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PubMed2001

Involvement of K(+)-Cl(-)-cotransport in the apoptosis induced by N-ethylmaleimide in HepG2 human hepatoblastoma cells.

The role of K(+)-Cl(-)-cotransport in apoptosis in human cancer cells was investigated. N-Ethylmaleimide, a K(+)-Cl(-)-cotransport activator, induced apoptosis in a dose-dependent manner in HepG2 human hepatoblastoma cells. N-Ethylmaleimide induced Cl(-)-dependent K(+) efflux, indicating that K(+)-Cl(-)-cotransport is functionally present in HepG2 cells. Calyculin-A and genistein, inhibitors of K(+)-Cl(-)-cotransport, significantly prevented both K(+)-Cl(-)-cotransport activation and apoptosis induced by N-ethylmaleimide. These results demonstrate, for the first time, a novel role for K(+)-Cl(-)-cotransport in apoptosis in human hepatoma cells. These results further suggest that K(+)-Cl(-)-cotransport may be a valuable target for therapeutic interventions for human hepatoma.

Apoptosis↗
PubMed2002

Effect of pertussis toxin and N-ethylmaleimide on voltage-dependent and -independent calcium current modulation in serotonergic neurons.

Introduction of GTP-gamma-S into a neuronal cell spontaneously results in G-protein activation. A possible contribution to this mechanism is that some receptors have a constitutive activity that stimulates GDP/GTP exchange resulting in increased GTPase activity of G-protein alpha subunits, leading to a facilitation of GTP-gamma-S binding. It follows that partial or complete uncoupling of receptors and G-proteins could inhibit Ca(2+) current modulation by GTP-gamma-S. This possibility was tested in acutely isolated rat dorsal raphe neurons by uncoupling the receptor and G-protein using N-ethylmaleimide and pertussis toxin. Since these compounds have been suggested to differentially block voltage-dependent inhibition, relative to voltage-independent, we investigated whether the apparent voltage-independent component of Ca(2+) channel modulation by 5-hydroxytryptamine (5-HT) shares the same mechanism as the voltage-dependent component. N-ethylmaleimide inhibited the response to 5-HT by about 50% but had no effect on the response to GTP-gamma-S. In dorsal raphe neurons 28.9% of the total response to 5-HT was voltage-independent. N-ethylmaleimide had identical effects on the voltage-dependent and -independent components as measured by tail current inhibition. The response to 5-HT was completely sensitive to pertussis toxin, and completely uncoupling the receptors and G-proteins did not affect the maximal response to GTP-gamma-S. Our results suggest that the apparent voltage-independent component of Ca(2+) channel modulation by 5-HT in dorsal raphe neurons might share the same mechanism as does the voltage-dependent component. In addition, these experiments provided evidence that partial or even complete uncoupling of receptors and G-proteins did not affect Ca(2+) current modulation by direct activators of G-proteins.

Animals↗
PubMed1982

Chemical modification of actin. Acceleration of polymerization and reduction of network formation by reaction with N-ethylmaleimide, (iodoacetamido)tetramethylrhodamine, or 7-chloro-4-nitro-2,1,3-benzoxadiazole.

We examined the properties of rabbit skeletal muscle actin labeled at Cys-373 with N-ethylmaleimide or with (iodoacetamido)tetramethylrhodamine, and of N-ethylmaleimide-actin further modified with 7-chloro-4-nitro-2,1,3-benzoxadiazole (which primarily labels Lys-372). All three derivatives polymerize more rapidly than unlabeled actin. As measured by fluorescence photobleaching recovery and low-shear viscometry, all three also show a lower extent of network formation relative to native actin. N-Ethylmaleimide has a much smaller effect on the rate of polymerization and on network formation than do the other two derivatives. We suggest that chemical modification of actin with these compounds may stabilize nuclei, accounting for the acceleration of polymerization. Stabilization of nuclei also reduces the average filament length at equilibrium, thereby reducing the extent of network formation. We note a parallel between these results and the effects that cytochalasin and capping proteins have on the polymerization of actin.

