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  • 1
    Electronic Resource
    Electronic Resource
    Humoral suppression inTrypanosoma cruzi infection in relation to the timing of antigen presentation (1980)
    Springer
    Parasitology research 64 (1980), S. 85-93 
    Details
    ISSN: 1432-1955
    Keywords: Trypanosoma cruzi ; Immunosuppression ; Immunenhancement ; Mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract (CBA×C57 B1/10)F1 mice infected intraperitoneally with 100 parasites ofTrypanosoma cruzi strain Y developed an infection with acute and chronic phases. Humoral suppression to sheep red blood cells was evident in both phases but enhancement of the response was achieved only at the beginning of the infection. A mitogen secreted by the parasite could explain both phenomenons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00927059
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  • 2
    Electronic Resource
    Electronic Resource
    Unimpaired delayed type hypersensitivity reactions in mice infected withTrypanosoma cruzi strain Y (1980)
    Springer
    Parasitology research 61 (1980), S. 179-185 
    Details
    ISSN: 1432-1955
    Keywords: Trypanosoma cruzi ; Delayed hypersensitivity ; Mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Delayed type hypersensitivity reactions (DTH) to DNFB in C3H (susceptible) and (CBA×C57B1/10)F1 (resistant) mice were not impaired inTrypanosoma cruzi strain Y infections. Mice were infected IP with 100 parasites and sensitized or challenged 11 days after infection at the peak of parasitaemia. DTH reactions were found to be enhanced in C3H infected mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925463
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  • 3
    Electronic Resource
    Electronic Resource
    Adsorption chromatography of phenylalanine (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 1324-1329 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260331015
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of methotrexate (MTX) on NAD(P)+ dehydrogenases of HeLa cells: malic enzyme, 2-oxoglutarate and isocitrate dehydrogenases (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 15 (1997), S. 259-264 
    Details
    ISSN: 0263-6484
    Keywords: methotrexate ; antineoplasic drug ; isocitrate dehydrogenase ; 2-oxoglutarate dehydrogenase ; malic enzyme ; HeLa cells ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of methotrexate (MTX) on oxygen uptake by permeabilized HeLa cells were evaluated. MTX did not inhibit state III respiration when the oxidizable substrate was succinate, but when the substrates were 2-oxoglutarate or isocitrate the respiration decreased about 50 per cent at 1·0 mM concentration of the drug. This effect was explained by inhibition of 2-oxoglutarate and isocitrate dehydrogenases by MTX. No effect was observed on succinate dehydrogenase. An evaluation of the effects of MTX on malic enzyme activity as measured by pyruvate plus lactate production in intact cells supplied with malate showed a decrease of about 40 per cent in metabolite production using 0·4 mM MTX. HeLa cell malic enzyme, as observed for other tumour cells, is compartmentalized in mitochondria and cytosol, and is another example of a dehydrogenase inhibited by MTX. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Methotrexate: Studies on the cellular metabolism. I. Effect on mitochondrial oxygen uptake and oxidative phosphorylation (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 6 (1988), S. 61-66 
    Details
    ISSN: 0263-6484
    Keywords: Liver mitochondria ; methotrexate ; antimetabolite ; anticancer ; oxygen uptake ; oxidative phosphorylation ; cytochrome b ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Effect of methotrexate (MTX) on mitochondrial oxygen uptake, oxidative phosphorylation and on the activity of several enzymes linked to respiratory chain was studied. MTX was able to inhibit state III respiration activated by ADP and to decrease the respiratory coefficient with the substrates α-ketoglutarate and glutamate; these effects became pronounced when mitochondria were pre-incubated with MTX for 10 min. No effect was observed on ATPase activity of undamaged or broken mitochondria; the same was true for NADH-oxidase, NADH-dehydrogenase, NADH-cytochrome c reductase, succinate oxidase, and cytochrome c oxidase activity. The effect on the steady-state of cytochrome b, as well as, the inhibitory effect on state III of respiration with NAD+-linked substrates, offers a reasonable possibility to suggesting that the inhibition site of MTX could be in a place anterior to cytochrome b region, and not linked to respiratory chain.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290060110
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  • 6
    Electronic Resource
    Electronic Resource
    Methotrexate: Studies on cellular metabolism. III.-Effect on the transplasma-membrane redox activity and on ferricyanide-induced proton extrusion by HeLa cells (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 7 (1989), S. 135-137 
    Details
    ISSN: 0263-6484
    Keywords: HeLa cells ; methotrexate ; anticancer ; transplasma electron transport ; ferricyanide-induced proton extrusion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect of methotrexate (MTX) on transplasma-membrane electron transport and ferricyanide-induced proton extrusion by HeLa cells was studied. Both systems were inhibited by MTX. It is suggested that inhibition of electron transport and proton extrusion caused by MTX could be associated with other metabolic alterations such as response to the increase in NADH levels and decrease in intracellular pH.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290070209
