Ascaris suum: Oxidative phosphorylation in mitochondria from developing eggs and adult muscle

Rodrick, Gary E.; Long, Susan K. De; Sodeman, William A.; Smith, Daryl L.

doi:10.1016/0014-4894(82)90132-1

Cited by 13 publications

(3 citation statements)

References 35 publications

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“…It is therefore apparent that the mammalian-type electron transport pathway varies widely between mitochondria of different nematodes, as well as between different life-cycle stages of the same nematode (Rodrick, Long, Sodeman & Smith, 1982; probably reflecting an adaptation to the availability of oxygen; hence the correlation of this pathway with worm size and habitat (Fry & Jenkins, 1984 a;Atkinson, 1980). It is unclear whether such variability reflects a dilution of this pathway within the overall mitochondrial population of the worm, or whether this pathway is concentrated in subpopulations of mitochondria or mitochondria associated with certain tissues.…”

Section: Introductionmentioning

confidence: 99%

Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Fry

Beesley

1985

Parasitology

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Cytochemical staining with diaminobenzidine (DAB) has been used to locate cytochrome oxidase activity in mitochondria from major tissues of three intestinal parasitic nematodes, Nippostrongylus brasiliensis, Haemonchus contortus and Ascaridia galli. Deposition of DAB reaction product was uniform and relatively intense in mitochondria from all tissues studied in N. brasiliensis. However, mitochondria from different tissues of H. contortus and A. galli varied considerably in their cytochemical staining, decreasing in the order hypodermis < muscle < gut < reproductive tissue. Mitochondria in gut and reproductive tissue of A. galli possessed little or no cytochrome oxidase activity. These results are compatible with respect to oxygen availability and the extent and localization of the mammalian-type aerobic mitochondrial electron transport pathway in intestinal parasitic nematodes.

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Section: Introductionmentioning

confidence: 99%

Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Fry

Beesley

1985

Parasitology

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“…Besides the problem of bioavailability, the lack of effect on adult worms of inhibitors and uncouplers of oxidative phosphorylation may be due in part to the ability of this life-cycle stage to survive on ATP generated by substrate level phosphorylation alone. Rodrick, Long, Sodeman & Smith (1982) have shown that mitochondrial oxidative phosphorylation capability in adult Ascaris is severely diminished compared to that in embryonated eggs and free-living larvae; similarly, oxidative phosphorylation in mitochondria of adult N. brasiliensis is only some 50 % efficient compared to free-living stages . There would appear therefore to be less of a demand for ATP generated by oxidative phosphorylation in the adult worm, and indeed a large proportion of adult worm mitochondria may naturally assume an 'uncoupled' state.…”

Section: Discussionmentioning

confidence: 99%

Nippostrongylus brasiliensis: the effect of mitochondnal inhibitors on life-cycle stages

Fry

Jenkins

1984

Parasitology

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The effects of mitochondrial inhibitors on the in vitro development of Nippostrongylus brasiliensis have been studied in free-living and parasitic life-cycle stages. Mitochondrial inhibitors were chosen as being representative of established electron transport inhibitors and oxidative phosphorylation inhibitors and uncouplers of the classical mammalian respiratory chain. All mitochondrial inhibitors tested were highly effective in killing or retarding development of free-living stages of N. brasiliensis. Free-living stages were particularly susceptible to such inhibitors upon hatching of embryonated eggs to 1st-stage larvae. Concentrations of inhibitors effective against free-living stages were consistent with their level of inhibition against isolated mitochondria from embryonated eggs and 3rd-stage infective larvae. Results suggest an absolute requirement in the development of free-living stages for the mammalian-like respiratory chain and associated oxidative phosphorylation. Electron transport inhibitors were effective in retarding at least the initial development of 4th-stage larvae to adults, but only antimycin A and azide produced a lasting effect leading to worm death. Oxidative phosphorylation inhibitors and uncouplers were ineffective against developing parasitic stages of N. brasiliensis. Experiments on whole-worm respiration indicated that most electron transport inhibitors were able to penetrate the adult worm, but oxidative phosphorylation inhibitors were without effect on whole-worm respiration. Results suggest that the mammalian-like electron transport chain is a necessary requirement to adult N. brasiliensis, but oxidative phosphorylation in the adult worm may not be required for development and survival in vitro although it could be necessary to support the parasite in vivo.

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“…This procedure was modeled after the original mitochondrial isolation procedure for mammalian tissues (Schneider and Hogeboom, 1950;Hogeboom et al, 1948). However, other media utilizing isoosmotic mannitol with sucrose in a fashion similar to media used by some investigators for the isolation and/or assay of mitochondria from helninths (Papa et al, 1970;Murfitt et al, 1976;Kohler, 1977;Kohler and Bachmann, 1980;Rodrick et al, 1982) blue crab gill (Chen and Lehninger, 1973) and mammalian tissues (Johnson and Lardy, 1967;Greenawalt, 1974) have been used with some molluscan tissues (Holwerda and de Zwaan, 1979;Vorhaben et al, 1980;de Zwaan et al, 1981;Zaba, 1983) Mitochondria prepared in buffer A had P/0 ratios which were character istic for the particular substrate (glutamate, proline, succinate, malate) and showed a high degree of respiratory control with most of these sub strates (Table 2, Figure 4). Of the substrates tested, only pyruvate failed to generate state 3 respiration (Figure 4).…”

Section: Most Procedures For the Isolation Of Mitochondria From The Tmentioning

confidence: 99%

Amino acid catabolism by ribbed mussel (Modiolus demissus) gill tissue: studies on isolated mitochondria and the L-amino acid oxidase

Burcham¹

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Gill tissue from Modiolus demissus has a general L-amino acid oxidase (EC 1.4.3.2) associated with proteinaceous particles sedimenting at 15,000xg. The oxidase is most active between pH 4.5 and pH 5 in citrate buffer with L-a-amino acids having three or more carbons, with no hydroxyl or methyl substitutions for hydrogens on the p-carbons, and no charged groups on the ^-carbon. The apparent K^s for L-leucine and L-ornithine were identical (2.5raM). Glycine, taurine, L-proline, arainooxyacetic acid, L-cycloserine, and EDTA would not act as substrates or inhibitors. The enzyme is reasonably active at pH 4.8 (6-8 pmoles Og consumed/g wet tissue/h at 25®C) and may have a role in the catabolism of some of the amino acids which do not accumulate during hyperosmotic stress.

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Ascaris suum: Oxidative phosphorylation in mitochondria from developing eggs and adult muscle

Cited by 13 publications

References 35 publications

Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Nippostrongylus brasiliensis: the effect of mitochondnal inhibitors on life-cycle stages

Amino acid catabolism by ribbed mussel (Modiolus demissus) gill tissue: studies on isolated mitochondria and the L-amino acid oxidase

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