The reaction between the superoxide anion radical and cytochrome c

Butler, J. A. V.; Jayson, G. G.; Swallow, A. J.

doi:10.1016/0005-2728(75)90124-3

Cited by 136 publications

(58 citation statements)

References 18 publications

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“…We used three different assays to examine the respiratory burst in our system: DCF, a H 2 O 2 -dependent fluorescent probe (16); CytC, whose reduction by superoxide causes a change in protein absorbance at 550 nm (33); and EPR with the spin trap DMPO, which measures multiple species of ROI through spectral differences in the adducts formed by the reaction of DMPO with ROI (20). The use of complementary assays to study the respiratory burst was necessary because of the known limitations in sensitivity and specificity of each assay type.…”

Section: Discussionmentioning

confidence: 99%

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Crowther

Kutala²,

Kuppusamy³

et al. 2004

The Journal of Immunology

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Alveolar macrophages are important host defense cells in the human lung that continuously phagocytose environmental and infectious particles that invade the alveolar space. Alveolar macrophages are prototypical alternatively activated macrophages, with up-regulated innate immune receptor expression, down-regulated costimulatory molecule expression, and limited production of reactive oxygen intermediates (ROI) in response to stimuli. Surfactant protein A (SP-A) is an abundant protein in pulmonary surfactant that has been shown to alter several macrophage (Mφ) immune functions. Data regarding SP-A effects on ROI production are contradictory, and lacking with regard to human Mφ. In this study, we examined the effects of SP-A on the oxidative response of human Mφ to particulate and soluble stimuli using fluorescent and biochemical assays, as well as electron paramagnetic resonance spectroscopy. SP-A significantly reduced Mφ superoxide production in response to the phorbol ester PMA and to serum-opsonized zymosan (OpZy), independent of any effect by SP-A on zymosan phagocytosis. SP-A was not found to scavenge superoxide. We measured Mφ oxygen consumption in response to stimuli using a new oxygen-sensitive electron paramagnetic resonance probe to determine the effects of SP-A on NADPH oxidase activity. SP-A significantly decreased Mφ oxygen consumption in response to PMA and OpZy. Additionally, SP-A reduced the association of NADPH oxidase component p47phox with OpZy phagosomes as determined by confocal microscopy, suggesting that SP-A inhibits NADPH oxidase activity by altering oxidase assembly on phagosomal membranes. These data support an anti-inflammatory role for SP-A in pulmonary homeostasis by inhibiting Mφ production of ROI through a reduction in NADPH oxidase activity.

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Section: Discussionmentioning

confidence: 99%

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Crowther

Kutala²,

Kuppusamy³

et al. 2004

The Journal of Immunology

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“…29) However, it is thought that the reduction of cytochrome c during the glycation reaction may occur by superoxide and by direct reduction from the Amadori compound. 22) Therefore superoxide anion generation during the glycation reaction has been confirmed by the SOD-dependent reduction of cytochrome c, [30][31][32][33] and the amount of superoxide formed was calculated.…”

Section: Discussionmentioning

confidence: 99%

Generation of Superoxide Anions during the Reaction of Guanidino Compounds with Methylglyoxal.

Nohara

Usui

Kinoshita

et al. 2002

CHEMICAL & PHARMACEUTICAL BULLETIN

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Uremic toxins are accumulated in the blood of patients with chronic renal failure (CRF), although alteration of the toxicity by the interaction of various uremic retention products has not been precisely clarified. In this study, we found that cytochrome c added to incubation mixtures containing guanidino compounds and methylglyoxal in phosphate buffer solution (pH 7.4) resulted in reduction of cytochrome c. Superoxide anions were generated from incubation mixtures of each guanidino compound with methylglyoxal, because the reduction was inhibited by the addition of superoxide dismutase. The incubation mixture containing each guanidino compound and methylglyoxal had different rates of generation of the superoxide anion from other mixtures. A relatively higher superoxide anion formation rate was observed in the incubation mixture containing Arg and methylglyoxal (7.9؎0.5 nmol · m ؊1 · min ؊1 ), or in the incubation mixture containing methylguanidine and methylglyoxal (6.3؎0.6 nmol · ml ؊1 · min ؊1). These findings suggest that interactions of various uremic retention products which accumulate in the blood of uremic patients may generate reactive oxygen species and may be involved in the oxidative stress observed in CRF patients. The addition of aminoguanidine, which is known to inhibit the formation of advanced glycation end products, to a mixture of guanidino compounds and methylglyoxal inhibited reactions between guanidino compounds and methylglyoxal.

