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PubMed1989

Involvement of ATP-dependent aminophospholipid translocation in maintaining phospholipid asymmetry in diamide-treated human erythrocytes.

Crosslinking of membrane skeletal proteins such as spectrin by oxidation of their SH-groups can be provoked by treatment of intact erythrocytes with diamide. Shortly after exposure of human erythrocytes to diamide and despite the transverse destabilization of the lipid bilayer that was observed in these cells (Franck, P.F.H., Op den Kamp, J.A.F., Roelofsen, B. and Van Deenen, L.L.M. (1986) Biochim. Biophys. Acta 857, 127-130), no abnormalities could be detected regarding the asymmetric distribution of the phospholipids when probed by either the prothrombinase assay or brief exposure of the cells to a modified phospholipase A2 with enhanced membrane penetrating capacity. This asymmetry appeared to undergo dramatic changes however, when the ATP content of the cytosol had decreased to less than 10% of its original level during prolonged incubation of the treated cells. These observations indicate that the initial maintenance of phospholipid asymmetry in diamide-treated erythrocytes can be solely ascribed to the action of the ATP-dependent aminophospholipid translocase. This view is supported by experiments involving radiolabeled phospholipids of which trace amounts had been inserted into the outer membrane leaflet of diamide-treated red cells and which still showed a preferential translocation of both aminophospholipids in favour of the inner monolayer, be it that the efficiency of the translocase was found to be impaired when compared to control cells.

Adenosine Triphosphate↗
PubMed1981

Diamide, temperature and spontaneous transmitter release at the neuromuscular junction: stimulation of exocytosis by a direct effect on membrane fusion?

The thiol-oxidizing agent diamide markedly increases m.e.p.p. frequency at the frog neuromuscular junction, even at low [Ca2+]0 and also when the mitochondria are uncoupled with DNP. The effect is reversed by dithioerythritol and is very temperature-sensitive, with a marked transition at 16 degrees C; m.e.p.p. frequency is raised 2- to 5-fold at 13-15 degrees C and 55- to 60-fold at 17-20 degrees C. Diamide increases the frequency of large amplitude m.e.p.p.s, the effect being explicable as the fusion of two or more vesicles. It is concluded that (a) diamide does not act at the Ca2+ channels of the plasma membrane, nor at the mitochondria. It affects the release system directly via an alteration of membrane protein --SH groups; (b) the eventual decline in m.e.p.p. frequency after DNP treatment is because of the exhaustion of mitochondrial Ca2+ rather than a depletion of quanta; (c) the major effect of temperature is on the release mechanism, perhaps via a phase-change in the phospholipoproteins of the plasmalemma or vesicles, rather than an elevation of [Ca2+]i; (d) either diamide or temperatures above 16 degrees C make Ca2+ more effective in promoting vesicle-plasmalemma fusion.

Action Potentials↗
PubMed1988

Diamide alters membrane Na+ and K+ conductances and increases internal resistance in the isolated rat lens.

The voltage and conductance of the isolated rat lens were measured using a two-internal-microelectrode technique and the potassium permeability was calculated by applying Goldman theory to 86Rb efflux data. The SH oxidizing agent diamide induces a multiphasic response in lens voltage, conductance and potassium permeability. The initial response (less than or equal to 30 min) to 1 mM diamide consists of a small depolarization (approximately 10 mV) of membrane potential accompanied by a significant decrease in conductance. The 86Rb efflux and permeability data also show an initial decrease. As this initial response is abolished by TEA (20 mM) it is probably due to an inactivation of voltage-sensitive potassium channels. After 30 min exposure to 1 mM diamide both the electrical conductance and the rate of depolarization increase. The 86Rb permeability also increases. Since the conductance increase is abolished by replacing Na+ by methyl glucamine and as it is reduced by amiloride (10(-4) M) the second phase is probably due to the activation of nonspecific cation channels. The third phase is only apparent after prolonged (approximately 12 hr) incubation in 1 mM diamide and consists of a marked increase in the bulk resistance component of the lens impedance. It is suggested that this component arises from an increase in the resistance of the fibre cell gap junctions. This cellular uncoupling may be due to calcium entering the lens through the nonspecific cation channels.

Amiloride↗
PubMed1991

Diamide induces reversible changes in morphology, cytoskeleton and cell-cell coupling in lens epithelial cells.

