide in the Chinese hamster ovary model of multidrug resistance.

Many of the cytotoxic substrates of the multidrug transporter are organic cations. Cimetidine, procainamide, and tetraethylammonium bromide were used in a Chinese hamster ovary model of multidrug resistance, to study handling of noncytotoxic cationic transport probes. Cimetidine and procainamide, but not tetraethylammonium, accumulated to a greater extent (5-fold) in the sensitive CHOAUXB1 (AB) cell line than in the resistant CHRC5 (C5) cell line. Accumulation of both cimetidine and procainamide was significantly increased by verapamil in C5 but not AB. Procainamide accumulation in both AB and C5 was temperature dependent and occurred by passive diffusion. Diltiazem, nifedipine, rifampin, tamoxifen, rhodamine, and ethidium also increased procainamide accumulation in C5 but not AB. Azide in glucose-free medium increased procainamide accumulation in C5, and this was reversed when glucose, but not 3-O-methylglucose, was added. Procainamide efflux rates were similar in AB and C5 and not affected by verapamil or azide. The initial rate of procainamide uptake was higher in AB than in C5, and both verapamil and azide increased the initial rate of procainamide uptake in C5. Thus, differences in accumulation of the noncytotoxic transport probe procainamide in the colchicine-sensitive and colchicine-resistant components of the Chinese hamster ovary cell line mimic the accumulation of known cytotoxic substrates for the multidrug transporter, such as colchicine, vinblastine, and doxorubicin. The differential accumulation of procainamide is due to differences in rates of drug influx, rather than efflux. Since procainamide influx is passive and decreased accumulation in the resistant line appears to parallel M(r) 170,000 glycoprotein presence and activity, we would speculate that decreased procainamide accumulation may be due to an indirect effect of the M(r) 170,000 glycoprotein, such as its effect on intracellular pH.

Animals↗
PubMedDate not supplied

["Oxygen regulation" of the respiratory chain composition in the yeast Debaryomyces hansenii under multiple stress].

It was shown that two stress factors, hypoxia and hyperosmotic shock, if applied simultaneously to the yeast Debaryomyces hansenii, display an antagonistic mode of interaction, which results in an increased degree of halophily of this microorganism under microaerobic conditions. Studies of the effects of respiration inhibitors (sodium azide and salicyl hydroxamic acid, SHA) and of the pattern of changes in the composition of the respiratory chain of Debaryomyces hansenii under the stated stress conditions led to the suggestion of three (or four) chains of electron transfer functioning simultaneously in the cell: the classical respiratory chain involving cytochrome-c oxidase, an alternative respiratory chain involving a cyanide- and azide-resistant oxidase, and additional respiratory chains involving oxidases resistant to salt, azide and SHA. Thus, the antagonistic mode of interaction between hypoxia and hyperosmotic shock results from the redirection of the electron flow from the salt-susceptible respiratory systems to the salt-unsusceptible ones encoded by "the hypoxia genes" and activated (induced) under microaerobic conditions.

Anaerobiosis↗
PubMed1977

Innocuity and toxicity testing of non-viral components of foot-and-mouth disease vaccines.

Some biological properties of 3 different adjuvants: saponin, DEAE-dextran and sodium azide applied in foot-and-mouth vaccines have been studied. As tested in guinea pigs, by dialysis of various batches of saponin, the author succeeded in reducing their toxicity by 80 to 90%, their hemolytic activity by 60 to 75% and their inflammatory capacity by 40 to 50%, whereas in cattle the inflammatory capacity of dialyzed saponin batches decreased by 80 to 90%. The inflammatory capacity of DEAE-dextran is about 50 to 60% less than that of the saponin. The effect of saponin and sodium azide has directly been studied in virus suspension also. Neither the saponin nor the sodium azide affected adversely the infectivity and immunogenicity of the antigen. The loss of potency due to the storage of the vaccine is not in relationship with the presence of the two above-named components.