4-Chloro-7-nitrobenzofurazan↗
PubMed1979

Identification of the N-ethylmaleimide reactive protein of the mitochondrial phosphate transporter.

The mitochondrial phosphate carrier is inhibited by the SH reagents p-(hydroxymercuri)benzoate and N-ethylmaleimide. Based on an analysis utilizing dodecyl sulfate-polyacrylamide gels, an SH-containing 32 000-dalton protein has been identified as a component of the phosphate carrier system. Two other N-[3H]ethylmaleimide-labeled proteins of the inner mitochondrial membrane have been eliminated from this role [Wholrab, H., & Greaney, J., Jr. (1978) Biochim. Biophys. Acta 503, 425] on the basis that band IV (45,000 daltons) is absent from heart sonic submitochondrial particles and band VII (6 500 daltons) does not react with p-(hydroxymercuri)benzoate. The mobility of the 32 000-dalton protein (0.43) is lower than that of the gamma subunit of the mitochondrial ATPase (0.46) and the carboxyatractyloside binding protein (0.48) on 12.5% dodecyl sulfate-polyacrylamide gels. In these flight muscle mitochondria, 0.87 nmol of N-[3H]ethylmaleimide per nmol of cytochrome a is bound to the 32,000-dalton protein.

Animals↗
PubMed1983

Partial disruption of naturally occurring groups of insulin receptors on adipocyte plasma membranes by dithiothreitol and N-ethylmaleimide: the role of disulfide bonds.

In this ultrastructural study, monomeric ferritin-insulin was used to further elucidate the role of disulfide bonds in maintaining the natural groups of insulin receptors on adipocyte plasma membranes. Dithiothreitol (1 mM) caused partial disruption of the occupied receptor groups with an increase in single receptors to greater than 50% of total occupied receptors. N-Ethylmaleimide (1 mM) disrupted the groups to the same extent as dithiothreitol and the effect was partly additive with the dithiothreitol effect. The magnitude of the disruption caused by dithiothreitol or N-ethylmaleimide was similar to that caused by cytochalasin B. Dithiothreitol, a reducing agent, caused a marked increase in binding of insulin to the plasma membranes while N-ethylmaleimide and cytochalasin B, both thiol reagents, had little if any effect on insulin binding. These data suggest that two different sets of disulfide bonds are involved. One set was susceptible to both reducing and thiol reagents and responsible for holding the receptor groups together, and the other set was susceptible to reducing agents only and related to the increased insulin binding caused by dithiothreitol. A proposed model is discussed.

Adipose Tissue↗
PubMed2002

Brain-derived neurotrophic factor regulates surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid receptors by enhancing the N-ethylmaleimide-sensitive factor/GluR2 interaction in developing neocortical neurons.

In hippocampal neurons, the exocytotic process of alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA)-type glutamate receptors is known to depend on activation of N-methyl-d-aspartate channels and its resultant Ca(2+) influx from extracellular spaces. Here we found that brain-derived neurotrophic factor (BDNF) induced a rapid surface translocation of AMPA receptors in an activity-independent manner in developing neocortical neurons. The receptor translocation became evident within hours as monitored by [(3)H]AMPA binding and was resistant against ionotropic glutamate receptor antagonists as evidenced with surface biotinylation assay. This process required intracellular Ca(2+) and was inhibited by the blockers of conventional exocytosis, brefeldin A, botulinum toxin B, and N-ethylmaleimide. To explore the translocation mechanism of individual AMPA receptor subunits, we utilized the human embryonic kidney (HEK) 293 cells carrying the BDNF receptor TrkB. After the single transfection of GluR2 cDNA or GluR1 cDNA into HEK/TrkB cells, BDNF triggered the translocation of GluR2 but not that of GluR1. Subsequent mutation analysis of GluR2 carboxyl-terminal region indicated that the translocation of GluR2 subunit in HEK293 cells involved its N-ethylmaleimide-sensitive factor-binding domain but not its PDZ-interacting site. Following co-transfection of GluR1 and GluR2 cDNAs, solid phase cell sorting revealed that GluR1 subunits were also able to translocate to the cell surface in response to BDNF. An immunoprecipitation assay confirmed that BDNF stimulation can enhance the interaction of GluR2 with N-ethylmaleimide-sensitive factor. These results reveal a novel role of BDNF in regulating the surface expression of AMPA receptors through a GluR2-NSF interaction.

