Characterization of the mitochondria of the free-living nematode, caenorhabditis elegans
References (27)
- et al.
A mutant affecting the heavy chain of myosin in Caenorhabditis elegans
J. molec. Biol.
(1974) - et al.
The colorimetric determination of phosphorus
J. Biol. Chem.
(1925) Determination of protein: a modification of the Loury Method that gives a linear photometric response
Analyt. Biochem.
(1972)- et al.
The catalytic effect of 2,4-dinitrophenol on adenosinetriphosphate hydrolysis by cell particles and soluble enzynmes
J. Biol. Chem.
(1953) - et al.
Restoration of oxidative phosphorylation in ‘non-phosphorylating’ submitochrondrial particles by oligomycin
Biochem. biophys. Res. Commun.
(1965) - et al.
Biochemical studies of skeletal muscle mitochondria—I. Microanalysis of cytochrome content, oxidative and phosphorylative activities of mammalian skeletal muscle mitochondria
Archs Biochem. Biophys.
(1968) - et al.
Inhibition of an electron transport component by Antimycin A
J. Biol. Chem.
(1952) - et al.
Nematode biochemistry—XII. Mitochondria from the free-living nematode Turbatrix aceti
Int. J. Biochem.
(1970) Studies on the phosphorylation in Ascaris Mitochondria
Adenine Triphosphatase activity in Ascaris muscle mitochondria
Comp. Biochem. Physiol.
(1974)
On Cytochrome oxidase—I. The extinction coefficients of cytochrome and cytochrome
Biochim. biophys. Acta
A method for the simultaneous quantitative estimation of cytochomes a, b, c, and in mitochondria
Archs Biochem. Biophys.
The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation
Biochemistry
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Deficiencies in mitochondrial dynamics sensitize Caenorhabditis elegans to arsenite and other mitochondrial toxicants by reducing mitochondrial adaptability
2017, ToxicologyCitation Excerpt :To address this knowledge gap, we screened ten known and suspected mitochondrial toxicants (2,4-dinitrophenol (DNP), acetaldehyde, acrolein, aflatoxin B1 (AfB1), arsenite, cadmium, cisplatin, doxycycline, paraquat, rotenone) for exacerbation of mitochondrial dysfunction in fission (drp-1)-, fusion (fzo-1, eat-3 (MFN2, OPA1 homologs, respectively))-, and mitophagy (pink-1, pdr-1 (PINK1, PARK2 homologs, respectively))-deficient Caenorhabditis elegans. C. elegans is a powerful in vivo model to study mitochondrial gene-environment interactions, as mitochondrial function and many biochemical pathways are well conserved with humans (Maglioni and Ventura, 2016; Murfitt et al., 1976; O'Riordan and Burnell, 1989; Okimoto et al., 1992; Tsang and Lemire, 2003; Zhang et al., 2013). In vivo analysis is important, as mitochondrial function is dependent upon intercellular signals, many of which arise from diverse tissues and cell types, and are lost in in vitro models (McBride et al., 2006).
Infertility and recurrent miscarriage with complex II deficiency-dependent mitochondrial oxidative stress in animal models
2016, Mechanisms of Ageing and DevelopmentCitation Excerpt :On the other hand, TNFα/TNFR1 binding signal requires the TNFR1-associated death domain (TRADD)-composed complex I and II formation that activates distinct downstream survival and apoptotic signaling pathways, respectively (Jiang et al., 1999; Hsu et al., 1995). Apoptosis-inducible complex II is composed of TRADD, FADD and caspase-8, and is formed after TNFR1 receptosome endocytosis leading to caspase-8 activation as mentioned below (Schneider-Brachert et al., 2004; Micheau and Tschopp, 2003; Lin et al., 1999). Given this, the both TNFα/TNFR1 and FasL/Fas -mediated apoptosis are similarly induced by the caspase-8-dependent modulations.
Model animals for the study of oxidative stress from complex II
2013, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :It closely parallels its mammalian counterpart in its metabolism and structure. C. elegans mitochondrial DNA (mtDNA) is similar in size and gene content to that of humans [32,33]. The mev-1 mutant was isolated based upon its hypersensitivity to the ROS-generating chemical methyl viologen [27].
Utility of Caenorhabditis elegans in high throughput neurotoxicological research
2010, Neurotoxicology and TeratologyCitation Excerpt :Most ROS (e.g., superoxide anion, hydroxyl radical) are produced by incomplete reduction of oxygen at the electron transport chain (ETC) in the mitochondria [22], leading to oxidation and loss of function of proteins, lipids, and DNA [61]. The structure, metabolism, and bioenergetics of the C. elegans mitochondria are very similar to those of their human counterparts [48], contributing to their usefulness in investigating the mechanisms by which oxidative stress induces toxicity. Furthermore, the oxidative stress response in worms is highly conserved with mammals, especially the regulation of expression of detoxifying and antioxidant enzymes.
Chapter 2 Worm Watching: Imaging Nervous System Structure and Function in Caenorhabditis elegans
2009, Advances in GeneticsCitation Excerpt :For high‐resolution imaging studies such as measuring presynaptic protein distributions, the chief approach has been to pharmacologically immobilize animals and image them sandwiched between a coverslip and a hydrated agarose pad. Typical paralytic agents include the anesthetic phenoxypropanol (Schuske et al., 2003; Sulston and Horvitz, 1977), the mitochondrial poison azide (Murfitt et al., 1976; Nonet, 1999; Nurrish et al., 1999), the nAChR agonist levamisole/tetramisole (Burbea et al., 2002; Juo and Kaplan, 2004; Lewis et al., 1980a,b), and the myosin blocker 2,3 butanedione monoxime (Dittman and Kaplan, 2006; Sieburth et al., 2005). Worms immobilized with these agents can be imaged for brief periods (10–30 min) while their neurons remain relatively healthy.
The role of the electron transport SDHC gene on lifespan and cancer
2007, Mitochondrion