Disease relevance of Submitochondrial Particles

• The chemiluminescent superoxide indicators lucigenin and coelenterazine were compared in rat liver submitochondrial particles and cytoplasmic membranes from Paracoccus denitrificans [1].
• Using submitochondrial particles (SMP) from beef heart, pig kidney and rat liver in the ELISA, we detected partial organ specific anti-mitochondrial antibodies (AMA) against heart and kidney SMP in sera from patients with different forms of cardiomyopathies [2].
• Quantitative structure-activity relationships for the toxicity of chlorophenols to mammalian submitochondrial particles [3].

Psychiatry related information on Submitochondrial Particles

• The effect of chronic alcohol consumption on steady-state kinetic characteristics of cytochrome oxidase in rat liver was studied using submitochondrial particles prepared from ethanol-fed and control rats [4].

High impact information on Submitochondrial Particles

• Treatment of submitochondrial particles with dicyclohexylcarbodiimide or oligomycin so as to cause about 90% inhibition of ATPase activity was accompanied by a decrease in the binding of [gamma-32P]ATP in high-affinity catalytic sites [5].
• ADP-ribose bound to submitochondrial particles is rapidly turning over [6].
• The thermodynamic parameters that characterize the inhibition of cytochrome c oxidase activity, in rat liver submitochondrial particles, by n-butanol, tetracaine, and dibucaine were obtained [7].
• Diethylpyrocarbonate (Et2PC) inhibits the succinate dehydrogenase [succinate:(acceptor) oxidoreductase, EC 1.3.99.1] activity of submitochondrial particles, Complex II (succinate:ubiquinone oxidoreductase), and the soluble, pure succinate dehydrogenase [8].
• Synthesis of adenosine triphosphate in respiration-inhibited submitochondrial particles induced by microsecond electric pulses [9].

Biological context of Submitochondrial Particles

• In liver submitochondrial particles, O2-. was formed only when succinate and antimycin A were used together, as substrate and inhibitor of the electron transport chain, respectively [10].
• Detergent activation of ATP hydrolysis is also present in inhibitor-reconstituted systems, i.e. submitochondrial particles, Triton extracts, and soluble F1-ATPase [11].
• Monitoring the rates of oxidation of NADH in submitochondrial particles with artificial oxidants, observing the kinetics of the ferricyanide assay, and measuring the concentration of iron-sulfur centers elicited by EPR permitted ascertaining the type of NADH dehydrogenase present and its relative concentration in different experimental situations [12].
• Effects of chronic ethanol intoxication on oxidative phosphorylation in rat liver submitochondrial particles [13].
• To observe lipid peroxidation of additive-free submitochondrial particles, we incubated submitochondrial particles in the absence of exogenous irons and t-butyl hydroperoxide [14].

Anatomical context of Submitochondrial Particles

• H+ transport by coated vesicles was not inhibited by vanadate (0.1 mM) or ouabain (2 mM) and differed from H+ transport by rat liver submitochondrial particles in its greater resistance to inhibition by oligomycin (10 pM to 10 microM) and N,N'-dicyclohexylcarbodiimide (DCCD) (0.1-100 microM) and its sensitivity to N-ethylmaleimide (0.1-2 mM) [15].
• The energy requirement for electron transport inhibition in submitochondrial particles indicates that energy-dependent accumulation of the dyes by mitochondria cannot alone explain the energy requirement for the cyanine dye inhibition of NADH oxidation [16].
• Proton uptake by submitochondrial particles was about 50-fold more sensitive to dicyclohexylcarbodiimide than the proton uptake by chromaffin granule membranes [17].
• The ADP/ATP translocator was selectively labeled with the triplet probe eosin-5-maleimide (EMA) after pretreatment with N-ethylmaleimide in beef heart mitochondria, as reported previously for submitochondrial particles (Müller, M., Krebs, J. J. R., Cherry, R. J., and Kawato, S. (1982) J. Biol. Chem. 257, 1117-1120) [18].
• For this purpose, experimental models consisting of intact mitochondria, ubiquinone-depleted/reconstituted submitochondrial particles, and ONOO(-)-supplemented mitochondrial membranes were used [19].

Associations of Submitochondrial Particles with chemical compounds

• When ubiquinone is reincorporated into extracted submitochondrial particles, the signal is again easily produced by partial reduction [20].
• It is readily elicited in submitochondrial particles by partial reduction, but has not been observed in submitochondrial particles from which ubiquinone has been removed by pentane extraction [20].
• Antimycin A stimulated the production of O2-. in normal rat liver and slow-growth-rate tumor, but not in fast-growth-rate tumor submitochondrial particles [10].
• The rate of (O2(./-)) generation by submitochondrial particles (SMPs) was inversely related to their alpha-tocopherol content but unrelated to CoQ content [21].
• Submitochondrial particles catalyze transhydrogenation from NADPH to [14C]NADP [22].

Gene context of Submitochondrial Particles

• However, ATP synthase has a much lower affinity for STF1 than for IF1, as demonstrated by kinetic studies of ATPase inhibition in submitochondrial particles by externally added IF1 and STF1 at pHs ranging from 5.5 to 8 [23].
• The oxidation of NADH in submitochondrial particles isolated from MUC1, MUC2 and MUC3 mucidin-resistant mutants of Saccharomyces cerevisiae is specifically resistant to mucidin [24].
• Incubations of A. suum submitochondrial particles, NADH, tiglyl-CoA, purified A. suum electron-transfer flavoprotein, and the 2-methyl branched-chain acyl-CoA dehydrogenase resulted in the rotenone-sensitive, dehydrogenase-dependent formation of 2-methylbutyryl-CoA [25].
• Incubations of A. suum submitochondrial particles with NADH, 2-methylcrotonyl-CoA, purified A. suum electron-transfer flavoprotein and 2-methyl branched-chain enoyl-CoA reductase resulted in significant 2-methylbutyryl-CoA formation, which was inhibited by both rotenone and antisera to the purified ETF-RO [26].
• Furthermore, SfA does not prevent CyP-D binding to submitochondrial particles or detergent-solubilized adenine nucleotide translocase (ANT), implying that CyP-D binding to the ANT does not require PPIase activity but pore opening does [27].

Analytical, diagnostic and therapeutic context of Submitochondrial Particles

• Titrations of the rate of superoxide (O2-) generation in rotenone-treated submitochondrial particles were similar with the ratio [NADH]/[NAD] and that of 3-acetyl pyridine adenine nucleotide in spite of different midpoint potentials of the two couples [28].
• Association of ethylammonium and perchlorate ions with unenergized submitochondrial particles was measured by centrifugation, in the presence of a high concentration of impermeant salt to minimize association with the external surface [29].
• Furthermore, H2O2 production increased from undetectable control levels to 2.2 +/- 0.3 nmol X min-1 X mg-1 after treatment of submitochondrial particles with doxorubicin (200 microM) [30].
• The binding of ATP radiolabeled in the adenine ring or in the gamma- or alpha-phosphate to F1-ATPase in complex with the endogenous inhibitor protein was measured in bovine heart submitochondrial particles by filtration in Sephadex centrifuge columns or by Millipore filtration techniques [31].
• 8. Gel filtration of submitochondrial particles from glucose-de-repressed cells gave similar results, whereas loss of ATPase occurred in submitochondrial particles from glucose-repressed cells [32].

References