Calcium-induced transformation of cardiolipin nanodisks

Fox, Colin A.; Ellison, Patricia A.; Ikon, Nikita; Ryan, Robert O.

doi:10.1016/j.bbamem.2019.03.005

Cited by 18 publications

(11 citation statements)

References 29 publications

(32 reference statements)

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“…Addition of calcium ions at a concentration of 2.5 mM to solution of sonicated phosphatidylcholine liposomes containing from 5 to 20 mole% cardiolipin induced an increase in turbidity of liposomal samples studied by spectrophotometry at 325 nm. An increase in turbidity was attributed to the aggregation of liposomes [84,91,92]. 31 P-NMR signals from multilamellar dispersions of phosphatidylcholine containing 20 mol% cardiolipin in 5 mM CaCl 2 solution revealed the co-existence of two phospholipid phases: inverted hexagonal (H II ) lipid phase and lamellar bilayer phase [93].…”

Section: Coexistence Of Bilayer and Non-bilayer Phases In Membranes Containing Cardiolipinmentioning

confidence: 99%

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Gasanoff

Yaguzhinsky

Garab

2021

Cells

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The present review is an attempt to conceptualize a contemporary understanding about the roles that cardiolipin, a mitochondrial specific conical phospholipid, and non-bilayer structures, predominantly found in the inner mitochondrial membrane (IMM), play in mitochondrial bioenergetics. This review outlines the link between changes in mitochondrial cardiolipin concentration and changes in mitochondrial bioenergetics, including changes in the IMM curvature and surface area, cristae density and architecture, efficiency of electron transport chain (ETC), interaction of ETC proteins, oligomerization of respiratory complexes, and mitochondrial ATP production. A relationship between cardiolipin decline in IMM and mitochondrial dysfunction leading to various diseases, including cardiovascular diseases, is thoroughly presented. Particular attention is paid to the targeting of cardiolipin by Szeto–Schiller tetrapeptides, which leads to rejuvenation of important mitochondrial activities in dysfunctional and aging mitochondria. The role of cardiolipin in triggering non-bilayer structures and the functional roles of non-bilayer structures in energy-converting membranes are reviewed. The latest studies on non-bilayer structures induced by cobra venom peptides are examined in model and mitochondrial membranes, including studies on how non-bilayer structures modulate mitochondrial activities. A mechanism by which non-bilayer compartments are formed in the apex of cristae and by which non-bilayer compartments facilitate ATP synthase dimerization and ATP production is also presented.

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Section: Coexistence Of Bilayer and Non-bilayer Phases In Membranes Containing Cardiolipinmentioning

confidence: 99%

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Gasanoff

Yaguzhinsky

Garab

2021

Cells

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“…The interactions of pS263/S263E with pS280/S280E and of pS268/S268E with pS311/S311E were the most significant. Note that the observed ion-mediated interaction might be too strong for sodium ions in the current force-field 58 , but similar or even stronger interactions are expected to occur in the presence of multivalent ions such as , which strongly interact with phosphate 59 . Moreover, the ion-mediated interactions are likely to be environment- and salt-dependent and could be used as an additional regulation mechanism.…”

Section: Discussionmentioning

confidence: 90%

Phosphorylation-induced changes in the PDZ domain of Dishevelled 3

Jurásek

Kumar

Paclíková

et al. 2021

Sci Rep

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The PDZ domain of Dishevelled 3 protein belongs to a highly abundant protein recognition motif which typically binds short C-terminal peptides. The affinity of the PDZ towards the peptides could be fine-tuned by a variety of post-translation modifications including phosphorylation. However, how phosphorylations affect the PDZ structure and its interactions with ligands remains elusive. Combining molecular dynamics simulations, NMR titration, and biological experiments, we explored the role of previously reported phosphorylation sites and their mimetics in the Dishevelled PDZ domain. Our observations suggest three major roles for phosphorylations: (1) acting as an on/off PDZ binding switch, (2) allosterically affecting the binding groove, and (3) influencing the secondary binding site. Our simulations indicated that mimetics had similar but weaker effects, and the effects of distinct sites were non-additive. This study provides insight into the Dishevelled regulation by PDZ phosphorylation. Furthermore, the observed effects could be used to elucidate the regulation mechanisms in other PDZ domains.

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“…The data reveal that both ND samples elute from the column in a single major peak, indicating a single particle population. Based on comparison of this elution profile with that of cardiolipin ND (Fox et al, 2019), which are 18-31 nm in diameter (Ikon et al, 2015), the data indicate that CoQ 10 ND have particle diameters in this range. Absorbance was monitored at 280 nm, with two components (apoA-I and CoQ 10 ) contributing to this signal in CoQ 10 ND and only one component contributing (apoA-I) in the empty ND.…”

Section: Fplc Gel Filtration Chromatography Of Coq 10 Ndmentioning

confidence: 86%

Assembly and Characterization of Biocompatible Coenzyme Q₁₀‐Enriched Lipid Nanoparticles

Moschetti

Vine

Lethcoe

et al. 2020

Lipids

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Coenzyme Q10 (CoQ10) is a strongly hydrophobic lipid that functions in the electron transport chain and as an antioxidant. CoQ10 was conferred with aqueous solubility by incorporation into nanoparticles containing phosphatidylcholine (PtdCho) and apolipoprotein (apo) A‐I. These particles, termed CoQ10 nanodisks (ND), contain 1.0 mg CoQ10/5 mg PtdCho/2 mg apoA‐I (97% CoQ10 solubilization efficiency). UV/Vis absorbance spectroscopy of CoQ10 ND revealed a characteristic absorbance peak centered at 275 nm. Incorporation of CoQ10 into ND resulted in quenching of apoA‐I tryptophan fluorescence emission. Gel filtration chromatography of CoQ10 ND gave rise to a single major absorbance peak and HPLC of material extracted from this peak confirmed the presence of CoQ10. Incubation of cultured cells with CoQ10 ND, but not empty ND, resulted in a significant increase in the CoQ10 content of mitochondria as well as enhanced oxidative phosphorylation, as observed by a ~24% increase in maximal oxygen consumption rate. Collectively, a facile method to solubilize significant quantities of CoQ10 in lipid nanoparticles has been developed. The availability of CoQ10 ND provides a novel means to investigate biochemical aspects of CoQ10 uptake by cells and/or administer it to subjects deficient in this key lipid as a result of inborn errors of metabolism, statin therapy, or otherwise.

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Calcium-induced transformation of cardiolipin nanodisks

Cited by 18 publications

References 29 publications

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Phosphorylation-induced changes in the PDZ domain of Dishevelled 3

Assembly and Characterization of Biocompatible Coenzyme Q₁₀‐Enriched Lipid Nanoparticles

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Calcium-induced transformation of cardiolipin nanodisks

Cited by 18 publications

References 29 publications

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Cardiolipin, Non-Bilayer Structures and Mitochondrial Bioenergetics: Relevance to Cardiovascular Disease

Phosphorylation-induced changes in the PDZ domain of Dishevelled 3

Assembly and Characterization of Biocompatible Coenzyme Q10‐Enriched Lipid Nanoparticles

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Assembly and Characterization of Biocompatible Coenzyme Q₁₀‐Enriched Lipid Nanoparticles