Animals↗
PubMed1987

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. III. Identification of cysteine residues whose modification with N-ethylmaleimide leads to loss of the Ca2+-transporting activity.

The reactive sulfhydryl group (SHD) (Kawakita et al. (1980) J. Biochem. 87, 609-617) which is essential for the decomposition of the E-P intermediate of Ca2+-transporting ATPase of the rabbit skeletal muscle sarcoplasmic reticulum has been identified. One sample of sarcoplasmic reticulum membranes was reacted for 3 min with 0.4 mM N-[3H]ethylmaleimide at pH 7.0 at 30 degrees C to a labeling density of 1 mol/mol ATPase without loss of the Ca2+-transporting activity. Another sample of the membranes was treated similarly with non-radioactive N-ethylmaleimide and then labeled with 0.4 mM N-ethyl[14C]maleimide for 17 min. An extensive loss of the Ca2+-transporting activity occurred during the period of this radio-labeling, thus substantiating the 14C-labeling of SHD. The labeled membranes were digested by thermolysin, and the labeled peptides were fractionated by gel filtration and reversed-phase HPLC. Two major radioactive peptides were present in both 3H- and 14C-labeled thermolytic digests, and each of the major components of 14C-labeled peptides had a counterpart in the major components of 3H-labeled peptides which behaved identically on HPLC. The major 14C-labeled peptides were purified and found to be identical with the two SHN peptides, TL-I and TL-II (Saito-Nakatsuka et al. (1987) J. Biochem. 101, 365-376), and 0.5 mol/mol ATPase each of Cys344 and Cys364 was assigned as SHD. It seems that the Ca2+-transport system retains its activity while either of the two Cys residues is unoccupied, but loses it when both of them are modified with N-ethylmaleimide.

Animals↗
PubMed1982

DNA polymerases of Tetrahymena pyriformis. I. Characterization of two N-ethylmaleimide-sensitive DNA polymerases from exponentially growing cells.

Two DNA polymerase activities, polymerases A and B, were separated from the Triton-treated cell homogenate of exponentially growing Tetrahymena pyriformis by phosphocellulose column chromatography. Their properties were as follows. Polymerase A: The molecular weight was about 140,000, the sedimentation value was about 6.2S, the optimum Mg2+ concentration was 15 mM, the optimum K+ (or Na+) concentration was 20 mM, and the optimum pH was 7.4. The enzyme activity was inhibited by cytosine-beta-D-arabinofuranoside-5'-triphosphate (araCTP) or aphidicolin, but not by 2'-3'-dideoxythymidine-5'-triphosphate (ddTTP). Polymerase B: The molecular weight was about 70,000, the sedimentation value was 4.3S, the optimum Mg2+ concentration was 15 mM, the optimum K+ (or Na+) concentration was 150 mM, and the optimum pH was 8.4. The enzyme activity was inhibited by ddTTP, but not by araCTP or aphidicolin. Polymerases A and B were both found to be N-ethylmaleimide-sensitive. These results indicate that at least two N-ethylmaleimide-sensitive DNA polymerases, A and B, are present in exponentially growing Tetrahymena cells. Polymerase A bears many similarities to DNA polymerase alpha of higher eukaryotes and polymerase B also bears similarities to DNA polymerase beta except as regards N-ethylmaleimide sensitivity. Based on the properties of polymerases A and B, the relation of Tetrahymena DNA polymerases reported by several investigators is discussed.

Animals↗
PubMed1986

Chemical modification of the brown-fat-mitochondrial uncoupling protein with tetranitromethane and N-ethylmaleimide. A cysteine residue is implicated in the nucleotide regulation of anion permeability.

