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Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo

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Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo. / Lindenmeyer, Maja T; García-Piñeres, Alfonso J; Castro, Victor; Merfort, Irmgard.

in: ANAL BIOCHEM, Jahrgang 328, Nr. 2, 15.05.2004, S. 147-54.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Lindenmeyer, MT, García-Piñeres, AJ, Castro, V & Merfort, I 2004, 'Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo', ANAL BIOCHEM, Jg. 328, Nr. 2, S. 147-54. https://doi.org/10.1016/j.ab.2004.01.021

APA

Lindenmeyer, M. T., García-Piñeres, A. J., Castro, V., & Merfort, I. (2004). Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo. ANAL BIOCHEM, 328(2), 147-54. https://doi.org/10.1016/j.ab.2004.01.021

Vancouver

Lindenmeyer MT, García-Piñeres AJ, Castro V, Merfort I. Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo. ANAL BIOCHEM. 2004 Mai 15;328(2):147-54. https://doi.org/10.1016/j.ab.2004.01.021

Bibtex

@article{0a9d7aef67b94f2db5f1f5da305c6c7c,
title = "Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo",
abstract = "Reporter enzymes such as firefly luciferase or beta-galactosidase of Escherichia coli are frequently used to study transcriptional activity of genes and to investigate the effects of novel compounds on gene or transcription factor activity. It is generally assumed that the activity of these enzymes is unaffected by the treatment conditions. Therefore, this factor is not considered when interpreting the data obtained. Biologically active compounds such as sesquiterpene lactones (SLs) have also been tested in reporter gene assays for their influence on gene expression. Here we show in in vitro and ex vivo experiments that SLs inhibit firefly luciferase activity probably by direct targeting of the enzyme while beta-galactosidase remains almost completely unaffected. The loss of luciferase activity after SL treatment could be an effect of their sulfhydryl-modifying potency and the subsequent alteration of the enzyme's tertiary structure. These results demonstrate that the effect of the test substance on the reporter enzyme used should be taken into consideration when the transcriptional effect of novel compounds is investigated.",
keywords = "Animals, Cells, Cultured, Dose-Response Relationship, Drug, Enzyme Inhibitors, Escherichia coli, Genes, Reporter, Lactones, Luciferases, NF-kappa B, Sesquiterpenes, Statistics as Topic, Time Factors, Transcription, Genetic, beta-Galactosidase, Journal Article, Research Support, Non-U.S. Gov't",
author = "Lindenmeyer, {Maja T} and Garc{\'i}a-Pi{\~n}eres, {Alfonso J} and Victor Castro and Irmgard Merfort",
year = "2004",
month = may,
day = "15",
doi = "10.1016/j.ab.2004.01.021",
language = "English",
volume = "328",
pages = "147--54",
journal = "ANAL BIOCHEM",
issn = "0003-2697",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Sesquiterpene lactones inhibit luciferase but not beta-galactosidase activity in vitro and ex vivo

AU - Lindenmeyer, Maja T

AU - García-Piñeres, Alfonso J

AU - Castro, Victor

AU - Merfort, Irmgard

PY - 2004/5/15

Y1 - 2004/5/15

N2 - Reporter enzymes such as firefly luciferase or beta-galactosidase of Escherichia coli are frequently used to study transcriptional activity of genes and to investigate the effects of novel compounds on gene or transcription factor activity. It is generally assumed that the activity of these enzymes is unaffected by the treatment conditions. Therefore, this factor is not considered when interpreting the data obtained. Biologically active compounds such as sesquiterpene lactones (SLs) have also been tested in reporter gene assays for their influence on gene expression. Here we show in in vitro and ex vivo experiments that SLs inhibit firefly luciferase activity probably by direct targeting of the enzyme while beta-galactosidase remains almost completely unaffected. The loss of luciferase activity after SL treatment could be an effect of their sulfhydryl-modifying potency and the subsequent alteration of the enzyme's tertiary structure. These results demonstrate that the effect of the test substance on the reporter enzyme used should be taken into consideration when the transcriptional effect of novel compounds is investigated.

AB - Reporter enzymes such as firefly luciferase or beta-galactosidase of Escherichia coli are frequently used to study transcriptional activity of genes and to investigate the effects of novel compounds on gene or transcription factor activity. It is generally assumed that the activity of these enzymes is unaffected by the treatment conditions. Therefore, this factor is not considered when interpreting the data obtained. Biologically active compounds such as sesquiterpene lactones (SLs) have also been tested in reporter gene assays for their influence on gene expression. Here we show in in vitro and ex vivo experiments that SLs inhibit firefly luciferase activity probably by direct targeting of the enzyme while beta-galactosidase remains almost completely unaffected. The loss of luciferase activity after SL treatment could be an effect of their sulfhydryl-modifying potency and the subsequent alteration of the enzyme's tertiary structure. These results demonstrate that the effect of the test substance on the reporter enzyme used should be taken into consideration when the transcriptional effect of novel compounds is investigated.

KW - Animals

KW - Cells, Cultured

KW - Dose-Response Relationship, Drug

KW - Enzyme Inhibitors

KW - Escherichia coli

KW - Genes, Reporter

KW - Lactones

KW - Luciferases

KW - NF-kappa B

KW - Sesquiterpenes

KW - Statistics as Topic

KW - Time Factors

KW - Transcription, Genetic

KW - beta-Galactosidase

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.ab.2004.01.021

DO - 10.1016/j.ab.2004.01.021

M3 - SCORING: Journal article

C2 - 15113690

VL - 328

SP - 147

EP - 154

JO - ANAL BIOCHEM

JF - ANAL BIOCHEM

SN - 0003-2697

IS - 2

ER -