Adjuvants, Immunologic↗
PubMed1977

[Copper and nervous system. An experimental study (author's transl)].

Sodium azide is known to produce alterations in mammalian copper proteins, thus rendering them unable to bind exogenous metal, which remains in the "labile pool" condition. Continuous administration of sodium azide at LD50 for 30 days causes copper accumulation in several tissues and even in the nervous system, with characteristic changes in neurones and glial cells, very much resembling the alterations observed in Wilson's disease. Dietary copper administration, on the contrary, though raising the level of tissue-bound metal, does not produce cellular damage. These findings allow us to suppose that sodium azide may alterate the coppper chelating proteins in the tissues, especially in the nervous system, thus causing the storage of cell-toxic "labile pool" metal. The pathogenesis of Wilson's disease and the problem of "pathoclisis" in the nervous system are debated.

Animals↗
PubMed1989

Axial coordination of ferric Aplysia myoglobin.

Resonance Raman spectra of ferric Aplysia myoglobin in the ligand-free and the azide-bound forms have been studied over a wide pH range to determine the coordination states of the heme iron atom. In the hydroxide form at high pH (approximately 9) the iron is six-coordinate and is in a high/low spin equilibrium. As the pH is lowered below the acid/alkaline transition (pKa = 7.5), the heme becomes five-coordinate. When the pH is lowered even further no other changes in the resonance Raman spectrum are detected; thus, the heme remains five-coordinate down to pH 4, the lowest value studied. For ferric azide-bound Aplysia myoglobin, the iron is six-coordinate in a high/low spin equilibrium at all pH values (4.8-9). These data indicate (i) that the unusual reactivity toward azide previously observed at neutral pH is indeed related to the absence of a coordinated water molecule, and (ii) that causes other than the heme coordination are responsible for the spectral differences and the ligand-binding kinetics differences observed below pH 6.

Animals↗
PubMed1979

The effect of age in culture on the uptake and metabolism of methotrexate by primary cultures of hepatocytes.

Primary monolayer cultures of rat hepatocytes show an initial transient azide-sensitive capacity to concentrate methotrexate several-fold from the medium. However, after 48 h in culture they lose the azide-sensitive ability to accumulate methotrexate. The uptake of (+) 5-methyltetrahydrofolate and folate is not altered greatly with time in culture and is unaffected by azide. Once inside the cell, methotrexate is converted predominantly to di- and triglutamate derivatives. After a short exposure to methotrexate (up to 4 h) most of the intracellular methotrexate is unaltered, but by 24 h nearly 80% is present as polyglutamates. Unlike the capacity of the cells to accumulate methotrexate, the ability of the cells to form polyglutamates does not appear to diminish with the age of the culture.

Animals↗
PubMed1978

Photoreactive probes for high resolution mapping of membrane proteins.

The preparation and characterization of a novel series of radioactively labeled membrane probes is described. These probes are carbohydrate derivatives of fatty acids which contain a photosensitive azide moiety at a specified distance along the alkyl chain. The function of the carbohydrate group is to restrict the azide function to the outer surface monolayer of sealed membrane systems. The azide probes have been used in several well-characterized membrane systems including erythrocyte ghosts, membrane-enveloped viruses, and artificial vesicles. Upon activation, the probes attach to integral proteins to form a stable, covalent complex which may be extracted and identified. The activation protocol is outlined and some of the preliminary results are discussed.

Azides↗
PubMed1981

Antigenic modulation of lymphocytic surface immunoglobulin yielding resistance to complement-mediated lysis. II. Relationship to redistribution of the antigen.

