The effect of rotenone on respiration and its point of attack

Lindahl, Per Eric; Öberg, K.E.

doi:10.1016/0014-4827(61)90033-7

Cited by 190 publications

(84 citation statements)

References 4 publications

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“…Apoptosis was triggered with rotenone, an inhibitor of complex I in the mitochondrial respiratory chain (10,16). Rotenone is widely used in studies of the activation of mitochondriadependent caspase pathways (20,21,29,30).…”

Section: Methodsmentioning

confidence: 99%

Subcellular localization of Apaf-1 in apoptotic rat pituitary cells

Potokar

Kreft²,

Chowdhury³

et al. 2006

American Journal of Physiology-Cell Physiology

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A key step in the intrinsic apoptotic pathway is the assembly of the apoptosome complex. The apoptosome components are well known; however, the physiology of the assembly of the apoptosome complex at the cellular level is still poorly defined. The aim of this work was to study the subcellular distribution of the apoptosome scaffold protein apoptotic protease-activating factor 1 (Apaf-1) before and after triggering apoptosis in single somatotrophs. Somatotrophs are the subject of extensive pituitary tissue remodeling in different physiological situations in which the quality and the number of pituitary cells are determined by cell proliferation and apoptosis. We show herein that 2 h after triggering apoptosis with rotenone, Apaf-1 redistributed to the proximity of mitochondria. In addition, the degree of colocalization between Apaf-1 and fluorescently labeled caspase-9 significantly increased during the same period. Furthermore, we show herein for the first time in single cells that the colocalization between Apaf-1 and cytochrome c increases only transiently, indicating a transient interaction between cytochrome c and Apaf-1 during the activation of apoptosis in these cells.

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Section: Methodsmentioning

confidence: 99%

Subcellular localization of Apaf-1 in apoptotic rat pituitary cells

Potokar

Kreft²,

Chowdhury³

et al. 2006

American Journal of Physiology-Cell Physiology

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“…In experiments in which hexanoate and palmitate were incubated together, ketone body production from the combination was about the same as from hexanoate alone, whereas the 3-hydroxybutyrate/acetoacetate ratio was greater than that observed for cells incubated with palmitate alone. The effects of rotenone [22] and antimycin [23] on cellular respiration and fatty acid oxidation are presented in Table 2. inhibition of the respiration of isolated mitochondria incubated with palmitate or palniitoylcarnitine was brought about by 0.5 pM antimycin; R. Gregory and M. N. Berry, unpublished observations.)…”

Section: Coniparison Of' H Q U T I C Hexunoute Und Pulmitute Oxidutionmentioning

confidence: 99%

Compartmentation of Fatty Acid Oxidation in Liver Cells

Berry¹,

Gregory²,

Grivell³

et al. 1983

European Journal of Biochemistry

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When isolated liver cells from starved rats were incubated with fatty acids, the rates of 0 , uptake and ketone body production in the presence of hexanoate were somewhat greater than with added palmitate. However, the 3-hydroxybutyrate/acetoacetate ratio was consistently higher in the presence of palmitate. Moreover, palmitate was much more effective than hexanoate in slowing the restoration to normal of an elevated lactatc/pyruvate ratio. This action of palmitate was counteracted by inhibitors of long-chain fatty acid oxidation to ketone bodies. Palmitate, but not hexanoate, partially inhibited lactate-stimulated ethanol oxidation. These effects of palmitate were in most instances exaggerated in cells from clofibrate-treated rats, which had somewhat higher rates of ketogenesis.When cells were incubated with rotenone, ketone bodies were produced at about 30% of control rates and accumulated almost entirely as 3-hydroxybutyrate. In the presence of antimycin, ketone body accumulation from added palmitate again occurred at about 30% of control rates, but ketogenesis from endogenous substrates or hexanoate was inhibited to a greater extent. Cells from clofibrate-treated rats were equally sensitive to antimycin but considerably less inhibited by rotenone than control cells, although the 3-hydroxybutyrate/acetoacetate ratio remained very high.The depression of fatty acid oxidation in cells incubated with rotenone could be relieved to a considerable degree by coupling the dehydrogenation of hydroxyacyl-CoA to the reduction of acetoacetate. This observation was found to be valid only for longer chain fatty acids (Cl0-Cl8). The coupling of octanoate oxidation lo acetoacetate reduction was promoted by the addition of carnitine. Carnitine did not increase the coupling of the oxidation of other fatty acids tested to acetoacetate reduction.The formation of labelled ketone bodies from [l-'4C]palmitate and [l-'4C]hexanoate was also examined. When the two fatty acids were presented together to rotenone-poisoned cells in the presence of acetoacetate, hexanoate caused some inhibition of 14C02 formation and ketone body production from [l-'4C]palmitate, but the converse did not apply. In fact palmitate stimulated the oxidation of [l-14C]hexanoate to 14C0, and labelled ketone bodies. This stimulation was abolished by low levels of 2,4-dinitrophenol.The results of these experiments are explained on the basis of compartmentation of fatty acid oxidation between mitochondrial matrix and peroxisomes. Whereas both long-chain and short-chain fatty acids can be oxidized within the mitochondrial matrix, an additional site of long-chain acyl-CoA oxidation exists in the peroxisomes. Thus, peroxisomes and mitochondria co-operate in the oxidation of long-chain fatty acids. The oxidation of long-chain acyl groups within the peroxisomes and the subsequent transfer of reducing equivalents to the mitochondria, probably via a glycerol 1-phosphate shuttle, explains why long-chain fatty acids induce a more reduced 'redox state' than shortchain species...

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“…Isolated liver cells from starved rats were incubated with rotenone which, by inhibiting NADH dehydrogenase [29], strongly depressed oxidation of [l-14C]palmitate to 14C02 and ketone bodies, and decreased respiration by X0%. The addition of 10 mM acetoacetate completely restored ketone body formation and brought about a partial recovery of Oruptake and 14C02 production.…”

Section: K107mentioning

confidence: 99%

The function of energy‐dependent redox reactions in cell metabolism

Berry¹

1980

FEBS Letters

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The effect of rotenone on respiration and its point of attack

Cited by 190 publications

References 4 publications

Subcellular localization of Apaf-1 in apoptotic rat pituitary cells

Subcellular localization of Apaf-1 in apoptotic rat pituitary cells

Compartmentation of Fatty Acid Oxidation in Liver Cells

The function of energy‐dependent redox reactions in cell metabolism

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