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At least 19 recordsLinked to original sources
PubMed1981

Mechanism of growth stimulation of L1210 cells by 2-mercaptoethanol in vitro. Role of the mixed disulfide of 2-mercaptoethanol and cysteine.

The mechanism of the growth-promoting action of 2-mercaptoethanol on mouse lymphoma L1210 cells in vitro has been studied. The normal line of L1210 is deficient in its capacity to take up cystine, and this limits the growth of the cells in normal culture media containing cystine. In the presence of 2-mercaptoethanol, the cells obtain a high capacity to utilize cystine in the medium. The reaction of 2-mercaptoethanol with cystine produces a mixed disulfide of 2-mercaptoethanol and cysteine. The mixed disulfide is taken up by the cells mainly via the L system, a transport system for neutral alpha-amino acids such as leucine. The mixed disulfide within the cells is rapidly reduced to produce cystine and 2-mercaptoethanol which escapes rapidly into the medium and reacts with cystine again. With the aid of this cyclic action of 2-mercaptoethanol, the cells are able to utilize cystine constantly.

Amino Acids↗
PubMed1983

Mechanism of augmentation of the antibody response in vitro by 2-mercaptoethanol in murine lymphocytes. II. A major role of the mixed disulfide between 2-mercaptoethanol and cysteine.

Five thiol compounds including 2-mercaptoethanol (2-ME) were examined for their augmenting effects on in vitro antibody response to sheep erythrocytes. Three compounds were effective with the following order of activity; 2-ME greater than dithiothreitol greater than cysteamine. Glutathione and thioglycollate failed to enhance the response. The same order or effectiveness was seen in the stimulation of [35S]cystine uptake by murine lymphocytes by these thiols. Murine lymphocytes took up cysteine five to six times more rapidly than cystine. It is, however, unlikely that 2-ME stimulation of cystine uptake is solely due to the reduction of cystine into cysteine, because 2-ME was still stimulatory after free thiol groups had disappeared in the medium containing 2-ME and [35S]cystine. The mixed disulfide of cysteine with 2-ME (Cys-2-ME) was found to be an only product after free thiols had been oxidized. [35S]Cys-2-ME was taken up by the lymphocytes with a comparable rate to cysteine via a transport system common to that of leucine and phenylalanine. Cysteine was, however, transported via a different route. It was observed that Cys-2-ME was readily metabolized to cysteine and glutathione after the uptake. Cys-2-ME added to cystine-free RPMI 1640 medium could support the antibody response as efficiently as cystine plus 2-ME. These observations strongly suggest that 2-Me stimulates cystine uptake and, therefore, enhances the antibody response through the formation of the mixed disulfide with cysteine.

Adjuvants, Immunologic↗
PubMed1983

Mechanism of augmentation of the antibody response in vitro by 2-mercaptoethanol in murine lymphocytes. III. Serum-bound and oxidized 2-mercaptoethanol are available for the augmentation.

The fetal calf serum (FCS) that was incubated with 2-mercaptoethanol (2-ME) followed by the removal of free 2-ME could support the antibody response to sheep erythrocytes in vitro as effectively as native FCS plus 2-ME. The supporting activity of 2-ME-pulsed FCS was reversibly abrogated by the treatment with dithiothreitol followed by dialysis. In addition, iodoacetamide-treated FCS did not acquire the supportiveness by 2-ME pulsing. These observations suggest that the activity of 2-ME-pulsed FCS would be due to the mixed disulfide between 2-ME and FCS components. On the other hand, the disulfide form of 2-ME (2-MEox) could also augment the antibody response as effectively as fresh 2-ME (the reduced form). These derivatized forms of 2-ME as well as fresh 2-ME was found to stimulate the transport of [35S]cystine into murine lymphocytes when the uptake was examined by the long-term experiments (24 hr). These stimulations were thought to be mediated by the formation of the mixed disulfide between 2-ME and cysteine because the lymphocytes promoted the reaction of [35S]cystine with 2-MEox- or 2-ME-pulsed FCS to produce the mixed disulfide that had been shown to be taken up by the lymphocytes four to five times more rapidly than cystine. Therefore, it was suggested that 2-MEox, and 2-ME-pulsed FCS could augment the antibody response in a similar fashion to 2-ME by stimulating the uptake of cystine, an essential amino acid.

