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At least 289 records · Page 16Linked to original sources
PubMed1977

[The influence of biophysical factors on biological oxidation and redox processes. 17. Changes in electron transfer and of oxidative phosphorylation steps in liver mitochondria after ultrasonic treatment (author's transl)].

Ultrasonic treatment in vivo brought about distinct changes in liver mitochondria which developed in two directions as to oxygen consumption and oxidative phosphorylation. An increase of oxygen incorporation occurs with short term as well as with long-term experiences. The ratio P/O which expresses the step of oxidative phosphorylation decreases to 1 in the course of one hour after ultrasonic treatment. The results obtained and the supposition that they are related to modifications of NAD-coenzymes and flavoproteins, likewise of the activity of succinic dehydrogenase, of NADH2-cytochrom-c-reductases and cytochrom-c-oxidase, lead to the conclusion that ultrasonic energy is a factor intensifying the transfer of reduced equivalents in the shortened respiratory chain, a factor disturbing electron-proton transfer in the normal respiratory chain of NAD-coenzymes, and a releasing factor for two of the sites of coupling electron transfer with oxidative phosphorylation.

Animals↗
PubMed2001

Protective effect of metronidazole on uncoupling mitochondrial oxidative phosphorylation induced by NSAID: a new mechanism.

BACKGROUND: The pathogenesis of non-steroidal anti-inflammatory drug (NSAID) enteropathy is complex. It involves uncoupling of mitochondrial oxidative phosphorylation which alters the intercellular junction and increases intestinal permeability with consequent intestinal damage. Metronidazole diminishes the inflammation induced by indomethacin but the mechanisms remain speculative. A direct effect on luminal bacteria has traditionally been thought to account for the protective effect of metronidazole. However, a protective effect of metronidazole on mitochondrial oxidative phosphorylation has never been tested. AIMS: To assess the protective effect of metronidazole on mitochondrial uncoupling induced by indomethacin and also on the increased intestinal permeability and macroscopic damage. MATERIAL AND METHODS: The protective effect of metronidazole was evaluated in rats given indomethacin; a macroscopic score was devised to quantify intestinal lesions, and intestinal permeability was measured by means of (51)Cr-ethylenediaminetetraacetic acid. The protective effect of metronidazole against mitochondrial uncoupling induced by indomethacin was assessed using isolated coupled rat liver mitochondria obtained from rats pretreated with metronidazole or saline. RESULTS: Metronidazole significantly reduced the macroscopic intestinal damage and increase in intestinal permeability induced by indomethacin; furthermore, at the mitochondrial level, it significantly reduced the increase in oxygen consumption in state 4 induced by indomethacin and caused less reduction of the respiratory control rate. CONCLUSION: Our study confirmed the beneficial effects of metronidazole on intestinal damage and intestinal permeability, and demonstrated, for the first time, a direct protective effect of metronidazole on uncoupling of mitochondrial oxidative phosphorylation caused by NSAIDs.

Animals↗
PubMed1983

Uncoupling of oxidative phosphorylation in rat liver mitochondria following the administration of dimethyl sulphoxide.

A single intraperitoneal injection of 275 mg of dimethyl sulphoxide (DMSO) to rats (100-125 g body weight) effectively uncouples oxidative phosphorylation in liver mitochondria during the period from 2 hr to 5 day post-injection. Higher doses of DMSO are inhibitory to mitochondrial respiration. DMSO has however no uncoupling action on oxidative phosphorylation in vitro. On the other hand, dimethyl sulphide (DMS), a known metabolite of DMSO, brings about the uncoupling effect in vitro. The uncoupling of oxidative phosphorylation by normal mitochondria could also be achieved if these are pre-incubated (30 min at 0 degrees C) with the post-mitochondrial liver supernatant derived from rat injected with DMSO, 2-24 hr prior to sacrifice. These results provide explanation for the observed uncoupling effect exerted by DMSO in vivo.

Animals↗
PubMedDate not supplied

[The intensity of oxidative phosphorylation and the function of the adenylate system in the liver mitochondria of active and hibernating susliks Citellus undulatus].

