Cardiolipin requirement by cytochrome oxidase and the catalytic role of phospholipid

Fry, Mitchell; Green, David E.

doi:10.1016/0006-291x(80)90622-1

Cited by 221 publications

(77 citation statements)

References 8 publications

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“…4 a mitochondrial phospholipid with two phosphate headgroups and four acyl chains, is required for the optimal function of numerous mitochondrial processes, including oxidative phosphorylation (OXPHOS) (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13), protein import (14 -17), establishment of cristae morphology (18,19), fission and fusion (20 -22), and apoptosis (23,24). Despite limited acyl chain specificity of the CL biosynthetic enzymes (25,26), the acyl chain composition of CL within an organism or cell type displays a remarkable degree of homogeneity (27).…”

Section: Cardiolipin (Cl)mentioning

confidence: 99%

Unremodeled and Remodeled Cardiolipin Are Functionally Indistinguishable in Yeast

Baile¹,

Sathappa

Lu³

et al. 2014

Journal of Biological Chemistry

111

162

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Background:The phospholipid cardiolipin undergoes acyl chain remodeling after biosynthesis, which has been hypothesized to optimize mitochondrial function. Results: ⌬cld1 yeast, containing unremodeled cardiolipin, have no mitochondrial morphology or oxidative phosphorylation defects. Conclusion: Cardiolipin remodeling is not required for optimal mitochondrial bioenergetic function in yeast. Significance: Cardiolipin remodeling may be important for presently unknown mitochondrial processes and/or have unappreciated physiological functions.

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Section: Cardiolipin (Cl)mentioning

confidence: 99%

Unremodeled and Remodeled Cardiolipin Are Functionally Indistinguishable in Yeast

Baile¹,

Sathappa

Lu³

et al. 2014

Journal of Biological Chemistry

111

162

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show abstract

“…Several studies have indicated that this lipid is involved in different inner mitochondrial membrane functions. The best documented is the absolute requirement of the activity of the cytochrome-c oxidase for cardiolipin [4,5]. Also, the activity of other mitochondrial enzymes is strongly affected by the presence of this lipid [6].…”

Section: Introductionmentioning

confidence: 99%

Further aspects of the Ca2+-dependent polymorphism of bovine heart cardiolipin

Kruijff

Verkleij

Leunissen‐Bijvelt

et al. 1982

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…44), including complex I, III and IV of the respiratory chain. It has been demonstrated that for the above enzyme systems full reactivation after extensive delipidation requires the presence of cardiolipin in the reconstitution medium [45,46]. Therefore, we propose that the effects of adriamycin exerted on the four complexes of the respiratory chain as described here can be explained in terms of adriamycin-cardiolipin interactions.…”

Section: Discussionmentioning

confidence: 74%

Effects of adriamycin on respiratory chain activities in mitochondria from rat liver, rat heart and bovine heart. Evidence for a preferential inhibition of complex III and IV

Nicolay

Kruijff

1987

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The inhibition of respiratory chain activities in rat liver, rat heart and bovine heart mitochondria by the anthracycline antibiotic adriamycin was measured in order to determine the adriamyein-sensitive sites. It appeared that complex HI and IV are efficiently affected such that their activities were reduced to 50% of control values at 175 + 25 pM adriamycin. Complex I displayed a minor sensitivity to the drug. Of the complex-l-related activities tested, only duroquinone oxidation appeared sensitive (50% inhibition at approx. 450 I~M adriamycin). Electron-transfer activities catalyzed by complex II remained essentially unaltered up to high drug concentrations. Of the activities measured for this complex, only duroquinone oxidation was significantly affected. However, the adriamycin concentration required to reduce this activity to 50% exceeded I mM. Mitochondria isolated from rat liver, rat heart and bovine heart behaved essentially identical in their response to adriamycin. These data support the conclusion that, in these three mitochondrial systems, the major drug-sensitive sites lie in complex III and IV. Cytochrome c oxidase and succinate oxidase activity in whole mitochondria exhibited a similar sensitivity towards adriamycin, as inner membrane ghosts, suggesting that the drug has direct access to its inner membrane target sites irrespective of the presence of the outer membrane. By measuring NADH and succinate oxidase activities in the presence of exogenously added cytochrome c, it appeared that adriamycin was less inhibitory under these conditions. This suggests that adriamycin competes with cytochrome c for binding to the same site on the inner membrane, presumably cardiolipin.

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Cardiolipin requirement by cytochrome oxidase and the catalytic role of phospholipid

Cited by 221 publications

References 8 publications

Unremodeled and Remodeled Cardiolipin Are Functionally Indistinguishable in Yeast

Unremodeled and Remodeled Cardiolipin Are Functionally Indistinguishable in Yeast

Further aspects of the Ca2+-dependent polymorphism of bovine heart cardiolipin

Effects of adriamycin on respiratory chain activities in mitochondria from rat liver, rat heart and bovine heart. Evidence for a preferential inhibition of complex III and IV

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