Treatment of brown adipose tissue mitochondria with tetranitromethane or N-ethylmaleimide decreases the affinity with which inhibitory nucleotide GDP binds to the tissue-specific uncoupling protein. Both reagents modify cysteine residues which are 'accessible' and 'buried' to 5,5'-dithio-bis(2-nitrobenzoic acid) (Nbs2). Modification of the single Nbs2-accessible residue correlates with the loss of high-affinity binding sites for GDP. Tetranitromethane does not affect the Cl- or H+ permeability of the protein in the absence of nucleotide, while N-ethylmaleimide increases both by 70-80%. Bound GDP is a less effective inhibitor of Cl- permeability after N-ethylmaleimide or tetranitromethane treatment, but retains much of the ability to inhibit H+ permeation.

Adipose Tissue, Brown↗
PubMed1991

Identification of Lys116 as the target of N-ethylmaleimide inactivation of ferredoxin:NADP+ oxidoreductase.

Oxidized ferredoxin:NADP+ oxidoreductase (FNR) was slowly and irreversibly inactivated by N-ethylmaleimide. Complete protection against inactivation was afforded by saturating concentrations of NADP+. In the presence of NADPH, a rapid inhibition of the enzyme ensued; however, this inhibition was found to be reversible. In the tryptic map of the flavoprotein, modified with N-ethyl[2,3-14C]maleimide in oxidizing conditions, a unique radioactive peptide was found. Its sequence comprised residues 110-117 of the enzyme: Lys116 was shown to be the residue alkylated by N-ethylmaleimide. It is noteworthy that the same residue of FNR was found to be modified by 5-dimethylaminoaphthalene-1-sulfonyl(dansyl) chloride at the putative NADP(H)-binding site [Cidaria, D., Biondi, P. A., Zanetti, G. & Ronchi, S. (1985) Eur. J. Biochem. 146, 295-299]. Furthermore, the data reported here demonstrate that the sulfhydryl groups of FNR are not involved in enzyme inactivation by N-ethylmaleimide.

Amino Acids↗
PubMed1993

N-ethylmaleimide-inhibited electrogenic K+ secretion in the ampulla of the frog semicircular canal.

1. The mechanisms of K+ secretion into endolymph were studied on a preparation of isolated semicircular canal with different pharmacological inhibitors. Three periods of 5 or 30 min were performed, the first as control, the second in the presence of the drugs added to the apical or the basolateral bathing solution, and the third as recovery. Apical fluid was sampled at the beginning and the end of each period, transepithelial potential was recorded, Na+, K+, and Cl- concentrations, and K+ efflux, with 86Rb+ as a tracer, were measured and K+ fluxes were calculated. 2. When both sides of the epithelium were bathed with perilymph-like solution, the epithelium absorbed Na+, secreted K+, and generated a lumen positive potential. 3. The ATPases inhibitors, ouabain (10(-5) and 10(-3) M) and N-ethylmaleimide (10(-4) and 10(-3) M) inhibited the electrogenic K+ secretion when added to the basolateral fluid. N-ethylmaleimide (10(-3) M) applied to the apical fluid during a 5 min period decreased the K+ influx by 43% and the transepithelial potential by 66%. Other ATPase inhibitors, harmaline (10(-3) M), omeprazole (10(-4) M), vanadate (10(-4) M and 10(-3) M), N,N'-dicyclohexylcarbodiimide (DCC, 10(-5) M), 7-chloro-4-nitrobenz-2-oxa-1,3-diazole (NBD-Cl, 5 x 10(-6) M and 5 x 10(-5) M), and bafilomycin (10(-7) M) did not affect the K+ transport nor the transepithelial potential when they were added to the apical fluid. 4. The Na(+)-K(+)-Cl- co-transporter inhibitor, bumetanide, decreased both the transepithelial potential and the K+ transport when added to the basolateral solution but not to the apical one. At 10(-6) M, bumetanide maximally decreased the K+ influx by about 60%. 5. K+ channel blockers, quinine (10(-4) M), TEA (5 x 10(-3) M), added to the apical solution and barium (2 x 10(-3) M) added to either the apical or the basolateral solutions, did not affect the K+ transport and the transepithelial potential. 6. The carbonic anhydrase inhibitor acetazolamide (10(-3) M) added to both apical and basolateral solutions did not affect the K+ transport and the transepithelial potential. 7. It is concluded that, in the ampulla of the semicircular canal, a basolateral Na(+)-K(+)-Cl- co-transporter energized by the Na+, K(+)-ATPase was involved for 60% in the K+ secretion into endolymph. The electrogenic K+ transport would partly depend on a N-ethylmaleimide-sensitive protein possibly located at the apical plasma membrane or intracellularly.

