Monovalent cations in mitochondrial oxidative phosphorylation

Gómez‐Puyou, Armando; Gómez‐Puyou, Marietta Tuena de

doi:10.1007/bf00745045

Cited by 17 publications

(2 citation statements)

References 92 publications

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“…45 Reported risk variants for AD in African American individuals include ABCA7 (OMIM 604001), 46 AKAP9 (OMIM 605414), 47 TREM2 (OMIM 605086), 48 and COBL (OMIM 610317) and SLC10A2 (OMIM 601295). 49 In addition to the potential risk-modifying effects of these variants on environmental factors important for AD, it may be that 1 or more of these variants attenuates the effect of APOE ε4 such that Afric an Americ an indiv iduals have less AP OE ε4-associated risk for AD than do white individuals.…”

Section: Discussionmentioning

confidence: 99%

Assessment of Racial Disparities in Biomarkers for Alzheimer Disease

et al. 2019

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Section: Discussionmentioning

confidence: 99%

Assessment of Racial Disparities in Biomarkers for Alzheimer Disease

et al. 2019

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“…Mitochondria from bovine hearts and Mg‐ATP submitochondrial particles were prepared as described in [18,19]. F1–IF1 was prepared as in [19], except that the complex obtained from the Sepharose–hexylammonium column was applied to a Superdex 200 HR FPLC column and eluted with 50 mM Tris–SO 4 pH 6.5. The eluted F1–IF1 complex was concentrated in Centricon filters to between 5 and 10 mg/ml, and stored at −70°C.…”

Section: Methodsmentioning

confidence: 99%

Equilibrium between monomeric and dimeric mitochondrial F1–inhibitor protein complexes

et al. 2001

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Mg-ATP particles from bovine heart mitochondria have more than 95% of their F1 in complex with the inhibitor protein (IF1). The F1^IF1 complex was solubilized and purified. The question addressed was if this naturally occurring complex existed as monomers or dimers. Size exclusion chromatography and electron microscopy showed that most of the purified F1^IF1 complex was a dimer of two F1^IF1. As determined by the former method, the relative concentrations of dimeric and monomeric F1^IF1 depended on the concentration of protein that was applied to the column. Apparently, there is an equilibrium between the two forms of F1^IF1. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Mitochondria from the salt-tolerant yeast Debaryomyces hansenii (halophilic organelles?)

Cabrera‐Orefice

Guerrero–Castillo

Luévano‐Martínez

et al. 2010

J Bioenerg Biomembr

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The yeast Debaryomyces hansenii is considered a marine organism. Sea water contains 0.6 M Na(+) and 10 mM K(+); these cations permeate into the cytoplasm of D. hansenii where proteins and organelles have to adapt to high salt concentrations. The effect of high concentrations of monovalent and divalent cations on isolated mitochondria from D. hansenii was explored. As in S. cerevisiae, these mitochondria underwent a phosphate-sensitive permeability transition (PT) which was inhibited by Ca(2+) or Mg(2+). However, D. hansenii mitochondria require higher phosphate concentrations to inhibit PT. In regard to K(+) and Na(+), and at variance with mitochondria from all other sources known, these monovalent cations promoted closure of the putative mitochondrial unspecific channel. This was evidenced by the K(+)/Na(+)-promoted increase in: respiratory control, transmembrane potential and synthesis of ATP. PT was equally sensitive to either Na(+) or K(+). In the presence of propyl-gallate PT was still observed while in the presence of cyanide the alternative pathway was not active enough to generate a Delta Psi due to a low AOX activity. In D. hansenii mitochondria K(+) and Na(+) optimize oxidative phosphorylation, providing an explanation for the higher growth efficiency in saline environments exhibited by this yeast.

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Monovalent cations in mitochondrial oxidative phosphorylation

Cited by 17 publications

References 92 publications

Assessment of Racial Disparities in Biomarkers for Alzheimer Disease

Assessment of Racial Disparities in Biomarkers for Alzheimer Disease

Equilibrium between monomeric and dimeric mitochondrial F1–inhibitor protein complexes

Mitochondria from the salt-tolerant yeast Debaryomyces hansenii (halophilic organelles?)

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