curcumin has been researched along with fluorexon* in 5 studies
5 other study(ies) available for curcumin and fluorexon
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Modulation of multidrug resistant in cancer cells by EGCG, tannic acid and curcumin.
Cancer is one of the most common life-threatening diseases worldwide; many patients develop multidrug resistance after treatment with anticancer drugs. The main mechanism leading to multidrug resistance is the overexpression of ABC transporters in cancer cells. Chemosensitizers are needed to inhibit the activity of ABC transporters, resulting in higer intracellular concentration of anticancer drugs. Some secondary metabolites have been reported to be chemosensitizers by inhibiting ABC transporters. Epigallocatechin gallate (EGCG), tannic acid, and curcumin were employed in this study. Different assays were used to detect whether they have the ability to inhibit P-gp activity and overcome multidrug resistance in cancer cells overexpressing P-gp. Hypothesis/Purpose: CEM/ADR 5000 and Caco-2 cell lines, which overexpress P-gp, are multidrug resistant cell lines. We first detected whether the combination of polyphenols (EGCG, tannic acid, curcumin) and doxorubicin, an anticancer drug, is synergistic or not. To further understand the potential mechanism, EGCG, tannic acid, and curcumin were tested to check whether they have the ability to inhibit P-gp activity. When P-gp activity is inhibited, the intracellular concentration of doxorubicin is higher, resulting in enhanced cytotoxicity of doxorubicin.. The P-gp overexpressing human colon cancer cell line Caco-2 and human T-lymphoblastic leukemia cell line CEM/ADR 5000 were used in this study. Two-drug combinations (doxorubicin + polyphenol) and three-drug combinations (doxorubicin + polyphenol + digitonin) were tested to examine potential synergism. The potential mechanism leading to synergism would be the inhibition of P-gp activity. A Rhodamine 123 assay and Calcein-AM assay in Caco-2 and CEM/ADR 5000, respectively, were used to detect P-gp inhibition by EGCG, curcumin, and tannic acid.. MTT assay was used to determine the cytotoxicity of doxorubicin, polyphenols and digitonin alone, and then their combinations. Furthermore, Rhodamine 123 and Calcein-AM were used to detect the effects of polyphenols on the activity of P-gp.. The results demonstrated that a combination of non-toxic concentrations of each polyphenol with doxorubicin synergistically sensitized Caco-2 and CEM/ADR 5000 cells. Furthermore, three-drug combinations (doxorubicin + polyphenol + digitonin) were much more effective. In addition, the activity of P-gp in Caco-2 and CEM/ADR 5000 cells was measured. Consistent with the combination results, tannic acid and curcumin decreased the activity of P-gp both in Caco-2 and CEM/ADR 5000. EGCG, which weakly affected the activity of P-gp in CEM/ADR 5000, only had an effect on P-gp under higher concentration in Caco-2 cells.. Our results show that EGCG, curcumin, and tannic acid, when combined with doxorubicin, can exert synergism, mediated by a reduced activity of P-gp. This study suggests that polyphenols, by modulating the activity of P-gp, may be used as chemosensitisers. Topics: Antineoplastic Agents; ATP Binding Cassette Transporter, Subfamily B, Member 1; Caco-2 Cells; Catechin; Curcumin; Digitonin; Doxorubicin; Drug Resistance, Multiple; Drug Resistance, Neoplasm; Drug Synergism; Fluoresceins; Humans; Polyphenols; Rhodamine 123; Tannins | 2018 |
Bactericidal activity of curcumin I is associated with damaging of bacterial membrane.