Adjuvants, Immunologic↗
PubMed1982

Mechanism of augmentation of the antibody response in vitro by 2-mercaptoethanol in murine lymphocytes. I. 2-Mercaptoethanol-induced stimulation of the uptake of cystine, an essential amino acid.

The mechanism of augmentation of the primary antibody response in vitro by 2-mercaptoethanol (2-ME) was investigated. By using cystine-free RPMI 1640 medium, it was demonstrated that cyst(e)ine was absolutely required for eliciting the following murine lymphocyte reactions: antibody response to sheep erythrocytes, proliferative response to concanavalin A or lipopolysaccharide (LPS), and polyclonal antibody response induced by LPS. The maximal antibody response was attained with 2.5-5 mM cysteine or half-cystine. The serial feeding of fresh cysteine markedly amplified its capacity to support antibody response particularly when cysteine concentration was suboptimal. Such an effect was not observed in the serial addition of cystine. On the other hand, the dose-response curve of cystine was dramatically shifted to lower concentrations by the addition of 2-ME (1 x 10(-5) M), which alone could not elicit the antibody response in the absence of cystine, nor could it augment furthermore the maximal response induced by 2.5 mM half-cystine. Commercially available RPMI 1640 medium contains 0.41 mM half-cystine, which proved to be a suboptimal concentration for eliciting the maximal response. 35S-cystine was incorporated into murine lymphocytes five to six times more slowly than 35S-cysteine. The rate of cystine uptake, however, was accelerated by 2.5-fold in the presence of 1 x 10(-5) M 2-ME. A close correlation was observed between dose-response profiles of 2-ME in augmenting the antibody response and the stimulation of cystine uptake. These results strongly suggest that one of the roles of 2-ME in augmenting the antibody response in vitro is to facilitate the use of cystine contained in RPMI 1640 medium only at a suboptimal concentration.

Amino Acids, Essential↗
PubMed1996

The effects of mercaptoethanol-formaldehyde on tissue fixation and protein retention.

The study compared the effects of mercaptoethanol-formaldehyde and formaldehyde alone, on tissue fixation and protein retention in human and mouse tissues. Shrinkage of tissues and the penetration rate of the fixatives were assessed. The cross-linking ability of the fixatives was determined by viscometry, sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and spectrophotometry, using bovine serum albumin and human haemoglobin. Tissues fixed in buffered 0.0025% mercaptoethanol-4% formaldehyde showed good nuclear and cytoplasmic detail, better than those fixed in buffered 4% formaldehyde. There was no significant difference in shrinkage. A mixture of 0.0025% mercaptoethanol-4% formaldehyde penetrated faster into adult liver than 4% formaldehyde. The mean penetration rate (+/-SE) or coefficient of diffusibility of 0.0025% mercaptoethanol-4% formaldehyde into adult liver was 1.32 +/- 0.01 and that of 4% formaldehyde was 1.12 +/- 0.06 (p < 0.04). Both fixatives diffused more rapidly into mouse liver than into human liver. The cross-linking ability of mercaptoethanol-formaldehyde depends on the concentration of the fixative and the time of fixation. Bovine serum albumin (15%) and 0.1% mercaptoethanol alone formed a gel, whilst electrophoresis showed monomers in the supernatant. Mercaptoethanol (0.1%) also rapidly decreased the absorption at 420 nm, suggesting denaturation. It seems that mercaptoethanol increases the number of thiol groups available to form cross-links with formaldehyde. This study demonstrated that mercaptoethanol-formaldehyde fixed and cross-linked tissues better than formaldehyde at 3 h and 4 h, but not at 1 h and 2 h. The most effective concentration of mercaptoethanol for tissue fixation in 4% formaldehyde is 0.0025%.

Animals↗
PubMed1972

The effects of mercaptoethanol and of peritoneal macrophages on the antibody-forming capacity of nonadherent mouse spleen cells in vitro.