Experiments were carried out on guinea-pig L2C leukaemic lymphocytes to investigate the mechanism of antigenic modulation of their surface immunoglobulin (Ig) defined as the conferring by anti-Ig of resistance to lysis by anti-Ig plus complement. The phenomenon reflects, and is probably a consequence of, redistribution of the Ig molecules by bivalent antibody. Fab fragments of the antibody were completely ineffective. Parallel studies by indirect immunofluorescence of the movement of th surface antigen-antibody complexes revealed that modulation for syngeneic complement was apparent when the complexes were minimally aggregated: capping and extensive endocytosis were not necessary. Modulation for xenogeneic (rabbit) complement required more extensive movement but was still appreciable while complexes persisted on the surface. Sodium azide at 10 mM, which inhibits antibody-induced redistribution of surface molecules, diminished modulation. In experiments omitting pre-incubation with antibody alone, the presence of azide during incubations with anti-Ig plus syngeneic complement increased lysis from a low and variable to a consistently high level; there was no effect on the already high level of lysis occurring with the non-modulating anti-Ia plus syngeneic complement. This effect of azide provides further evidence that antigenic modulation can be a major factor determining a cell's survival when it is confronted simultaneously by antibody and complement.

Animals↗
PubMed1999

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes.

Quasi-elastic light scattering (QELS), electrophoretic light scattering (ELS), CD spectroscopy, and azide binding titrations were used to study the complexation at pH 6.8 between ferrihemoglobin and three polyelectrolytes that varied in charge density and sign. Both QELS and ELS show that the structure of the soluble complex formed between ferrihemoglobin and poly(diallyldimethylammonium chloride) [PDADMAC] varies with protein concentration. At fixed 1.0 mg/mL polyelectrolyte concentration, protein addition increases complex size and decreases complex mobility in a tightly correlated manner. At 1.0 mg/mL of greater protein concentration, a stable complex is formed between one polyelectrolyte chain and many protein molecules (i.e., an intrapolymer complex) with apparent diameter approximately 2.5 times that of the protein-free polyelectrolyte. Under conditions of excess polyelectrolyte, each of the three ferrihemoglobin-polyelectrolyte solutions exhibits a single diffusion mode in QELS, which indicates that all protein molecules are complexed. CD spectra suggest little or no structural disruption of ferrihemoglobin upon complexation. Azide binding to the ferrihemoglobin-poly(2-acrylamide-2-methylpropanesulfonate) [PAMPS] complex is substantially altered relative to the polyelectrolyte-free protein, but minimal change in induced by complexation with an AMPS-based copolymer of reduced linear charge density. The change in azide binding induced by PDADMAC is intermediate between that of PAMPS and its copolymer.

Animals↗
PubMed1989

The lipoxygenase pathway and chemiluminescence in horse eosinophilic leukocytes.

It was shown in several cell types that the dual lipoxygenase and cyclooxygenase inhibitor eicosatetraynoic acid but not the cyclooxygenase inhibitor acetylsalicylic acid suppressed luminol-dependent chemiluminescence. Since lipoxygenase is known to generate chemiluminescence in vitro, these observations were interpreted as evidence for a direct contribution of the lipoxygenase pathway to light emission in intact cells. We have investigated a possible contribution of the lipoxygenase to the chemiluminescence of horse eosinophils by directly comparing the formation of the byproduct chemiluminescence with the formation of stable end-products of the lipoxygenase pathway, leukotrienes and HETEs. Azide as well as eicosatetraynoic acid almost completely inhibited chemiluminescence stimulated by the calcium ionophore A23187 but had less effect on the formation of leukotrienes. The tumour-promoting ester, phorbol myristate acetate, stimulated chemiluminescence in an azide- and eicosatetraynoic acid-sensitive manner and failed to evoke the production of leukotrienes. Azide, but also eicosatetraynoic acid inhibited the luminol-dependent chemiluminescence generated by isolated eosinophil peroxidase in the presence of H2O2. Our results argue against a direct role of the lipoxygenase pathway in the generation of light in horse eosinophilic leukocytes but do not exclude that product(s) of this pathway may be involved in stimulus-response coupling.

Animals↗