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  • 7
    Electronic Resource
    Electronic Resource
    Citrinin affects the oxidative metabolism of BHK-21 cells (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 13 (1995), S. 267-271 
    Details
    ISSN: 0263-6484
    Keywords: BHK cells ; glucose utilization ; lactate ; pyruvate ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of citrinin on energy production along the respiratory chain and on glycolytic lactate production were examined in BHK-21 cultured cells. Citrinin inhibited the oxygen consumption rate by about 45 per cent. The respiratory rate of digitonin-treated cells energized with succinate, in the presence of ADP, was reduced by about 39 per cent. The mycotoxin inhibited the glucose utilization of BHK-21 cells by about 86 per cent. Cells treated with citrinin produced a small quantity of pyruvate, but were unable to produce lactate. It is concluded that BHK-21 cells cannot generate lactate when oxidative metabolism is inhibited by citrinin. The perturbations in BHK-21 cells caused by citrinin are due to alterations in mitochondrial function and in the glycolytic anaerobic pathway.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290130407
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  • 8
    Electronic Resource
    Electronic Resource
    Mechanism of citrinin-induced dysfunction of mitochondria. IV - Effect on Ca2+ transport (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 13 (1995), S. 53-59 
    Details
    ISSN: 0263-6484
    Keywords: Kidney cortex and liver mitochondria ; BHK-21 cultured cells ; 2-oxoglutarate and pyruvate dehydrogenases ; calcium transport ; citrinin ; mycotoxin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect of citrinin on Ca2+ transport was studied in isolated kidney cortex and liver mitochondria, and baby hamster kidney cultured cells. The mycotoxin significantly inhibited the activity of 2-oxoglutarate and pyruvate dehydrogenases in both kidney cortex and liver mitochondria. Citrinin promoted a decrease in the velocity and in the total capacity of Ca2+ uptake, in both mitochondria. Apparently, citrinin acts by a mechanism similar to ruthenium red. In intact cultured cells, citrinin also had a preferential effect on mitochondrial Ca2+ fluxes. Citrinin promoted a marked decrease in the Ca2+ level in the mitochondrial matrix, whereas that of the extramitochondiral fraction became less affected. All the observed effects were dependent on the citrinin concentration.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290130110
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  • 9
    Electronic Resource
    Electronic Resource
    Mitochondrial sensitivity to AZT (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 16 (1998), S. 173-181 
    Details
    ISSN: 0263-6484
    Keywords: AZT ; mitochondrial disease ; bioenergetics ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The possibility of tissue-specific effects regarding mitochondrial sensitivity to AZT was evaluated in this study. When mitochondria isolated from liver, kidney, skeletal and cardiac muscle were oxidizing glutamate, a dose-dependent inhibition by AZT of state 3 respiration was observed; using succinate as substrate the inhibition occurred only in skeletal and cardiac muscle mitochondria. The same results were obtained with FCCP-uncoupled mitochondria. NADH oxidase of intact and disrupted mitochondria, isolated from all four tissues was strongly inhibited. Succinate oxidase activity was inhibited by AZT only in intact mitochondria from skeletal and cardiac muscles, suggesting the involvement of succinate transport systems. Similarly, inhibition by the drug of the hydrolytic activity of H+-ATPase was observed only in mitochondria of these tissues. These effects taken together, indicate a tissue/carrier-specific inhibition in vitro, although its precise mechanism requires further research. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Methotrexate: Studies on cellular metabolism. IV. Effect on the mitochondrial oxidation of cytosolic-reducing equivalents in HeLa cells (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 8 (1990), S. 199-203 
    Details
    ISSN: 0263-6484
    Keywords: HeLa cells ; methotrexate ; anti-cancer ; malate-aspartate shuttle ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect of methotrexate (MTX) on the mitochondrial oxidation of cytosolic-reducing equivalents in HeLa cells was studied. MTX inhibited (100 per cent) malate dehydrogenase activity, but no effect was observed on that of GOT. MTX (0.5 mM) inhibited (100 per cent) the activity of reconstituted enzymatic system MDH-GOT, probably as a consequence of inhibition of malate dehydrogenase activity. MTX decreased pyruvate production (54 per cent), demonstrating its inhibitory action on the malate-aspartate shuttle. Blockage of the malate-aspartate shuttle by MTX accounts for the decrease in cellular energetic gain. The results obtained are consistent with the view that in HeLa cells, as well as in other tumour cells, the trasport of reducing equivalents from cytoplasmic NADH into the respiratory chain of mitochondria is via the malate-aspartate shuttle.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290080403
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