Effects of Diethyl Ether and Halothane on Firefly Luciferin Bioluminescence

Ueda, Issaku

doi:10.1097/00000542-196509000-00003

Cited by 43 publications

(26 citation statements)

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“…As shown in Fig. 10, structurally unrelated compounds such as halothane [101], fatty acids [102,103], pifithrin-a [104], lipoic acid [105], N-pyridin-2-ylbenzamide analogues [106], and 2-phenylbenzothiazole analogue [107] also inhibit luciferase activity. In cell-based luciferase reporter assays, the stabilization of luciferase by inhibitors results in the counterintuitive phenomenon of signal stimulation [108,109].…”

Section: Inhibitors Of Firefly Luciferasementioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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Firefly luciferase is a member of the acyl-adenylate/thioester-forming superfamily of enzymes and catalyzes the oxidation of firefly luciferin with molecular oxygen to emit light. Knowledge of the luminescence mechanism catalyzed by firefly luciferase has been gathered, leading to the discovery of a novel catalytic function of luciferase. Recently, we demonstrated that firefly luciferase has a catalytic function of fatty acyl-CoA synthesis from fatty acids in the presence of ATP, Mg(2+) and coenzyme A. Based on identification of fatty acyl-CoA genes in firefly, Drosophila, and non-luminous click beetles, we then proposed that the evolutionary origin of firefly luciferase is a fatty acyl-CoA synthetase in insects. Further, we succeeded in converting the fatty acyl-CoA synthetase of non-luminous insects into functional luciferase showing luminescence activity by site-directed mutagenesis.

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Section: Inhibitors Of Firefly Luciferasementioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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“…In the 1980s, however, after the discovery of an effect of anesthetics on firefly luciferase (32), Franks and Lieb (33) first showed enzyme inhibition by GAs (34) and then differences in potency between GAs enantiomers (35,36). This finding pointed to a protein site of action, likely a weakly chiral hydrophobic pocket (37)(38)(39).…”

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Electron spin changes during general anesthesia in Drosophila

Turin

Skoulakis

Horsfield

2014

Proc. Natl. Acad. Sci. U.S.A.

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We show that the general anesthetics xenon, sulfur hexafluoride, nitrous oxide, and chloroform cause rapid increases of different magnitude and time course in the electron spin content of Drosophila. With the exception of CHCl 3 , these changes are reversible. Anesthetic-resistant mutant strains of Drosophila exhibit a different pattern of spin responses to anesthetic. In two such mutants, the spin response to CHCl 3 is absent. We propose that these spin changes are caused by perturbation of the electronic structure of proteins by general anesthetics. Using density functional theory, we show that general anesthetics perturb and extend the highest occupied molecular orbital of a nine-residue α-helix. The calculated perturbations are qualitatively in accord with the Meyer-Overton relationship and some of its exceptions. We conclude that there may be a connection between spin, electron currents in cells, and the functioning of the nervous system.

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“…In a first part, we sought to investigate if a direct inhibitory effect, as was already described for halothane on pure luciferase enzyme, could be detected for regularly used volatile mouse anesthetics in intact cells as well [30]. Fluc expressing R1M cells were allowed to adhere in small culture flasks overnight.…”

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confidence: 99%

Inhibition of Firefly Luciferase by General Anesthetics: Effect on In Vitro and In Vivo Bioluminescence Imaging

et al. 2012

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Bioluminescence imaging is routinely performed in anesthetized mice. Often isoflurane anesthesia is used because of its ease of use and fast induction/recovery. However, general anesthetics have been described as important inhibitors of the luciferase enzyme reaction.AimTo investigate frequently used mouse anesthetics for their direct effect on the luciferase reaction, both in vitro and in vivo.Materials and Methodsisoflurane, sevoflurane, desflurane, ketamine, xylazine, medetomidine, pentobarbital and avertin were tested in vitro on luciferase-expressing intact cells, and for non-volatile anesthetics on intact cells and cell lysates. In vivo, isoflurane was compared to unanesthetized animals and different anesthetics. Differences in maximal photon emission and time-to-peak photon emission were analyzed.ResultsAll volatile anesthetics showed a clear inhibitory effect on the luciferase activity of 50% at physiological concentrations. Avertin had a stronger inhibitory effect of 80%. For ketamine and xylazine, increased photon emission was observed in intact cells, but this was not present in cell lysate assays, and was most likely due to cell toxicity and increased cell membrane permeability. In vivo, the highest signal intensities were measured in unanesthetized mice and pentobarbital anesthetized mice, followed by avertin. Isoflurane and ketamine/medetomidine anesthetized mice showed the lowest photon emission (40% of unanesthetized), with significantly longer time-to-peak than unanesthetized, pentobarbital or avertin-anesthetized mice. We conclude that, although strong inhibitory effects of anesthetics are present in vitro, their effect on in vivo BLI quantification is mainly due to their hemodynamic effects on mice and only to a lesser extent due to the direct inhibitory effect.

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Effects of Diethyl Ether and Halothane on Firefly Luciferin Bioluminescence

Cited by 43 publications

References 0 publications

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Electron spin changes during general anesthesia in Drosophila

Inhibition of Firefly Luciferase by General Anesthetics: Effect on In Vitro and In Vivo Bioluminescence Imaging

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