Curcumin, an important constituent of turmeric, is known for various biological activities, primarily due to its antioxidant mechanism. The present study focused on the antibacterial activity of curcumin I, a significant component of commercial curcumin, against four genera of bacteria, including those that are Gram-positive (Staphylococcus aureus and Enterococcus faecalis) and Gram-negative (Escherichia coli and Pseudomonas aeruginosa). These represent prominent human pathogens, particularly in hospital settings. Our study shows the strong antibacterial potential of curcumin I against all the tested bacteria from Gram-positive as well as Gram-negative groups. The integrity of the bacterial membrane was checked using two differential permeabilization indicating fluorescent probes, namely, propidium iodide and calcein. Both the membrane permeabilization assays confirmed membrane leakage in Gram-negative and Gram-positive bacteria on exposure to curcumin I. In addition, scanning electron microscopy and fluorescence microscopy were employed to confirm the membrane damages in bacterial cells on exposure to curcumin I. The present study confirms the broad-spectrum antibacterial nature of curcumin I, and its membrane damaging property. Findings from this study could provide impetus for further research on curcumin I regarding its antibiotic potential against rapidly emerging bacterial pathogens. Topics: Anti-Bacterial Agents; Bacteria; Cell Membrane; Cell Membrane Permeability; Colony Count, Microbial; Curcumin; Flow Cytometry; Fluoresceins; Kinetics; Microbial Sensitivity Tests; Microbial Viability; Microscopy, Fluorescence; Propidium; Spectrometry, Fluorescence | 2015 |
An antifungal mechanism of curcumin lies in membrane-targeted action within Candida albicans.
The aim of this study is to investigate the antifungal mechanism of curcumin. This polyphenolic compound has been used traditionally in Asia for medicinal, culinary, and other purposes. Although antifungal effect of curcumin has been reported, this is the first study for its mode of action underlying disruption of plasma membrane in Candida albicans. The leakage of potassium ion from the fungal cytosol and dissipation in membrane potential was detected by bis-(1,3-dibutylbarbituric acid)trimethine oxonol [DiBAC4 ] staining. We also investigated an increase in membrane permeability in curcumin-treated C. albicans with influx of propidium iodide assay. Fluorescence analysis with 1,6-diphenyl-1,3,5-hexatriene supported the membrane-targeted mechanism of action indicating membrane disruption. On the basis of these results, we studied the effects of curcumin treatment on model membrane to elucidate its antifungal mechanism. Using calcein leakage assays from curcumin-treated large unilamellar vesicles and giant unilamellar vesicles, we found that curcumin has membrane-active mechanism inducing leakage of intracellular component through the flappy membrane. Therefore, this study suggests that curcumin exerts antifungal activity via inducing disruption of fungal plasma membrane. Topics: Antifungal Agents; Barbiturates; Candida albicans; Cell Membrane; Curcumin; Diphenylhexatriene; Fluoresceins; Fluorescence; Isoxazoles; Potassium; Propidium | 2014 |
Inhibition of multidrug resistance proteins MRP1 and MRP2 by a series of alpha,beta-unsaturated carbonyl compounds.
To study the possible interplay between glutathione metabolism of and MRP inhibition by thiol reactive compounds, the interactions of a series of alpha,beta-unsaturated carbonyl compounds with multidrug resistance proteins 1 and 2 (MRP1/ABCC1 and MRP2/ABCC2) were studied. Alpha,beta-unsaturated carbonyl compounds react with glutathione, and therefore either their parent compound or their intracellularly formed glutathione metabolite(s) can modulate MRP-activity. Inhibition was studied in Madin-Darby canine kidney cells stably expressing MRP1 or MRP2, and isolated Sf9-MRP1 or Sf9-MRP2 membrane vesicles. In the latter model system metabolism is not an issue. Of the series tested, three distinct groups could be discriminated based on differences in interplay of glutathione metabolism with MRP1 inhibition. Curcumin inhibited MRP1 transport only in the vesicle model pointing at inhibition by the parent compound. The glutathione conjugates of curcumin also inhibit MRP1 mediated transport, but to a much lesser extent than the parent compound curcumin. In the cellular model system, it was demonstrated that glutathione conjugation of curcumin leads to inactivation of its inhibitory potential. Demethoxycurcumin and bisdemethoxycurcumin inhibited MRP1 in both the vesicle and cellular model pointing at inhibitory potency of at least the parent compound and possibly their metabolites. A second group, including caffeic acid phenethyl ester inhibited MRP1-mediated calcein transport only in the MDCKII-MRP1 cells, and not in the vesicle model indicating that metabolism appeared a prerequisite to generate the active inhibitor. Finally cinnamaldehyde, crotonaldehyde, trans-2-hexanal, citral, and acrolein did not inhibit MRP1. For MRP2, inhibition was much less in both model systems, with the three curcuminoids being the most effective. The results of this study show the importance to study the complex interplay between MRP-inhibitors and their cellular metabolism, the latter affecting the ultimate potential of a compound for cellular MRP-inhibition. Topics: Aldehydes; Animals; Biological Transport; Cell Line; Curcumin; Dogs; Fluoresceins; Humans; Membrane Transport Modulators; Membrane Transport Proteins; Multidrug Resistance-Associated Protein 2; Multidrug Resistance-Associated Proteins; Transfection | 2005 |
Interplay between MRP inhibition and metabolism of MRP inhibitors: the case of curcumin.
