Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Fry, Mitchell; Beesley, Julian E.

doi:10.1017/s003118200004909x

Cited by 17 publications

(3 citation statements)

References 11 publications

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“…Stoichiometries of cytochromes in mitochondria from N. brasiliensis and A. galli muscle and gut + reproductive tissue indicate a descending rank order with respect to the relative content of cytochrome aa3, and this agrees with previous cytochemical observations (Fry & Beesley, 1985). It also matches those percentages of total electron Table 1.…”

Section: Discussionsupporting

confidence: 89%

Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli

Paget

Fry

Lloyd

1988

Biochemical Journal

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1. Mitochondria isolated from the gut-dwelling nematodes Nippostrongylus brasiliensis and Ascaridia galli (muscle and gut + reproductive tissue) were examined for cytochromes, and it was observed that N. brasiliensis and A. galli muscle tissue mitochondria contained a-, b- and c-type cytochromes, but their stoichiometries were quite different (1:2:1.9 and 1:11.4:13.6 respectively); A. galli gut + reproductive-tissue mitochondria, however, only contained b and c cytochromes, in a ratio of 1:0.8. 2. CO difference spectra showed the presence of CO-reacting b-type cytochrome(s) in all three types of mitochondria; the fast-reacting species comprised 30, 44 and 39% of the total in N. brasiliensis, A. galli muscle and A. galli gut + reproductive-tissue mitochondria respectively. 3. Cytochrome aa3 was observed in N. brasiliensis mitochondria and in those from A. galli muscle, but was below the level of detectability (less than 0.005 nmol/mg of protein) for A. galli gut + reproductive-tissue mitochondria. 4. Photochemical action spectra for the reversal of CO inhibition of the endogenous respiration of whole worms (at 24 microM- and 40 microM-O2 respectively for N. brasiliensis and A. galli) gave maxima at 598 and 542-543 nm, corresponding to the alpha- and beta-absorption maxima of cytochrome aa3, and at 567 nm (b-type cytochrome) for both worms. These results suggest that cytochrome aa3 is the major functional oxidase in N. brasiliensis, whereas the CO-reacting b-type cytochrome dominates in A. galli.

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Section: Discussionsupporting

confidence: 89%

Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli

Paget

Fry

Lloyd

1988

Biochemical Journal

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“…The low environmental oxygen concentrations experienced by A. galli in situ (0-20 LM-02; Atkinson, 1980) and the disproportionate concentration of cytochrome oxidase-positive mitochondria within peripheral tissues of this worm (Fry & Beesley, 1985) suggests that, in vivo, the cortex tissues (including the gut plus reproductive tissues) of the worm are at best supplied with oxygen at extremely low levels. Comparisons of the apparent Km values for oxygen between whole worms utilizing endogenous substrates and uncoupled isolated mitochondria provided with succinate or L-oc-glycero-phosphate shows a more-than-20-fold discrepancy; this suggests the existence of a substantial oxygen gradient through the worm.…”

Section: Discussionmentioning

confidence: 99%

The O2-dependence of respiration and H2O2 production in the parasitic nematode Ascaridia galli

Paget¹,

Fry

Lloyd³

1988

Biochemical Journal

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1. Respiration in the parasitic nematode worm Ascaridia galli was inhibited at O2 concentrations in excess of 255 microM, and an apparent Km,O2 of 174 microM was determined. 2. Mitochondria-enriched fractions isolated from the tissues of A. galli have much lower apparent Km,O2 values (approx. 5 microM). They produce H2O2 in the energized state; higher rates of H2O2 production were observed in the presence of the uncoupler carbonyl cyanide m-chlorophenylhydrazone. 3. Antimycin A inhibited respiration in muscle tissue mitochondria by 10%, but had no effect on respiration in gut + reproductive tissue mitochondria; the major portion of respiration in both types of mitochondria could be attributed to an alternative electron-transport pathway. 4. o-Hydroxydiphenyl, an inhibitor of alternative electron-transport pathways, inhibits respiration by 98% and completely inhibits the production of H2O2 in gut-plus-reproductive-tissue mitochondria; respiration and H2O2 production in muscle tissue mitochondria were inhibited by 90 and 86% respectively. 5. Another inhibitor of alternative electron transport, salicylhydroxamic acid, had the same effect as o-hydroxydiphenyl on H2O2 production and respiration in gut-plus-reproductive-tissue mitochondria. However, its effect on muscle tissue mitochondria was complex; a low concentration (0.35 mM) stimulated H2O2 production, whereas 3 mM inhibited respiration by 87% and prevented H2O2 production completely. 6. The similarities between the apparent Km,O2 values for H2O2 production and respiration in muscle mitochondria and in gut-plus-reproductive-tissue mitochondria suggests that the site of H2O2 production on the alternative electron-transport chain is cytochrome 'o'. 7. These results are discussed in relation to potential O2 toxicity in A. galli.

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“…Giemsa and acid-fuchsin and other specifie stains have been used to elucidate the internai structure of the bursa, genital cone, and spicules in temporary and permanently mounted specimens of sorne strongylate nematodes (Stringfellow, 1969(Stringfellow, , 1971. Histochemical staining has also been widely applied in elucidating biochemical activity in nematode tissue (Maki and Yanagisawa, 1980;Fry and Beesley, 1985). However, specimens are most often studied as wholemounts in a standard clearing agent such as glycerine, lactophenol, or phenol-alcohol (Pritchard and Kruse, 1982).…”

mentioning

confidence: 99%

Carmine-Propionic Acid Stain for Elucidation of Fine Cellular Structure in Nematodes

Khrustalev¹,

Hoberg²

1996

The Journal of Parasitology

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Cytochemical localization of cytochrome oxidase in tissues of parasitic nematodes

Cited by 17 publications

References 11 publications

Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli

Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli

The O2-dependence of respiration and H2O2 production in the parasitic nematode Ascaridia galli

Carmine-Propionic Acid Stain for Elucidation of Fine Cellular Structure in Nematodes

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