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“…More recently, this model has been refined to propose that hypoxia may induce a conformational change in complex III of the mitochondrial respiratory chain (ubiquinol cytochrome c oxidoreductase), which facilitates interaction between the ubisemiquinone radical (UQ ⅐ ) and O 2 , to enhance O 2 ⅐Ϫ formation (19,39,56). Another possible mechanism for increased mitochondrial ROS generation in hypoxia stems from the ability of oxidized cytochrome c to scavenge O 2 ⅐Ϫ (22,71). Oxygen limitation at complex IV could lead to cytochrome c reduction, abrogating its ability to scavenge O 2 ⅐Ϫ , thus enhancing mitochondrial ROS leakage.…”

Section: ⅐ϫmentioning

confidence: 99%

Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling

Hoffman

Salter²,

Brookes³

2007

American Journal of Physiology-Heart and Circulatory Physiology

143

114

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Hoffman DL, Salter JD, Brookes PS. Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling. Am J Physiol Heart Circ Physiol 292: H101-H108, 2007. First published September 8, 2006; doi:10.1152/ajpheart.00699.2006.-Mitochondria are proposed to play an important role in hypoxic cell signaling. One currently accepted signaling paradigm is that the mitochondrial generation of reactive oxygen species (ROS) increases in hypoxia. This is paradoxical, because oxygen is a substrate for ROS generation. Although the response of isolated mitochondrial ROS generation to [O 2] has been examined previously, such investigations did not apply rigorous control over [O2] within the hypoxic signaling range. With the use of open-flow respirometry and fluorimetry, the current study determined the response of isolated rat liver mitochondrial ROS generation to defined steady-state [O2] as low as 0.1 M. In mitochondria respiring under state 4 (quiescent) or state 3 (ATP turnover) conditions, decreased ROS generation was always observed at low [O 2]. It is concluded that the biochemical mechanism to facilitate increased ROS generation in response to hypoxia in cells is not intrinsic to the mitochondrial respiratory chain alone but may involve other factors. The implications for hypoxic cell signaling are discussed.hypoxia-inducible factor; superoxide; free radicals; mitochondria; metabolism REACTIVE OXYGEN SPECIES (ROS) generated by mitochondria are key intermediates in a diverse array of cell signaling events, including regulation of the cell cycle (68), proliferation (51), metalloproteinases (65), apoptosis (54), protein kinases (8,16,54,64), phosphatases (62), growth factor signaling (78), and transcription factors (44, 52) (see Ref. 31 for review). One area of investigation that has been the focus of much recent interest is the potential role of mitochondrial ROS in the signaling events that occur during hypoxia, including the regulation of hypoxia-inducible factors such as HIF-1␣ (2, 4, 7, 10, 25, 32, 48, 56, 59, 67, 84 -86, 88, 89). Whereas the downstream effects of mitochondrially derived ROS are relatively well established (vide supra), the mechanisms and the directionality (i.e., increased or decreased) of mitochondrial ROS generation in hypoxia are currently under debate (59,86). This is an important area of study, since it appears that not only can mitochondria regulate HIF, but HIF and its downstream target genes (e.g., heme oxygenase) are important pathophysiological regulators of mitochondrial function (5, 42, 77). Thus, perturbing the mitochondria/HIF signaling loop may contribute to disease pathogenesis (10).A widely accepted model of hypoxic cell signaling is that mitochondrial ROS generation increases in hypoxia (7,25,32,67,85,86,88,89). This is proposed to occur via O 2 limitation at the terminal enzyme in the mitochondrial respiratory chain, cytochrome c oxidase (complex IV), causing a backup of electrons in the proximal chain and increase...

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The reaction between the superoxide anion radical and cytochrome c

Cited by 136 publications

References 18 publications

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Generation of Superoxide Anions during the Reaction of Guanidino Compounds with Methylglyoxal.

Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling

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