The multidrug resistance proteins MRP1 and MRP2 are efflux transporters with broad substrate specificity, including glutathione, glucuronide, and sulfate conjugates. In the present study, the interaction of the dietary polyphenol curcumin with MRP1 and MRP2 and the interplay between curcumin-dependent MRP inhibition and its glutathione-dependent metabolism were investigated using two transport model systems. In isolated membrane vesicles of MRP1- and MRP2-expressing Sf9 cells, curcumin clearly inhibited both MRP1- and MRP2-mediated transport with IC(50) values of 15 and 5 microM, respectively. In intact monolayers of MRP1 overexpressing Madin-Darby canine kidney (MDCKII-MRP1) cells, curcumin also inhibited MRP1-mediated activity, although with a 3-fold higher IC(50) value than the one observed in the vesicle model. Interestingly, MRP2-mediated activity was hardly inhibited in intact monolayers of MRP2-overexpressing MDCKII (MDCKII-MRP2) cells upon exposure to curcumin, whereas the IC(50) value in the vesicle incubations was 5 microM. The difference in extent of inhibition of the MRPs by curcumin in isolated vesicles as compared to intact cells, observed especially for MRP2, was shown to be due to a swift metabolism of curcumin to two glutathione conjugates in the MDCKII cells. Formation of both glutathione conjugates was about six times higher in the MDCKII-MRP2 cells as compared with the MDCKII-MRP1 cells, a phenomenon that could be ascribed to the significantly lower glutathione levels in the cell line. The efflux of both conjugates, identified in the present study as monoglutathionyl curcumin conjugates, was demonstrated to be mediated by both MRP1 and MRP2. From dose-response curves with Sf9 membrane vesicles, glutathionylcurcumin conjugates appeared to be less potent inhibitors of MRP1 and MRP2 than their parent compound curcumin. In conclusion, curcumin clearly inhibits both MRP1- and MRP2-mediated transport, but the glutathione-dependent metabolism of curcumin plays a crucial role in the ultimate level of inhibition of MRP-mediated transport that can be achieved in a cellular system. This complex interplay between MRP inhibition and metabolism of MRP inhibitors, the latter affecting the ultimate potential of a compound for cellular MRP inhibition, may exist not only for a compound like curcumin but also for many other MRP inhibitors presently or previously developed on the basis of vesicle studies. Topics: Animals; ATP Binding Cassette Transporter, Subfamily B; ATP Binding Cassette Transporter, Subfamily B, Member 1; ATP-Binding Cassette Transporters; Baculoviridae; Cell Line; Curcumin; Cyclosporine; Dinitrochlorobenzene; Dose-Response Relationship, Drug; Drug Resistance, Multiple; Ethacrynic Acid; Fluoresceins; Glutathione; Glutathione Transferase; Humans; Propionates; Quinolines; Recombinant Proteins; Spodoptera | 2003 |