Control of anesthetic response in C. elegans

Kayser, Bernhard; Rajaram, Shantadurga; Thomas, Susan M.; Morgan, Philip G.; Sedensky, Margaret M.

doi:10.1016/s0378-4274(98)00204-5

Cited by 10 publications

(5 citation statements)

References 13 publications

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“…The fact that sodium azide inhibits both cytochrome c oxidase (Duncan and Mackler 1966) and adenosine triphosphate (ATP) synthase (Herweijer et al 1985;Van der Bend et al 1985) makes the ability of C elegans to survive this chemically induced hypoxic state quite remarkable. Although other anesthetics have been tested (for examples see Kayser et al 1998;van Swinderen et al 1998), the question of the mechanism by which C elegans survives azide exposure remains unanswered.…”

Section: Introductionmentioning

confidence: 99%

Exposure to the metabolic inhibitor sodium azide induces stress protein expression and thermotolerance in the nematode Caenorhabditis elegans

Massie

Lapoczka²,

Boggs³

et al. 2003

Cell Stress Chaper

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Historically, sodium azide has been used to anesthetize the nematode Caenorhabditis elegans; however, the mechanism by which it survives this exposure is not understood. In this study, we report that exposure of wild-type C elegans to 10 mM sodium azide for up to 90 minutes confers thermotolerance (defined as significantly increased survival probability [SP] at 37 degrees C) on the animal. In addition, sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed enhanced Hsp70 expression, whereas Western blot analysis revealed the induction of Hsp16. We also tested the only known C elegans Hsp mutant def-21 (codes for Hsp90), which constitutively enters the stress-resistant state known as the dauer larvae. Daf-21 mutants also acquire sodium azide-induced thermotolerance, whereas 3 non-Hsp, constitutive dauer-forming mutants exhibited a variable response to azide exposure. We conclude that the ability of C elegans to survive exposure to azide is associated with the induction of at least 2 stress proteins.

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Section: Introductionmentioning

confidence: 99%

Exposure to the metabolic inhibitor sodium azide induces stress protein expression and thermotolerance in the nematode Caenorhabditis elegans

Massie

Lapoczka²,

Boggs³

et al. 2003

Cell Stress Chaper

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“…1,2 While reversible immobility produced by volatile anesthetics (VAs) occurs at concentrations higher than minimum alveolar concentration in humans, this end point obeys the Meyer-Overton rule, exhibits stereoselectivity, is not affected by nonimmobilizers, and fits well with the LC 50 /EC 50 ratio seen in mammals for VAs. 3 Most importantly, the molecular mechanisms that determine this end point control the anesthetic behavior of other organisms, including humans. 4–6…”

mentioning

confidence: 99%

Isoflurane Selectively Inhibits Distal Mitochondrial Complex I in Caenorhabditis Elegans

Kayser¹,

Suthammarak²,

Morgan

et al. 2011

Anesthesia &Amp; Analgesia

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BACKGROUND Complex I of the electron transport chain (ETC) is a possible target of volatile anesthetics (VAs). Complex I enzymatic activities are inhibited by VAs, and dysfunction of complex I can lead to hypersensitivity to VAs in worms and in people. Mutant analysis in Caenorhabditis (C.) elegans suggests that VAs may specifically interfere with complex I function at the binding site for its substrate ubiquinone. We hypothesized that isoflurane inhibits electron transport by competing with ubiquinone for binding to complex I. METHODS Wildtype and mutant C. elegans were used to study the effects of isoflurane on isolated mitochondria. Enzymatic activities of the ETC were assayed and dose-response curves determined using established techniques. Two-dimensional native gels of mitochondrial proteins were performed after exposure of mitochondria to isoflurane. RESULTS Complex I is the most sensitive component of the ETC to isoflurane inhibition; however the proximal portion of complex I (the flavoprotein) is relatively insensitive to isoflurane. Isoflurane and quinone do not compete for a common binding site on complex I. The absolute rate of complex I enzymatic activity in vitro does not predict immobilization of the animal by isoflurane. Isoflurane had no measurable effect on stability of mitochondrial supercomplexes. Reduction of ubiquinone by complex I displayed positive cooperative kinetics not disrupted by isoflurane. CONCLUSIONS Isoflurane directly inhibits complex I at a site distal to the flavoprotein subcomplex. However, we have excluded our original hypothesis that isoflurane and ubiquinone compete for a common hydrophobic binding site on complex I. In addition, immobilization of the nematode by isoflurane is not due to limiting absolute amounts of complex I electron transport as measured in isolated mitochondria.

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“…Low survival rates and complex microfabrication characterize other immobilization techniques. 13,15,16 However, the ALINK technique allows the same task to be completed in a more elegant manner. As shown in Fig.…”

Section: Laser Ablation For Lf Removalmentioning

confidence: 99%

“…Unlike other model animals, such as zebrafish or laboratory rats, the limited tools available impede the advanced work conducted on C. elegans. When worms must undergo surgery or be individually traced, only a few measures can be used to constrain them, such as microstructures, 13,14 CO 2 , 15 or anesthetics, 16,17 which may cause physical injury or neural damage. Optogenetically modified worms have shown potential for manipulation.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of the nematode caenorhabditis elegans with addressable light-induced heat knockdown (ALINK)

Chuang

Chen

et al. 2013

Lab Chip

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Caenorhabditis (C.) elegans is a model animal used in genetics, neuroscience, and developmental biology. Researchers often immobilize squirming worms to obtain high-quality images for analysis. However, current methods usually require physical contact or anesthetics. This can cause injuries to worm bodies or neuron disturbances. This study presents an alternative technique, called addressable light-induced heat knockdown (ALINK), to effectively immobilize worms by using light-induced sublethal heat. A microchip composed of an indium-tin-oxide (ITO) glass plate and an ITO glass plate coated with a photoconductive layer (a-Si:H) was produced. Worms to be immobilized were immersed in a liquid medium and sandwiched between the two plates. When the worms were irradiated with a focused laser beam in the presence of electric fields (referred to as an optoelectric treatment), the optoelectric effect heated the liquid medium. The neural functions of the worms shut down temporarily when a critical temperature (>31 °C) was reached. Their neural functions resumed after the heat source was removed. A temperature above 37 °C killed all worms. Using short-wavelength light reduced the worms' recovery time. An equivalent circuit was modeled to predict the operating modes, and an optoelectric treatment with a high-concentration medium enhanced rapid heating. A safe operating range (20 Vpp (peak-to-peak voltage), 100 kHz to 10 MHz, 31 to 37 °C) to induce heat knockdown (KD) was also investigated. The results show that the heat KD was well controlled, autonomous, and reversible. This technique can be used for worm immobilization.

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Control of anesthetic response in C. elegans

Cited by 10 publications

References 13 publications

Exposure to the metabolic inhibitor sodium azide induces stress protein expression and thermotolerance in the nematode Caenorhabditis elegans

Exposure to the metabolic inhibitor sodium azide induces stress protein expression and thermotolerance in the nematode Caenorhabditis elegans

Isoflurane Selectively Inhibits Distal Mitochondrial Complex I in Caenorhabditis Elegans

Immobilization of the nematode caenorhabditis elegans with addressable light-induced heat knockdown (ALINK)

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