Bioenergetics and death.
Specific inhibitors of mitochondrial functions were used in studies on the relation between bioenergetics and programmed cell death. The data of the authors are discussed in the review.
Apoptosis↗
Biomedical subjects
A V Avetisyan
Publications and source records attributed to A V Avetisyan.
Mildly oxidized glyceraldehyde-3-phosphate dehydrogenase as a possible regulator of glycolysis.
Influence of H2O2 on glycolysis was investigated. A hypothesis previously formulated was tested according to which a mild oxidation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) results in uncoupling of oxidation and phosphorylation at this step of glycolysis due to acylphosphatase activity of the oxidized enzyme. Incubation of a mixture of purified glycolytic enzymes, as well as a muscle extract, in the presence of 10-100 microM H2O2 was shown to result in an increase in the rate of glycolysis. The level of lactate accumulation in the oxidized samples increased by 80-150% compared to the samples containing mercaptoethanol. No ATP was formed by the H2O2-stimulated glycolysis. Thus, H2O2 really caused uncoupling of oxidation and phosphorylation in glycolysis. A role of GAPDH oxidation in regulation of glycolysis is discussed.
Adenosine Diphosphate↗
Photophosphorylation in alkalophilic halobacterial cells containing halorhodopsin: chloride-ion cycle?
Light-driven ATP synthesis is found in cells of the alkalophilic bacterium Natronobacterium pharaonis containing halorhodopsin but deficient in H+-pumping bacteriorhodopsin. Photophosphorylation occurs with cyanide-inhibited respiratory chain as well as without cyanide in conditions with low C1- concentration in the incubation medium. Increase in C1- concentration from 0.1 to 2.35 M in the incubation medium leads to inhibition of photophosphorylation. Continuous illumination increases membrane Delta Psi if respiration is inhibited by cyanide. This effect is stimulated by DCCD, an ATPase inhibitor. These data can be explained if one suggests that halorhodopsin pumps C1- into the cells whereas C1- release from the cells through C1--ATP-synthase is coupled with the ATP synthesis (chloride-ion cycle).
Adenosine Triphosphate↗
ATP-driven Na+ transport and Na(+)-dependent ATP synthesis in Escherichia coli grown at low delta mu H+.
In inverted subcellular vesicles of Escherichia coli grown at high delta mu H+ (neutral pH, no protonophorous uncoupler), ATP-driven Na+ transport and oxidative phosphorylation are completely inhibited by the protonophore CCCP. If E. coli was grown at low delta mu H+, i.e. at high pH or in the presence of uncoupler, some oxidative phosphorylation was observed in the vesicles even in CCCP-containing medium, and Na+ transport was actually stimulated by CCCP. The CCCP-resistant transport and phosphorylation were absent from the unc mutant lacking F0F1 ATPase. Both processes proved to be sensitive to (i) the Na+/H+ antiporter monensin, (ii) the Na+ uniporter ETH 157, (iii) the F0 inhibitors DCCD and venturicidin, and (iv) the F1 inhibitor aurovertin. The CCCP-resistant oxidative phosphorylation was stimulated by Na+ and arrested by oppositely directed delta pNa. These data are consistent with the assumption that, under appropriate growth conditions, the F0F1-type ATPase of E. coli becomes competent in transporting Na+ ions.
Adenosine Triphosphatases↗
Involvement of a d-type oxidase in the Na(+)-motive respiratory chain of Escherichia coli growing under low delta mu H+ conditions.
An attempt has been made to find out which of the two terminal oxidases, the d-type or the o-type, operates as a Na+ pump in Escherichia coli grown at low delta mu H+ conditions. For this purpose, mutants lacking either d or o oxidase have been studied. It is shown that a d-,o+ mutant grows slowly or does not grow at all under low delta mu H+ conditions (alkaline or protonophore-containing growth media were used). Inside-out subcellular vesicles from the d-,o+ mutant cannot oxidize ascorbate and TMPD, and cannot transport Na+ when succinate is oxidized in the presence of a protonophore. The same vesicles are found to transport Na+ when NADH is oxidized as if the Na(+)-motive NADH-quinone oxidase were operative. On the other hand, a mutant lacking o oxidase (d+,o-) grows at low delta mu H+ conditions as fast as the maternal E. coli strain containing both d and o oxidases. Corresponding vesicles oxidize ascorbate and TMPD as well as succinate, the oxidations being coupled to the protonophore-stimulated Na+ transport. Growth in the presence of a protonophore is found to induce a strong increase in the d oxidase level in the maternal d+,o+ E.coli strain. It is concluded that oxidase of the d-type, rather than of the o-type, operates as a Na+ pump in E. coli grown under conditions unfavorable for the H+ cycle.
Escherichia coli↗
Adaptation of Bacillus FTU and Escherichia coli to alkaline conditions: the Na(+)-motive respiration.
Mechanisms of Na+ transport into the inside-out subcellular vesicles of alkalo- and halotolerant Bacillus FTU and of Escherichia coli grown at different pH have been studied. Both microorganisms growing at pH 7.5 are shown to possess a system of the respiration-dependent Na+ transport which (i) is inhibited by protonophorous uncoupler, by delta pH-discharging agent diethylammonium (DEA) acetate, by micromolar cyanide arresting the H(+)-motive respiratory chain, and by amiloride, and (ii) is resistant to the Na+/H+ antiporter monensin and to Ag+, inhibitor of the Na(+)-motive respiratory chain. Growth at pH 8.6 strongly changes the activator and inhibitor pattern. Now (1) protonophore stimulates the Na+ transport, (2) DEA acetate is without effect in the absence of protonophore and is stimulating in its presence, (3) amiloride and low cyanide are ineffective, (4) monensin and Ag+ completely arrest the Na+ accumulation in the vesicles. Independent of pH of the growth medium, (a) valinomycin is stimulatory for the Na+ transport, (b) Na+ ionophore ETH 157 is inhibitory and, (c) Na+ transport can be supported by NADH----fumarate as well as by ascorbate (TMPD)----O2 electron transfers. Growth at alkaline pH results in the appearance of ascorbate (TMPD) oxidation resistant to low and sensitive to high cyanide concentrations. These relationships are in agreement with the concept (Skulachev, V.P. (1984) Trends Biochem. Sci. 9, 483-485) that adaptation to alkaline conditions in bacteria growing in the high [Na+] media causes substitution of Na+ for H+ as a coupling ion. The obtained data indicate that under alkaline conditions, Na+ can be pumped from the cell by the Na(+)-motive respiratory chain with neither H(+)-motive respiration nor the Na+/H+ antiporter involved. In the Na(+)-motive respiratory chain of Bac. FTU or E. coli, two Na+ pumps are localized, one in its initial and the other in its terminal spans.
Acclimatization↗
Uncoupling of respiration and oxidative phosphorylation in transformed mouse L929 fibroblasts induced by cocultivation with human erythroleukemic K562 cells or by tumor necrosis factor.
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Animals↗