The isolated frog lens epithelium can be maintained with its cell shape, cytoskeletal organization and membrane electrophysiological characteristics intact for more than 24 hr. Perifusion with the permeant oxidant diamide (1 mM) led to drastic, but reversible, changes in all the above parameters. After a 20 min exposure to diamide, the regular polygonal arrangement of the epithelial cells become increasingly disrupted as the cells reorganized and a 'rosette' pattern formed. The cells at the edges of the rosette pulled apart from one another while those in the centre maintained a relatively normal appearance. Blebs formed on the apical surface of all of the cells on prolonged exposure and the internal structure was also found to be severely disrupted. The cytoplasm became granular, vacuolated and the nucleus had a banded, non-homogeneous appearance. Phalloidin staining of F-actin microfilaments revealed that there was a general disruption of organization, with actin losing its association with the membrane. The microtubule array, organized around the centrosome, was also severely disrupted although microtubules were still discernible in most cells. During exposure to diamide the membrane potential depolarized and both electrical and dye coupling, which are normally extremely efficient in these cells, were disturbed. If the epithelium was exposed to 1 mM diamide for more than 45 min then all of the above changes were irreversible and cell death followed. If exposure was restricted to less than 30 min, then all of the above changes occurred and, in fact, progressed for over 1 hr; but if the epithelium was perifused for a further 20 hr in control medium, then most of the changes were reversible.

Actin Cytoskeleton↗
PubMed1985

Diamide blocks H+ conductance in mitochondrial H+-ATPase by oxidizing FB dithiol.

Effects of diamide on proton conductance of electron transport particles (ETPH), purified H+-ATPase (F1-F0), F0 of the H+-ATPase from beef heart mitochondria and binding of cadmium (109Cd) to the H+-ATPase have been examined in the present paper. When ETPH and purified H+-ATPase are treated with 1 mM diamide, ATP-dependent generation of membrane potential, monitored by the absorbance change produced by the redistribution of oxonol VI, is consistently inhibited. Diamide also blocks passive H+ conductance driven by a K+ diffusion potential in the membrane sector, F0, of H+-ATPase. Furthermore, diamide treatment drastically reduces the binding of 109Cd2+ to H+-ATPase, showing competition for the FB dithiol group.

Adenosine Triphosphatases↗
PubMed1992

Involvement of calpain in diamide-induced cataract in cultured lenses.

Lenses cultured in diamide first developed outer cortical opacities followed by nuclear cataract. Lens hydration and total calcium were markedly increased by diamide. Proteolysis of crystallins were observed in nuclear cataract lenses. Calpain in the soluble fraction of lenses cultured with diamide was decreased, while calpain in the insoluble fraction was increased. Co-culture with E64d, an inhibitor of cysteine protease such as calpain, especially prevented nuclear opacities and proteolysis of crystallins, indicating that calpain was involved in cataract formation by diamide.

Animals↗
PubMed1981

Cell membrane receptor classes delimited through cap formation either with diamide or with membrane mobility agent, A2C.

Receptors on normal human peripheral blood lymphocytes can be divided into two classes by means of the capping response exhibited in the presence of the reagents, diamide or colchicine (microtubule-related) and A2C (microtubule-independent). Diamide and colchicine promote capping of concanavalin A (Con A) receptors. Diamide capping is reversible, while colchicine capping is not reversible under the conditions used. A2C does not promote the capping of Con A receptors. In contrast, diamide and colchicine do not affect the rate at which either anti-immunoglobulin (anti-Ig) or wheat germ agglutinin (WGA) receptors cap, but A2C effectively enhances cap formation for both anti-Ig and WGA receptors. The simplicity of the classification method promises to be of use in the investigation of membrane receptors.

Azo Compounds↗
PubMed1987

S-thiolation of cytoplasmic cardiac creatine kinase in heart cells treated with diamide.

Two methods for quantitation of protein S-thiolation, by isoelectric focusing or by enzyme activity, were used for studying S-thiolation of cytoplasmic cardiac creatine kinase. With these methods, creatine kinase was identified as a major S-thiolated protein in both bovine and rat heart. In rat heart cell cultures, creatine kinase became 10% S-thiolated during a 10 min incubation with 0.2 mM diamide. This enzyme became S-thiolated more slowly than other heart cell proteins and it also dethiolated more slowly. Two sequential additions of diamide at a 25 min interval caused twice as much S-thiolation after the second addition as compared to the first. This increased sensitivity to the second diamide treatment may have resulted from glutathione loss during the first addition which produced a higher GSSG-to-GSH ratio after the second treatment. The GSSG-to-GSH ratio was highest prior to the maximum S-thiolation of creatine kinase, but, in general, the time course of glutathione was similar to the S-thiolation of creatine kinase. This study demonstrates that cytoplasmic creatine kinase is S-thiolated and, therefore, inhibited during a diamide-induced oxidative stress in heart cells. Implications for regulation of cardiac metabolism during oxidative stress are discussed.