Nonadherent mouse spleen cells exhibited poor viability and little or no capacity to form antibodies to sheep red cells in the Mishell-Dutton culture system. Viability and antibody-forming capacity could be restored by addition to these cultures of low concentrations of mercaptoethanol (10(-4)-10(-5)M), or by addition of appropriate numbers of mouse peritoneal macrophages. Macrophage concentrations lower than optimal resulted in lower lymphoid cell viability and correspondingly fewer plaque-forming cells, whereas excess macrophages resulted in marked inhibition of antibody formation despite good viability of the lymphocytes. Restoration of the nonadherent cells with mercaptoethanol was thus much simpler and more reproducible than it was with macrophages; furthermore, the number of plaque-forming cells developed in cultures restored with mercaptoethanol was approximately fourfold higher than it was in cultures restored with optimal numbers of macrophages. In the presence of mercaptoethanol, the plaque-forming capacity of the nonadherent spleen cells was not increased when small numbers of macrophages were added to the system, nor was it decreased when the few macrophages present in the nonadherent cells were further reduced or eliminated. Excess macrophages inhibited antibody formation in the cultures containing mercaptoethanol as they did in control cultures. Optimal restoration of plaque-forming capacity to the nonadherent spleen cells with mercaptoethanol required the reducing agent to be present throughout the 4 or 5 day culture period. Addition of mercaptoethanol 1 or more days after initiation of culture, or transfer of the cells to a medium free of mercaptoethanol before completion of the culture resulted in a reduction in the numbers of plaque-forming cells. The results suggest that mouse lymphoid cells do not require macrophages in order to form antibodies to sheep red cells in vitro, provided mercaptoethanol is present in the culture medium. The mechanism of action of mercaptoethanol under these conditions is not completely clear, but one of its effects is to promote the viability of lymphoid cells in the cultures.

Animals↗
PubMed1992

Effect of 2-mercaptoethanol on glutathione levels, cystine uptake and insulin secretion in insulin-secreting cells.

The role of glutathione (GSH) in the differentiated state of insulin-secreting cells was studied using 2-mercaptoethanol as a means of varying intracellular GSH levels. 2-Mercaptoethanol (50 microM) caused a marked increase of GSH in two rat insulinoma cell lines, RINm5F and INS-1, the latter being dependent on the presence of 2-mercaptoethanol for survival in tissue culture. The effect of 2-mercaptoethanol on GSH was shared by other thiol compounds. Since in other cell types 2-mercaptoethanol is thought to act on cystine transport, thereby increasing the supply of cysteine for GSH synthesis, we have studied [35S]cystine-uptake in INS-1 cells. At equimolar concentrations to cystine, 2-mercaptoethanol caused stimulation of [35S]cystine-uptake. The effect persisted in the absence of extracellular Na+, probably suggesting the involvement of the Xc- carrier system. INS-1 cells with a high GSH level, cultured 48 h with 2-mercaptoethanol, displayed a lower cystine uptake than control cells with a low GSH content. The effect of variations of the GSH levels on short-term insulin release was studied. No alteration of glyceraldehyde-induced or KCl-induced insulin release in RINm5F cells was detected. In contrast, both in islets and in INS-1 cells, a high GSH level was associated with a slightly lower insulin release. In INS-1 cells the effect was more marked at low glucose concentrations, resulting in an improved stimulation of insulin secretion. On the other hand, in islets, a decrease in the incremental insulin release evoked by glucose was seen. As in other cell types, oxidized glutathione (GSSG) was less than 5% of total GSH, and in INS-1 cells no change in the GSH/GSSG ratio was detected during glucose-induced or 3-isobutyl-1-methylxanthine-induced insulin release. In conclusion, 2-mercaptoethanol-dependent INS-1 cells, as well as RINm5F cells and islets of Langerhans, display a low capacity in maintaining intracellular levels of GSH in tissue culture without extracellular thiol supplementation; 2-mercaptoethanol possibly acts by promoting cyst(e)ine transport; changes in GSH levels caused a moderate effect on the differentiated function of insulin-secreting cells.

Animals↗
PubMed1991

Induction of lymphokine-activated killer activity in rat splenocyte cultures: the importance of 2-mercaptoethanol and indomethacin.