Animals↗
PubMed1989

Effect of N-ethylmaleimide treatment on naloxone binding in frog brain membranes.

Specific binding of (3H) naloxone to opioid receptors in frog (Rana esculenta) brain membranes was irreversibly inactivated by the sulfhydryl group alkylating agent N-ethylmaleimide (NEM). Saturation analysis of (3H) naloxone binding revealed a marked reduction in the number of ligand binding sites after N-ethylmaleimide treatment. Pretreatment of the membranes with unlabelled opioid ligands, i.e. naloxone, morphine, or the kappa selective dynorphin (1-13), and sodium ions resulted in considerable protection of (3H) naloxone binding against the N-ethylmaleimide blockade.

Animals↗
PubMed1986

Purification of N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes.

An N-ethylmaleimide-sensitive ATPase was purified 100-fold from chromaffin granule membranes. The purification procedure included solubilization with polyoxyethylene 9 lauryl ether, chromatography on hydroxylapatite and DEAE-cellulose columns, and glycerol gradient centrifugations. Inclusion of phosphatidylserine and a mixture of protease inhibitors during the purification procedure was necessary to maintain the activity of the preparation. The purified preparation contained four major polypeptides with molecular masses of about 115, 72, 57, and 39 kDa, which were copurified with the ATPase activity. The 115-kDa subunit binds [14C]dicyclohexylcarbodiimide and the subunits of 115 and 39 kDa bind [14C]N-ethylmaleimide. The ATP-dependent proton uptake activity of chromaffin granule membranes is inhibited 50% with about 20 microM N-ethylmaleimide, while over 5 mM concentrations of the inhibitor were required to block the ATPase activity of the membranes. The ATPase activity of the purified enzyme was inhibited via two different affinities: a high affinity site with a Ki in the microM range and a low affinity site in the mM range, each contributing to about 50% inhibition of the enzyme. It is concluded that the proton-ATPase of chromaffin granule membranes contains at least four subunits with the 115-kDa polypeptide being the main subunit having the active site for the ATPase activity of the enzyme.

Adenosine Triphosphatases↗
PubMed1981

The reaction of sulfhydryl groups of sodium and potassium ion-activated adenosine triphosphatase with N-ethylmaleimide. The relationship between ligand-dependent alterations of nucleophilicity and enzymatic conformational states.

The reaction between N-ethylmaleimide and (Na+ + K+)-ATPase, performed under ligand conditions which produce each of the kinetic states of the enzyme and their associated conformational forms, was examined through an analysis of the inhibition of enzymatic activity and the incorporation of radiolabeled reagent into the enzyme. The inactivation reactions displayed pseudo-first order kinetics with respect to the concentration of active enzyme, indicating that the loss of activity is associated with the alkylation of a unique sulfhydryl group. In the absence of enzyme phosphorylation, the nucleophilicity of this sulfhydryl group is affected primarily by the nature of the monovalent cation present and does not correlate with the conformational state. A method for determining the actual concentration and specific radioactivity of radiolabeled N-ethylmaleimide during the reaction with (Na+ + K+)-ATPase was developed, allowing the measurement of the total reactive sulfhydryl groups of native (Na+ + K+)-ATPase under conditions identical with those of the inactivation studies. The labeling of the enzyme complex is associated almost exclusively with the large polypeptide, which contains four sulfhydryl groups which react with this reagent. One of these residues is presumably the sulfhydryl responsible for inactivation of the enzyme. Two react stoichiometrically and rapidly with N-ethylmaleimide under all conditions. The nucleophilicity of the fourth sulfhydryl group is governed by the conformational state of the enzyme, but the alkylation of this residue does not result in loss of enzymatic activity.