Animals↗
PubMed1990

Diamide reduces cadmium accumulation by human lung carcinoma A549 cells.

Human lung carcinoma A549-T27 cells were used to determine the effect of diamide on cadmium accumulation. Treatment of the cells with diamide decreased their cellular glutathione content to 51.6 +/- 7% of control and significantly decreased their cadmium accumulation both as a function of time and as a function of Cd2+ concentration. Verapamil also decreased cadmium accumulation. Its effect compares well in magnitude with that which resulted from diamide treatment. No additive effect was observed when the cells were simultaneously treated with diamide and verapamil. The results suggest that a change in the GSH/GSSG ratio affects cadmium uptake. Further, calcium channels may be involved in cadmium uptake by A549-T27 cells in a fashion that is dependent on sulfhydryl status.

Azo Compounds↗
PubMed1983

Stimulatory and inhibitory effects of hydrogen peroxide, diamide and vitamin K-5 on sugar transport in rat soleus muscle.

The experiments examined the stimulatory effects of H2O2, diamide and vitamin K-5 on the uptake of D-[U-14C]xylose by rat soleus muscle. All three oxidants stimulated sugar transport to the same extent, which was 30-40% of the maximal stimulatory effect of insulin (0.1 U/ml). Maximum stimulation was achieved with vitamin K-5 (0.01-0.1 mM), diamide (0.3 mM) and H2O2 (5-10 mM); at these concentrations the oxidants did not affect muscle ATP levels. Cytochalasin B (5 microM) abolished oxidant-stimulated xylose uptake. Catalase (20 U/ml) abolished the stimulatory effect of H2O2, but did not affect diamide- or vitamin K-5-stimulated transport. The ability of oxidants to stimulate sugar transport in anaerobic muscle could be demonstrated in short term (30 min) experiments, where muscle contained about 50% of its original ATP, but not after 120 min, when ATP levels were depleted. Oxidant-stimulated sugar transport was diminished and even abolished at supra-optimal oxidant concentrations; at these higher concentrations muscle ATP levels were lowered. All three oxidants inhibited the stimulatory effect of 2,4-dinitrophenol on sugar transport; this effect could be demonstrated using those oxidant concentrations which induced maximal stimulation of basal xylose uptake and which did not affect muscle ATP. It is concluded that: (1) H2O2, diamide and vitamin K-5 stimulate stereospecific sugar transport in soleus muscle by some mechanism other than lowering of ATP levels; (2) stimulation of sugar transport by oxidants is an ATP-dependent process; (3) some oxidant-sensitive sulphydryl group is critically involved in the process which activates muscle sugar transport.

Adenosine Triphosphate↗
PubMed1984

Effect of diamide administration on longevity, oxygen consumption, superoxide dismutase, catalase, inorganic peroxides and glutathione in the adult housefly, Musca domestica.

The role of glutathione as an antioxidant was examined in the adult housefly by the administration of diamide, an oxidant of glutathione. Although diamide effectively oxidized glutathione, it also stimulated the synthesis of glutathione. Diamide induced a decrease in the rate of oxygen consumption and in the activity of superoxide dismutase. Diamide increased catalase activity and the concentration of inorganic peroxides at early ages. The results suggest that oxidation of glutathione induces counterbalancing adaptive changes in the housefly.

Animals↗
PubMed1985

Effects of diamide and iodoacetamide on the expression of the glycoprotein IIb/IIIa complex on blood platelets.

We have examined the effects of two agents that alter platelet thiol-disulphide status on platelet aggregation and on the ability of platelets to bind a monoclonal antibody (M148) that is directed toward an epitope on the glycoprotein IIb/IIIa complex. The immediate effect of both diamide and iodoacetamide is to enhance aggregation but after further incubation diamide, but not iodoacetamide, inhibits platelet aggregation. Incubation of platelets with diamide, but not iodoacetamide, is accompanied by a marked increase in the amount of M148 that binds to platelets. This is presumably a reflection of an altered distribution of glycoproteins on the platelet surface. It is known that diamide, but not iodoacetamide, leads to polymerisation of cytoskeletal proteins in platelets. Thus evidence is provided that agents that interact with the cytoskeleton inhibit platelet behaviour via an effect on surface glycoproteins.