The role of 2-mercaptoethanol and indomethacin in the induction of lymphokine-activated killer (LAK) activity by interleukin-2 (IL-2) in rat splenocyte cultures was investigated. Spleens from 4-month-old male rats of five different strains were tested. Splenocytes were cultured for 3-5 days in the presence of IL-2 (1000 U/ml) and LAK activity was assessed by 4-h 51Cr release assays with P815 and YAC-1 cells as targets. LAK activity could be induced by IL-2 in splenocytes from all rat strains, but only when 2-mercaptoethanol was present in the culture medium. Optimal LAK activity was induced when the 2-mercaptoethanol concentration in splenocyte cultures was at least 5 microM. Different rat strains showed differences in levels of in vitro induction of LAK activity. In the presence of 2-mercaptoethanol the level of LAK activity induced by IL-2 was high in BN and Lewis rats, intermediate in Wistar and Wag rats, and low in DZB rats. In the absence of 2-mercaptoethanol no or minimal LAK activity was induced. Furthermore we observed that addition of 50 microns indomethacin to the culture medium in the presence of 2-mercaptoethanol augmented the induction of LAK activity to some extent. In the absence of 2-mercaptoethanol, addition of indomethacin resulted only in low levels or no induction of LAK activity. We conclude that for optimal induction of LAK activity by IL-2 in rat splenocyte cultures 2-mercaptoethanol is essential, while indomethacin can only marginally further improve this induction.

Animals↗
PubMed1989

Full replacement of 2-mercaptoethanol by cysteine plus selenium compounds in augmenting DNA synthesis of mitogen-stimulated mouse spleen lymphocytes.

Mouse spleen lymphocytes require 2-mercaptoethanol for maximal mitogenic activation in vitro. Previous studies indicate that the lymphocytes are defective in the cystine transport activity and that they require 2-mercaptoethanol to utilize cystine. 2-Mercaptoethanol catalytically carries cysteine moiety into the cells in a mixed disulfide form. Because cysteine is easily oxidized to cysteine in the culture medium, it has been not easy to precisely examine the effect of near-physiological concentrations of cysteine on the activation of lymphocytes. By controlling the cysteine content in the medium, we have reviewed the effect of cysteine to see if cysteine replaces 2-mercaptoethanol in enhancing the DNA synthesis of lipopolysaccharide-stimulated lymphocytes. It was found that cysteine was less effective than 2-mercaptoethanol, and that cysteine fully replaced 2-mercaptoethanol when a selenium compound was supplemented. The effects of cysteine and selenium compounds were apparently independent and additive. Among the selenium compounds examined, sodium selenite and L-selenocystine were much more effective in stimulating DNA synthesis than sodium selenate and L-selenomethionine.

Animals↗
PubMed1990

Inactivation of (Na+,K+)-ATPase by beta-mercaptoethanol. Differential sensitivity to reduction of the three beta subunit disulfide bonds.

The relative rates of reduction of disulfide bonds in sheep kidney (Na+,K+)-ATPase were determined in order to test the hypothesis that cleavage of a single disulfide bond in the beta subunit is responsible for loss of ATPase activity upon treatment with high concentrations of beta-mercaptoethanol at elevated temperatures (Kawamura, M., and Nagano, K. (1984) Biochim. Biophys. Acta 774, 188-192). This was accomplished by peptide mapping of tryptic digests of the alpha and beta subunits after treatment with beta-mercaptoethanol. Alkylation with 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole of all free sulfhydryls and all newly produced sulfhydryls resulting from reduction of disulfides by beta-mercaptoethanol introduced a fluorophore into those residues. The protective effect of NaCl and KCl on ATPase activity was examined with regard to the ability of those salts to protect the disulfides from reduction. The results indicated that although the disulfides in the beta subunit exhibit differential stabilities to reduction, the reduction of no single disulfide in the beta subunit can be quantitatively correlated with the loss of ATPase activity and the ability to bind ouabain. The kinetics of inhibition of ouabain binding were identical to the kinetics of inhibition of ATPase activity, suggesting a delocalized denaturation rather than reduction of a single disulfide bond as the mechanism of beta-mercaptoethanol induced inhibition. NaCl and KCl only partially protected all three beta disulfides from reduction, but completely eliminated the loss of ATPase activity and ouabain binding sites induced by beta-mercaptoethanol. The results suggest a possible folding model for the beta subunit. The alpha subunit was found to contain three disulfide bonds, but these bonds were not reduced by the beta-mercaptoethanol treatment used to inactivate the ATPase activity.

Adenosine Triphosphate↗
PubMed1982

Requirement of 2-mercaptoethanol for in vitro growth factor production by T cells and vulnerability of the response to age.