The state of adenylate system and intensity of oxidative phosphorylation in liver mitochondria of active and hibernating ground squirrels were studied depending on the concentration of extramitochondrial Ca2+ ([Ca2+]ex). It was shown that at [Ca2+]ex.10(-7) M, the content of ATP as well as ATP/ADP ratio are slightly lower in the mitochondria of hibernating ground squirrels than in the mitochondria of active animals. The other parameters of the adenylate system under the same conditions differ insignificantly. [Ca2+]ex increase to 10(-6) M has little effect on the parameters of the adenylate system of active animals. On the contrary, the mitochondria of hibernating ground squirrels are strongly affected: the level of ATP is 1.5-fold and the ratio of ATP/ADP is almost 2-fold decreased. At both [Ca2+]ex the intensity of oxidative phosphorylation is essentially higher in the mitochondria of active ground squirrels. With increasing [Ca2+]ex the rate of ATP synthesis decreases, and in the mitochondria of hibernating animals the decrease is more pronounced than in the mitochondria of active animals. Thus, oxidative phosphorylation and adenylate system of mitochondria from hibernating ground squirrels are more sensitive to [Ca2+]ex increase than those of the mitochondria of active animals.

Adenosine Diphosphate↗
PubMed2000

Role of oxidative phosphorylation in Bax toxicity.

The Bcl-2-related protein Bax is toxic when expressed either in yeast or in mammalian cells. Although the mechanism of this toxicity is unknown, it appears to be similar in both cell types and dependent on the localization of Bax to the outer mitochondrial membrane. To investigate the role of mitochondrial respiration in Bax-mediated toxicity, a series of yeast mutant strains was created, each carrying a disruption in either a component of the mitochondrial electron transport chain, a component of the mitochondrial ATP synthesis machinery, or a protein involved in mitochondrial adenine nucleotide exchange. Bax toxicity was reduced in strains lacking the ability to perform oxidative phosphorylation. In contrast, a respiratory-competent strain that lacked the outer mitochondrial membrane Por1 protein showed increased sensitivity to Bax expression. Deficiencies in other mitochondrial proteins did not affect Bax toxicity as long as the ability to perform oxidative phosphorylation was maintained. Characterization of Bax-induced toxicity in wild-type yeast demonstrated a growth inhibition that preceded cell death. This growth inhibition was associated with a decreased ability to carry out oxidative phosphorylation following Bax induction. Furthermore, cells recovered following Bax-induced growth arrest were enriched for a petite phenotype and were no longer able to grow on a nonfermentable carbon source. These results suggest that Bax expression leads to an impairment of mitochondrial respiration, inducing toxicity in cells dependent on oxidative phosphorylation for survival. Furthermore, Bax toxicity is enhanced in yeast deficient in the ability to exchange metabolites across the outer mitochondrial membrane.

Biological Transport↗
PubMed1977

Prostaglandin production by methylcholanthrene-transformed mouse BALB/3T3: effect of oxidative phosphorylation inhibitors.

Oligomycin, antimycin, and 2,4-dinitrophenol, compounds that are known to inhibit oxidative phosphorylation by different mechanisms, inhibit the production of prostaglandins by serum-stimulated MC5-5 cells. The prostaglandin production that is stimulated by thrombin and bradykinin is inhibited by 2,4-dinitrophenol. Prostaglandin synthesis by MC5-5 cells from exogeneously-supplied arachidonic acid, however, is not affected by 2,4-dinitrophenol. Antimycin and 2,4-dinitrophenol also inhibit the serum-stimulated release of arachidonic acid from the cellular lipids, suggesting that it is the expression of phospholipase activity, a prerequisite for synthesis of prostaglandins by MC5-5 cells, that is dependent on oxidative phosphorylation.

Animals↗
PubMed1986

[Effect of thyroidectomy on phosphorylative oxidation and RNA synthesis in various regions of the brain in the adult monkey].

The subcellular effects of thyroidectomy in selected brain regions of Cynomolgus monkey were analyzed. 20 days after operation the respiratory rates, the activities of succinate cytochrome c reductase, glycerol-3-phosphate dehydrogenase and of oligomycin-sensitive ATPase were decreased in mitochondria isolated from all brain structures. The highest reduction (30%) was found in cerebral cortex and hippocampus. Cerebellar and striatal activities were reduced by about 20%. A smaller decrease (15%) was observed in thalamus. The effects of thyroidectomy on in vitro RNA synthesis were followed in cerebral cortex, cerebellum and thalamus. In the three analyzed regions, the activities of nucleolar and nucleoplasmic RNA polymerases dropped by 40%. Replacement therapy with T4 (2.5 micrograms/kg/day) or T3 (1 microgram/kg/day) administered immediately after thyroidectomy for 20 days, maintained mitochondrial and nuclear activities at normal level.

Adenosine Triphosphatases↗