Antibodies, Monoclonal↗
PubMed2003

Identification and characterization of a diamide sensitive mutant of Mycobacterium smegmatis.

A mutant, T7, highly sensitive to oxidative stress as caused by diamide was isolated from a Mycobacterium smegmatis mc(2)155 transposon mutant library. While wild-type M. smegmatis is able to grow well on solid media supplemented with 10 mM diamide, T7 is only able to grow on solid media containing up to 1 mM diamide. This mutant is also sensitive to other thiol modifying agents such as iodoacetamide and chlorodinitrobenzene. By sequencing the genomic DNA flanking the transposon, T7 was found to be mutated in the region upstream of the homolog of M. tuberculosis Rv0274 open reading frame. Sequence analysis revealed that Rv0274 is a member of a superfamily of metalloenzymes comprising enzymes such as extradiol dioxygenases, glyoxalases, and fosfomycin resistant glutathione transferases. Cloning and epichromosomal expression of M. tuberculosis Rv0274 in the mutant resulted in complementation of the sensitivity to diamide.

Amino Acid Sequence↗
PubMed2006

Combining the enantioselectivities of L-valine diamide and permethylated beta-cyclodextrin in one gas chromatographic chiral stationary phase.

An L-valine diamide chiral selector was attached to a polysiloxane through a long hydrocarbon spacer giving rise to a chiral stationary phase (CSP), Chirasil-Val-C11. The enantioselective properties of this readily accessible diamide CSP under gas chromatographic conditions were found to be similar to that of the commercially available Chirasil-Val CSP prepared by a polymer-analogous route. A new binary CSP, Chirasil-DexVal-C11, was synthesized by means of simultaneous attachment of both the L-valine diamide and permethylated beta-cyclodextrin selectors to a polysiloxane using platinum-catalyzed hydrosilylation, thereby overcoming the immiscibility problem known for Chirasil-Val and Chirasil-Dex. This binary CSP retained both the enantioselectivity of Chirasil-Val-C11 toward alpha-amino acid derivatives and the unsurpassed enantioselectivity of Chirasil-Dex toward underivatized chiral alcohols, ketones, and hydrocarbons. Furthermore, it was shown that the presence of the cyclodextrin selector in Chirasil-Val-C11 significantly improved the enantioseparation of proline, which represented a problematic amino acid on diamide CSPs.

Alcohols↗
PubMed2000

Receptors involved in the phagocytosis of senescent and diamide-oxidized human RBCs.

BACKGROUND: Senescent RBCs bear IgG and C3 opsonins that are three to four times less than required for similar phagocytosis of experimentally opsonized RBCs. STUDY DESIGN AND METHODS: Studies were performed to determine the phagocyte receptors involved in phagocytosis in vitro. The effect of clustering of opsonins and oxidative damage in the sequestration of RBCs was studied by exposing RBCs to BS3 (bis[sulfosuccinimidyl]-suberate) and diamide (azodicarboxylic acid bis[dimethyl-amide]). RESULTS: Sequestration of senescent RBCs was inhibited by the treatment of lymphokine-activated monocytes with N-acetyl-D-galactoseamine (GalNAc), arginine-glycine-aspartic acid (RGD), or antibodies to CR3, FcgammaRI, FcgammaRII, leukocyte response integrin (LRI), and integrin-associated protein (IAP). Exposure to BS3 alone did not enhance phagocytosis. The addition of serum resulted in opsonin binding. The level of opsonization required for sequestration was higher than on senescent RBCs and was only marginally inhibited by blocking CR3, FcgammaRI and FcgammaRII. Diamide treatment alone did not lead to sequestration. Diamide-treated RBCs exposed to serum bound opsonin much as did senescent RBCs, and sequestration was inhibited by GalNAc, RGD, and antibodies to CR3, FcgammaRI, FcgammaRII, LRI, and IAP. CONCLUSION: Membrane alterations resulting in the binding of opsonins and the sequestration of senescent RBCs may be similar to those that occur on diamide-oxidized RBCs. They suggest the need for cooperative events among oxidation, clustering and cross-linking, and serum opsonization.