The effects of 2-mercaptoethanol and age on spleen cells derived from young (3-4 months) and old (24-months) C57BL/6 mice were measured with respect to T cell growth factor or Interleukin 2 production. It was shown that: (A) 2-mercaptoethanol (or some homologue) is absolutely required for T cell growth factor production in vitro by murine cells (the optimum concentration is 5 X 10(-5) M for both young and old cells); (B) old cells are less responsive to suboptimum concentrations than young cells but their responses are not reduced to the same degree as young cells by supraoptimum toxic doses of 2-mercaptoethanol; and (C) at optimum 2-mercaptoethanol concentrations young and old cells have similar kinetic responses for T cell growth factor production and the accumulation of the T cell growth factor reaches a maximum between 18 and 24 hours. Considerations are presented of 2-mercaptoethanol (or some homologue) in its role as an important reactant in the production of T cell growth factor and in its susceptibility to aging.

Aging↗
PubMed1988

Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization.

1. Metallothionein behavior in SDS-PAGE has been characterized. 2. It has been found that metallothionein behavior in this electrophoretic system depends upon the reducing environment. Migration as a well-defined protein band is only achieved in the presence of 2-100 mM 2-mercaptoethanol. 3. Within those 2-mercaptoethanol levels, both rat and dogfish metallothionein migrate as a protein with a molecular weight several times higher than that expected by amino acid analyses. This is not due to molecule oxidations, since this effect is promoted by the presence of 2-mercaptoethanol. 4. No effect of 2-mercaptoethanol on metallothionein behavior is found in conventional PAGE. 5. The present results suggest that to study the effect of 2-mercaptoethanol in SDS-PAGE is a simple and accurate way to identify a protein as metallothionein. 6. It has also been found that metallothionein aggregates naturally in the absence of ionic strength.

Acetates↗
PubMed1996

Mechanism of activation of the tryptophan synthase alpha2beta2 complex. Solvent effects of the co-substrate beta-mercaptoethanol.

To characterize the conformational transitions that lead to activation of catalysis by the tryptophan synthase alpha2beta2 complex, we have determined the solvent effects of a co-substrate, beta-mercaptoethanol, and of a model nonsubstrate, ethanol, on the catalytic and spectroscopic properties of the enzyme. Our results show that ethanol and beta-mercaptoethanol both alter the equilibrium distribution of pyridoxal 5'-phosphate intermediates formed in the reactions of L-serine at the beta site in the alpha2beta2 complex. Addition of increasing concentrations of ethanol increases the proportion of the external aldimine of L-serine and decreases the proportion of the external aldimine of aminoacrylate. Low concentrations of the co-substrate beta-mercaptoethanol (Kd = approximately 13 mM) decrease the proportion of the external aldimine of aminoacrylate and induce formation of the quinonoid of S-hydroxyethyl-L-cysteine. Higher concentrations of beta-mercaptoethanol decrease the concentration of the quinonoid intermediate and increase the proportion of the external aldimine of L-serine. Data analysis shows that beta-mercaptoethanol and ethanol both interact or bind preferentially with the conformer of the enzyme that predominates when the aldimine of L-serine is formed and shift the equilibrium in favor of this conformer. We propose that a nonpolar region of the beta subunit, possibly the hydrophobic indole tunnel, becomes less exposed to solvent in the conformational transition that activates the alpha2beta2 complex.

Allosteric Regulation↗
PubMed1975

Specific inhibition of sclerotium formation by 2-mercaptoethanol and related sulfhydryl compounds in Sclerotium rolfsii.

Sclerotium formation in Sclerotium rolfsii was completely inhibited by 2-mercaptoethanol at a concentration of 2-4 mM without any adverse effect on mycelial growth. Concentrations lower than 2 mM had no effect on mycelial growth and sclerotium formation, whereas both were inhibited at concentrations higher than 4 mM. Complete inhibition of sclerotium formation with no effect on mycelial growth was also obtained by propyl mercaptan, 1-butyl mercaptan and 2-butyl mercaptan at a concentration of 0.10 mM. Sclerotium formation was also inhibited by benzyl mercaptan and thioglycolic acid at 0.15 mM and 2-4 mM concentration respectively, whereas it was only partially inhibited by L-cysteine and glutathione at 20 mM. Mycelium grown for 21 days in nutrient medium supplemented with mercaptoethanol at a concentration of 3 mM, when transferred into fresh medium without the chemical, grew normally and produced abundant mature sclerotia. Mercaptoethanol inhibited the initiation as well as the further development of young, unpigmented sclerotia. The mechanism of sclerotium formation was arrested completely when mercaptoethanol was added to the growth medium at any time between inoculation and the appearance of sclerotia of the "development" stage. It is suggested that the specific inhibitory action of mercaptoethanol could be used to study the mechanism of sclerotium formation

Cysteine↗
PubMed1983

Comparison of the 2-mercaptoethanol and dithiothreitol tests for determining Brucella immunoglobulin G agglutinating antibody in bovine serum.