Animals↗
PubMed1992

Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes.

Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) are required for the binding of N-ethylmaleimide-sensitive fusion protein (NSF) to Golgi membranes and are, therefore, required for intra-Golgi transport. We report the existence of distinct alpha/beta-SNAP and gamma-SNAP-binding sites in Golgi membranes that appear to be part of the same receptor complex. Cross-linking studies with alpha-SNAP demonstrate that an integral membrane protein of between 30-40 kDa is the alpha-SNAP binding component of the multi-SNAP receptor complex. These data suggest that SNAPs function by independently binding to a multi-SNAP membrane-receptor complex, thereby activating them to serve as adaptors for the targeting of NSF.

Amino Acid Sequence↗
PubMed1998

MgATP-dependent and MgATP-independent [3H]noradrenaline release from perforated synaptosomes both use N-ethylmaleimide-sensitive fusion protein.

In streptolysin-O (SLO)-perforated rat brain cortical synaptosomes, Ca2+-induced [3H]noradrenaline (3H-NA) release began with a phase lasting about 1 min that did not depend on MgATP. Subsequent release became increasingly MgATP-dependent. The first phase involved release from previously "primed" synaptic vesicles. MgATP-dependent release, on the other hand, was release from unprimed vesicles that needed to be primed by ATP hydrolysis before they could be fused with the presynaptic membrane. Vesicle depriming was detected by observing that the initial release decreased when the synaptosomes were perforated and incubated for 2 min in the absence of MgATP before increasing Ca2+ to promote release. One millimolar N-ethylmaleimide (NEM) inhibited both MgATP-dependent and MgATP-independent release at all times of incubation (0.5-5 min), and inhibition by NEM was partially reversed at short (0.5 min) and longer (5 min) times by adding intact N-ethylmaleimide sensitive fusion protein (NSF) to the perforated synaptosomes. Polyclonal antibodies against the N-terminal domain of NSF produced dose-dependent inhibition of Ca2+-induced 3H-NA release. This inhibition occurred in both early and late release phases and was highly significant at early times if the perforated synaptosomes were preincubated for 2 min with anti-NSF. These results indicate participation of NSF both after vesicular fusion, probably for separation of SNARE proteins in v/t-SNARE complexes before endocytosis, and, surprisingly, after docking, possibly to maintain vesicles in a primed state and reverse depriming during regulated secretion.

Adenosine Triphosphate↗
PubMed1997

N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex.

Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) GS28 and syntaxin 5 can be reciprocally coimmunoprecipitated from Golgi extracts, suggesting that they exist in a protein complex. When Golgi extract is preincubated with soluble NSF attachment proteins (alpha-SNAP) and N-ethylmaleimide-sensitive factor (NSF) under conditions that allow ATP hydrolysis by NSF, GS28 and syntaxin 5 become dissociated. GS28 and syntaxin 5 remain in a protein complex when Golgi extract is preincubated with similar amounts of alpha-SNAP and NSF under conditions that prevent ATP hydrolysis by NSF, suggesting that ATP hydrolysis by NSF is necessary for dissociating the GS28-syntaxin 5 complex. Since preincubation of Golgi extract with either alpha-SNAP or NSF alone has no effect on the GS28-syntaxin 5 complex, a concerted action of alpha-SNAP and NSF therefore mediates the dissociation of the GS28-syntaxin 5 complex. Furthermore, GS28 but not syntaxin 5 is capable of binding to immobilized alpha-SNAP when the GS28-syntaxin 5 complex is dissociated.

Animals↗
PubMed1993

Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.

N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem "ATP domains," each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.

Adenosine Triphosphatases↗