Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase
Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inh...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Balyan, Rajiv [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Schlagwörter: |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Ambiguous information and dilation: An experiment - Shishkin, Denis ELSEVIER, 2023, a journal of molecular and biochemical toxicology, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:240 ; year:2015 ; day:5 ; month:10 ; pages:208-218 ; extent:11 |
| Links: |
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| DOI / URN: |
10.1016/j.cbi.2015.08.011 |
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ELV029279461 |
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| 245 | 1 | 0 | |a Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase |
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| 520 | |a Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. | ||
| 520 | |a Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. | ||
| 650 | 7 | |a SK-MEL-28 |2 Elsevier | |
| 650 | 7 | |a Quinone |2 Elsevier | |
| 650 | 7 | |a Melanoma |2 Elsevier | |
| 650 | 7 | |a GST |2 Elsevier | |
| 650 | 7 | |a Luteolin |2 Elsevier | |
| 650 | 7 | |a Cancer |2 Elsevier | |
| 650 | 7 | |a Glutathione |2 Elsevier | |
| 700 | 1 | |a Kudugunti, Shashi K. |4 oth | |
| 700 | 1 | |a Hamad, Hamzah A. |4 oth | |
| 700 | 1 | |a Yousef, Mohammad S. |4 oth | |
| 700 | 1 | |a Moridani, Majid Y. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Shishkin, Denis ELSEVIER |t Ambiguous information and dilation: An experiment |d 2023 |d a journal of molecular and biochemical toxicology |g Amsterdam [u.a.] |w (DE-627)ELV009268340 |
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10.1016/j.cbi.2015.08.011 doi GBVA2015020000007.pica (DE-627)ELV029279461 (ELSEVIER)S0009-2797(15)30040-5 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 330 VZ 31.00 bkl 83.10 bkl Balyan, Rajiv verfasserin aut Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. SK-MEL-28 Elsevier Quinone Elsevier Melanoma Elsevier GST Elsevier Luteolin Elsevier Cancer Elsevier Glutathione Elsevier Kudugunti, Shashi K. oth Hamad, Hamzah A. oth Yousef, Mohammad S. oth Moridani, Majid Y. oth Enthalten in Elsevier Science Shishkin, Denis ELSEVIER Ambiguous information and dilation: An experiment 2023 a journal of molecular and biochemical toxicology Amsterdam [u.a.] (DE-627)ELV009268340 volume:240 year:2015 day:5 month:10 pages:208-218 extent:11 https://doi.org/10.1016/j.cbi.2015.08.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.00 Mathematik: Allgemeines VZ 83.10 Wirtschaftstheorie: Allgemeines VZ AR 240 2015 5 1005 208-218 11 045F 570 |
| spelling |
10.1016/j.cbi.2015.08.011 doi GBVA2015020000007.pica (DE-627)ELV029279461 (ELSEVIER)S0009-2797(15)30040-5 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 330 VZ 31.00 bkl 83.10 bkl Balyan, Rajiv verfasserin aut Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. SK-MEL-28 Elsevier Quinone Elsevier Melanoma Elsevier GST Elsevier Luteolin Elsevier Cancer Elsevier Glutathione Elsevier Kudugunti, Shashi K. oth Hamad, Hamzah A. oth Yousef, Mohammad S. oth Moridani, Majid Y. oth Enthalten in Elsevier Science Shishkin, Denis ELSEVIER Ambiguous information and dilation: An experiment 2023 a journal of molecular and biochemical toxicology Amsterdam [u.a.] (DE-627)ELV009268340 volume:240 year:2015 day:5 month:10 pages:208-218 extent:11 https://doi.org/10.1016/j.cbi.2015.08.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.00 Mathematik: Allgemeines VZ 83.10 Wirtschaftstheorie: Allgemeines VZ AR 240 2015 5 1005 208-218 11 045F 570 |
| allfields_unstemmed |
10.1016/j.cbi.2015.08.011 doi GBVA2015020000007.pica (DE-627)ELV029279461 (ELSEVIER)S0009-2797(15)30040-5 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 330 VZ 31.00 bkl 83.10 bkl Balyan, Rajiv verfasserin aut Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. SK-MEL-28 Elsevier Quinone Elsevier Melanoma Elsevier GST Elsevier Luteolin Elsevier Cancer Elsevier Glutathione Elsevier Kudugunti, Shashi K. oth Hamad, Hamzah A. oth Yousef, Mohammad S. oth Moridani, Majid Y. oth Enthalten in Elsevier Science Shishkin, Denis ELSEVIER Ambiguous information and dilation: An experiment 2023 a journal of molecular and biochemical toxicology Amsterdam [u.a.] (DE-627)ELV009268340 volume:240 year:2015 day:5 month:10 pages:208-218 extent:11 https://doi.org/10.1016/j.cbi.2015.08.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.00 Mathematik: Allgemeines VZ 83.10 Wirtschaftstheorie: Allgemeines VZ AR 240 2015 5 1005 208-218 11 045F 570 |