The dithiothreitol test was evaluated as a substitute for the 2-mercaptoethanol test for determining Brucella immunoglobulin G agglutinating antibody in bovine serum. The tests were compared on 207 card-positive sera that showed a standard tube-agglutination titer of incomplete 1:50 or higher. The tests agreed within one dilution with 182 of the 207 sera tested for an 87.9% rate of agreement. When titers were not the same, those obtained with the dithiothreitol test were more frequently lower than higher than those obtained with the 2-mercaptoethanol test. Sixteen sera that showed a titer with the 2-mercaptoethanol test were negative with the dithiothreitol test and two that showed a titer with the dithiothreitol test were negative with the 2-mercaptoethanol test. Results suggest that the dithiothreitol test is not a reliable substitute for the 2-mercaptoethanol test to detect immunoglobulin G agglutinating antibody in bovine serum.

Agglutination Tests↗
PubMed1983

[Effect of 2-mercaptoethanol on the individual periods of the mitotic cycle].

Dynamics of the mitotic cycle of the KEPV cells being on different interphase stages at the start of a 20 hour 2-mercaptoethanol (0.001 M) treatment has been studied during the treatment and for 11 hours after washing out the agent. The KEPV cells affected by mercaptoethanol during the interphase (G1, S, G2) were shown to continue their passage through the cycle to enter mitosis, but part of the cells of the S period and of the first half of the G2 period were arrested in the interphase. In the presence of mercaptoethanol, mitotic cells reach the metaphase stage, and their further behaviour depends on the duration of the treatment. For the first 8 hours of treatment, a phase of "unstable block" exists for cells that were in S and G2 periods at the beginning of treatment, while other cells are transformed into K-metaphases. 8 hours later a phase of "stable block" occurs and all the normal metaphases are transformed into K-metaphases. After washing out the culture from mercaptoethanol the cells are ejected from the block in K-metaphase. The transformation from K-metaphase into the normal metaphase is realised in the course of this process. The cells which were in S and G2 periods at the beginning of the treatment are ejected from the block simultaneously after washing, while the cells of the G1 period--with a small delay. After washing out mercaptoethanol the cells that were in the interphase (G1, S, G2) at the beginning of the treatment are capable of producing both multipolar mitoses and mitoses without cytotomy.

Animals↗
PubMed1985

Reduced glutathione in Chinese hamster ovary cells protects against inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 2-mercaptoethanol disulfide.

When the disulfide of 2-mercaptoethanol (ESSE) is added to the medium of cultured Chinese hamster ovary (CHO) cells, a time and concentration dependent release of 2-mercaptoethanol to the medium is observed. The reduction of ESSE to 2-mercaptoethanol by cells is a saturable process, the rate being approximately 50 nmoles of 2-mercaptoethanol per mg cell protein for an hour upon exposure to 250 microM ESSE. Reduction rate of ESSE by cells attached to a substratum is independent of glucose and insulin for periods up to 4 hours. However, in detached cells, swirled in suspension, addition of glucose and insulin is necessary in order to obtain a linear reduction rate of ESSE. The rate limiting enzyme in the sterol biosynthetic pathway, 3-hydroxy-3-methyl-glutaryl Coenzyme A reductase (E.C. 1.1.1.34), is inhibited by ESSE when isolated from CHO cells but total nonsaponifiable lipids synthesis from [2-14C]-acetate in intact cells is not affected by ESSE at concentrations up to 500 microM. Cytosolic reduced glutathione can spontaneously exchange disulfide bonds with ESSE and thus prevent it from inhibiting the reductase. Cultured cells respond to ESSE administration by elevating their total and acid-soluble glutathione levels. The use of ESSE as a perturbant of the GSH Status in cells is discussed.

Animals↗