Complement C3↗
PubMed1993

Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation.

Transcriptional regulation of the sodA gene, a member of the soxRS regulon encoding the manganese-containing superoxide dismutase (MnSOD; superoxide:superoxide oxidoreductase, EC 1.15.1.1) of Escherichia coli, was examined in a variety of regulatory mutants. Diamide, an oxidant that causes the anaerobic biosynthesis of the MnSOD polypeptide and also facilitates insertion of manganese at the active site, was found to anaerobically induce MnSOD in both soxRS and fur arcA fnr strains. Metal chelating agents also caused anaerobic induction of MnSOD in a fur arcA fnr triple mutant; however, this induction of MnSOD and of glucose-6-phosphate dehydrogenase (G6PD) by 1,10-phenanthroline was dependent on an intact soxRS locus. A strain of E. coli bearing a fusion of the soxS promoter to lacZ was used to demonstrate that both diamide and 1,10-phenanthroline caused anaerobic activation of soxS transcription. These results indicate that (i) both diamide and 1,10-phenanthroline induce the soxRS regulon anaerobically by stimulation of soxS transcription; (ii) diamide, but not metal chelators, also induces MnSOD biosynthesis by a soxRS-independent mechanism, perhaps mediated by effects on fur, arcA, or fnr-mediated repression of sodA; and (iii) the soxRS locus contains a metal-binding component and is responsive to the redox status of the cell.

Diamide↗
PubMed1995

Characterization of Arabidopsis thaliana cDNAs that render yeasts tolerant toward the thiol-oxidizing drug diamide.

Diamide oxidizes cellular thiols and induces oxidative stress. To isolate plant genes which may, when overexpressed, increase tolerance of plants toward oxidative damage, an in vivo diamide tolerance screening in yeasts was used. An Arabidopsis cDNA library in a yeast expression vector was used to transform a yeast strain with intact antioxidant defense. Cells from approximately 10(5) primary transformants were selected for resistance to diamide. Three Arabidopsis cDNAs which confer diamide tolerance were isolated. This drug tolerance was specific and no cross tolerance toward hydroperoxides was found. One cDNA (D3) encodes a polypeptide which has an amino-terminal J domain characteristic of a divergent family of DnaJ chaperones. Another (D18) encodes a putative dTDP-D-glucose 4,6-dehydratase. Surprisingly, the third cDNA (D22) encodes a plant homolog of gamma-glutamyltransferases. It would have been difficult to predict that the expression of those genes would lead to an improved survival under conditions of depletion of cellular thiols. Hence, we suggest that this cloning approach may be a useful contribution to the isolation of plant genes that can help to cope with oxidative stress.

Amino Acid Sequence↗
PubMed1988

Energy metabolism and quantal acetylcholine release: effects of botulinum toxin, 1-fluoro-2,4-dinitrobenzene, and diamide in the Torpedo electric organ.

In the Torpedo electric organ, a modified nerve-muscle system, type A botulinum toxin blocked the release of acetylcholine (ACh) quanta, both neurally evoked and spontaneous. At the same time, the toxin increased the release of a class of small miniature potentials (the subminiature potentials), reduced the ATP and more the creatine phosphate content of the tissue, and impaired the activity of creatine kinase (CK). Thus, we compared this pattern of changes with those provoked by 1-fluoro-2,4-dinitrobenzene (FDNB), an efficient inhibitor of CK. As expected, FDNB rapidly inactivated CK, which resulted in a profound depletion of ATP whereas the stores of creatine phosphate were preserved. In addition, FDNB caused conspicuous morphological alterations of nerve endings and ACh depletion. This agent also suppressed evoked and spontaneous quantal release whereas the occurrence of subminature potentials was markedly increased. Diamide, a penetrating thiol oxidizing substance, provoked first a transient rise in quantal ACh release and then blockade of transmission with, again, production of a large number of subminiature potentials. Creatine phosphate was depleted in the tissue by diamide, the ATP content reduced, and CK activity partly inhibited. The morphology of nerve terminals did not show obvious changes with either diamide or botulinum toxin at the stage of transmission failure. Although the three poisons acted by different mechanisms, this resulted in a rather similar pattern of physiological changes: failure of quantal release and enhancement of subquantal release. These results and experiments on synaptosomes indicated that CK inhibition was probably a crucial mechanism for FDNB but not for diamide or botulinum intoxication.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylcholine↗