| allfieldsGer |
10.1016/j.cbi.2015.08.011 doi GBVA2015020000007.pica (DE-627)ELV029279461 (ELSEVIER)S0009-2797(15)30040-5 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 330 VZ 31.00 bkl 83.10 bkl Balyan, Rajiv verfasserin aut Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. SK-MEL-28 Elsevier Quinone Elsevier Melanoma Elsevier GST Elsevier Luteolin Elsevier Cancer Elsevier Glutathione Elsevier Kudugunti, Shashi K. oth Hamad, Hamzah A. oth Yousef, Mohammad S. oth Moridani, Majid Y. oth Enthalten in Elsevier Science Shishkin, Denis ELSEVIER Ambiguous information and dilation: An experiment 2023 a journal of molecular and biochemical toxicology Amsterdam [u.a.] (DE-627)ELV009268340 volume:240 year:2015 day:5 month:10 pages:208-218 extent:11 https://doi.org/10.1016/j.cbi.2015.08.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.00 Mathematik: Allgemeines VZ 83.10 Wirtschaftstheorie: Allgemeines VZ AR 240 2015 5 1005 208-218 11 045F 570 |
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bioactivation of luteolin by tyrosinase selectively inhibits glutathione s-transferase |
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Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase |
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Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. |
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Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. |
| abstract_unstemmed |
Glutathione S-transferase (GST) plays a significant role in the metabolism and detoxification of drugs used in treatment of melanoma, resulting in a decrease in drug efficacy. Tyrosinase is an abundant enzyme found in melanoma. In this study, we used a tyrosinase targeted approach to selectively inhibit GST. In the presence of tyrosinase, luteolin (10 μM) showed 87% GST inhibition; whereas in the absence of tyrosinase, luteolin led to negligible GST inhibition. With respect to GSH, both luteolin-SG conjugate and luteolin-quinone inhibited ≥90% of GST activity via competitive reversible and irreversible mixed mechanisms with Ki of 0.74 μM and 0.02 μM, respectively. With respect to CDNB, the luteolin-SG conjugate inhibited GST activity via competitive reversible mechanism and competitively with Ki of 0.58 μM, whereas luteolin-quinone showed irreversible mixed inhibition of GST activity with Ki of 0.039 μM. Luteolin (100 μM) inhibited GST in mixed manner with Ki of 53 μM with respect to GSH and non-competitively with respect to CDNB with Ki of 38 μM. Luteolin, at a concentration range of 5–80 μM, exhibited 78–99% GST inhibition in human SK-MEL-28 cell homogenate. Among the 3 species of intact luteolin, luteolin-SG conjugate, and luteoline-quinone, only the latter two have potential as drugs with Ki < 1 μM, which is potentially achievable in-vivo as therapeutic agents. The order of GST inhibition was luteolin-quinone >> luteolin-SG conjugate >>> luteolin. In summary, our results suggest that luteolin was bioactivated by tyrosinase to form a luteolin-quinone and luteolin-glutathione conjugate, which inhibited GST. For the first time, in addition to intracellular GSH depletion, we demonstrate that luteolin acts as a selective inhibitor of GST in the presence of tyrosinase. Such strategy could potentially be used to selectively inhibit GST, a drug detoxifying enzyme, in melanoma cells. |
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| title_short |
Bioactivation of luteolin by tyrosinase selectively inhibits glutathione S-transferase |
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https://doi.org/10.1016/j.cbi.2015.08.011 |
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Kudugunti, Shashi K. Hamad, Hamzah A. Yousef, Mohammad S. Moridani, Majid Y. |
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Kudugunti, Shashi K. Hamad, Hamzah A. Yousef, Mohammad S. Moridani, Majid Y. |
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