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At least 487 records · Page 27Linked to original sources
PubMed1986

TPP+ accumulation in rat brain synaptosomes as a probe for Na+ channels.

Tetraphenylphosphonium (TPP+) accumulation in rat brain synaptosomes was measured in the presence of various stimuli. TPP+ accumulation was sensitive to an increase of extracellular K+ or to the presence of Na+ channel neurotoxins. Examination of the effects of drugs with different physico-chemical properties on TPP+ accumulation showed that there was no effect under low and high K+ conditions; pimozide, flunarizine and buterizine were active in the presence of veratridine or scorpion venom. These results were compared to data obtained for the specific binding of [3H]BTX-B, a selective marker for the Na+ channel. It can be concluded that certain drugs, although active on [3H]BTX-B binding, are not necessarily identified when TPP+ is used as probe.

Animals↗
PubMed1996

Reversal of in vitro lipopolysaccharide-induced suppression of contraction in rat aorta by NG-nitro-arginine, diphenyleneiodonium and di-2-thienyliodonium.

The effects of NG-nitro-L-arginine (L-NNA), D-NNA, diphenyleneiodonium and di-2-thienyliodonium on contraction were studied in endothelium-denuded rat aortic rings incubated for 4 h with lipopolysaccharide (10 mu g ml-1) or vehicle. Lipopolysaccharide reduced Emax and increased EC50 of the phenylephrine (10-9-10-5 M) curve. Addition of D-NNA (4, 6 x 10-4 M), L-NNA (1, 10 x 10-6 M) and diphenyleneiodonium (1, 3 x 10-7 M), but not di-2-thienyliodonium (10-7 M), increased Emax and reduced EC50 of the phenylephrine curve of lipopolysaccharide-incubated but not control rings. Therefore, D-NNA, L-NNA and diphenyleneiodonium, but not di-2-thienyliodonium, inhibit inducible NO synthase in vascular smooth muscles.

Animals↗
PubMed1983

Stoichiometry of the H+-ATPase of Escherichia coli cells during anaerobic growth.

The H+/ATP stoichiometry of the H+-ATPase was investigated in Escherichia coli cells growing under anaerobic conditions at pH 6 and 7. The protonmotive force was determined from the intracellular accumulation of benzoate and tetraphenylphosphonium ions, as well as the accumulation of lactose in this lac operon inducible, but beta-galactosidase negative strain. The phosphorylation potential was calculated from the cellular concentrations of ATP, ADP and inorganic phosphate. By comparing the phosphorylation potential and the proton motive force under these steady state conditions, the H+/ATP stoichiometry was determined to be 3, similar to the value previously found in the same cells growing under aerobic conditions.

Adenosine Diphosphate↗
PubMed1985

Multiple relationships between rate of oxidative phosphorylation and delta microH in rat liver mitochondria.

The relationship between rate of ATP synthesis and transmembrane electrochemical proton gradient has been determined in rat liver mitochondria oxidizing succinate, using the respiratory inhibitor malonate or the uncoupler FCCP to decrease delta microH progressively. As previously reported [(1982) Eur. J. Biochem. 126, 443-451] two different relationships are obtained depending on the method used. Evidence is presented that this result is not due to underestimation of the delta microH maintained by fast-respiring mitochondria, as recently suggested [(1985) FEBS Lett. 181, 323-327].

Adenosine Triphosphate↗
PubMed1986

The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits.

A binding site for the channel-blocking noncompetitive antagonist [3H]triphenylmethylphosphonium ([3H]TPMP+) was localized in the alpha-, beta- and delta-chains of the nicotinic acetylcholine receptor (AChR) from Torpedo marmorata electric tissue. The photolabel was found in homologous positions of the highly conserved sequence helix II, alpha 248, beta 254, and delta 262. The site of the photoreaction appears to not be affected by the functional state of the receptor. [3H]TPMP+ was found in position delta 262 independent of whether photolabeling was performed with the receptor in its resting, desensitized or antagonist state. A model of the AChR ion channel is proposed, according to which the channel is formed by the five helices II contributed by the five receptor subunits.

Affinity Labels↗
PubMed1986

Flow-force relationships in mitochondrial oxidative phosphorylation.

The rates of oxidation and phosphorylation in isolated rat-liver mitochondria have a steep dependence on the protonmotive force (delta mu H+) across the membrane. These experimentally observed relationships proved to be independent of the way in which delta mu H+ was varied. These results were obtained when the membrane potential (delta psi) was calculated from the distribution of K+ (in the presence of valinomycin). When triphenylmethylphosphonium (TPMP+) was used as a probe for delta psi, slightly different flow-force relationships were obtained. We conclude that unique relationships exist between delta mu H+ and the rates of oxidation and phosphorylation, and that under some conditions the behaviour of the probe TPMP+ is anomalous.

Animals↗
PubMed1989

ATP-synthase complex: the mechanism of control of ion fluxes induced by cumene hydroperoxide in mitochondria.

In state 4, the cumene hydroperoxide-induced decrease of mitochondrial transmembrane potential is prevented by the free radical scavenger, butylhydroxytoluene. This decrease is accompanied by accumulation of lipid hydroperoxides. Oligomycin suppresses the cumene hydroperoxide-induced uncoupling of mitochondria, but has no significant effect on lipid peroxidation. The transition of mitochondria from state 4 to state 3 by ADP addition leads to the suppression of both lipid peroxidation and mitochondrial uncoupling. This effect on lipid peroxidation is prevented by carboxyatractyloside and oligomycin.

Adenosine Diphosphate↗
PubMed1989

Indications to an NADPH oxidase as a possible pO2 sensor in the rat carotid body.

The rat carotid body superfused with low pO2 exhibited an optical absorbance spectrum which resembles the reduced spectrum of the NADPH oxidase in neutrophils. Diphenylene iodonium (DPI) as a specific inhibitor of the oxidase attenuated the reduced absorbance spectrum in the carotid body. Also absorbance bleaching by low doses of cyanide (50 and 100 microM) was inhibited by DPI, whereas higher doses of cyanide (300 microM) caused an absorbance spectrum typical for reduced cytochromes. It is concluded that an NADPH oxidase acts as a pO2 sensor in the carotid body with low affinity for oxygen and high affinity for cyanide.

Animals↗