Stoichiometry of Proton Translocation through the Respiratory Chain and Adenosine Triphosphatase Systems of Rat Liver Mitochondria

Mitchell, Peter; Moyle, Jennifer

doi:10.1038/208147a0

Cited by 271 publications

(121 citation statements)

References 7 publications

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“…IM impermeability is essential for maintaining the proton gradient that is required for oxidative phosphorylation [50,51]. This means that all constituents of the mitochondrial matrix and metabolites have to cross IM in a tightly regulated fashion, via selective channels and transporters.…”

Section: Im Permeabilizationmentioning

confidence: 99%

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

et al. 2007

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Mitochondrial membrane permeabilization (MMP) is considered as the "point-of-no-return" in numerous models of programmed cell death. Indeed, mitochondria determine the intrinsic pathway of apoptosis, and play a major role in the extrinsic route as well. MMP affects the inner and outer mitochondrial membranes (IM and OM, respectively) to a variable degree. OM permeabilization culminates in the release of proteins that normally are confined in the mitochondrial intermembrane space (IMS), including caspase activators (e.g. cytochrome c) and caspase-independent death effectors (e.g. apoptosis-inducing factor). Partial IM permeabilization disrupts mitochondrial ion and volume homeostasis and dissipates the mitochondrial transmembrane potential ( m ). The assessment of early mitochondrial alterations allows for the identification of cells that are committed to die but have not displayed yet the apoptotic phenotype. Several

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Section: Im Permeabilizationmentioning

confidence: 99%

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

et al. 2007

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“…Mitchell and Moyle were the first to propose a cation/proton antiport system which would allow mitochondria to extrude sodium and potassium against a highly unfavorable electrochemical gradient [106]. While the molecular identity of the mitochondrial NHE proposed by Mitchell and Moyle remains still elusive, 13 other NHE isoforms have been cloned thus far [18].…”

Section: Introductionmentioning

confidence: 99%

Traditional and emerging roles for the SLC9 Na+/H+ exchangers

Fuster

Alexander

2013

Pflugers Arch - Eur J Physiol

141

122

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The SLC9 gene family encodes Na + /H + exchangers (NHEs). These transmembrane proteins transport ions across lipid bilayers in a diverse array of species from prokaryotes to eukaryotes, including plants, fungi and animals. They utilize the electrochemical gradient of one ion to transport another ion against its electrochemical gradient. Currently, 13 evolutionarily conserved NHE isoforms are known in mammals [46,22,128]. The SLC9 gene family (solute carrier classification of transporters:www.bioparadigms.org) is divided into three subgroups [46]. The SLC9A subgroup encompasses plasmalemmal isoforms NHE1-5 (SLC9A1-5) and the predominantly intracellular isoforms NHE6-9 (SLC9A6-9). The SLC9B subgroup consists of two recently cloned isoforms, NHA1 and NHA2 (SLC9B1 and SLC9B2, respectively). The SLC9C subgroup consist of a sperm specific plasmalemmal NHE (SLC9C1) and a putative NHE, SLC9C2, for which there is currently no functional data [46].NHEs participate in the regulation of cytosolic and organellar pH as well as cell volume. In the intestine and kidney, NHEs are critical for transepithelial movement of Na + and HCO 3 -and thus for whole body volume and acid-base homeostasis [46]. Mutations in the NHE6 or NHE9 genes cause neurological disease in humans and are currently the only NHEs directly linked to human disease.However, it is becoming increasingly apparent that members of this gene family contribute to the pathophysiology of multiple human diseases.

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“…The resulting electrochemical proton gradient performs useful work when protons re-enter the matrix through the F o F " -ATPase (causing synthesis of ATP from ADP and P i [1]) or through other proteins to drive ion and substrate transport. However, the electrochemical proton gradient can also be dissipated by leak reactions catalysed by endogenous mitochondrial proton-conductance pathways [2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

“…UCP1 is inhibited by purine nucleotides such as ATP and GDP, and is activated by Abbreviations used : UCP, uncoupling protein ; TPMP + , triphenylmethyl phosphonium cation ; FCCP, carbonyl cyanide p-trifluoromethoxyphenylhydrazone. 1 To whom correspondence should be addressed, at the MRC Dunn Human Nutrition Unit (e-mail martin.brand!mrc-dunn.cam.ac.uk).…”

Section: Introductionmentioning

confidence: 99%

Effects of magnesium and nucleotides on the proton conductance of rat skeletal-muscle mitochondria

Cadenas

Brand

2000

Biochemical Journal

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During oxidative phosphorylation most of the protons pumped out to the cytosol across the mitochondrial inner membrane return to the matrix through the ATP synthase, driving ATP synthesis. However, some of them leak back to the matrix through a proton-conductance pathway in the membrane. When the ATP synthase is inhibited with oligomycin and ATP is not being synthesized, all of the respiration is used to drive the proton leak. We report here that Mg# + inhibits the proton conductance in rat skeletal-muscle mitochondria. Addition of Mg# + inhibited both oligomycin-inhibited respiration and the proton conductance, while removal of Mg# + using EDTA activated these processes. The proton conductance was inhibited by more than 80 % as free Mg# + was raised from 25 nM to 220 µM. Half-maximal inhibition occurred at about 1 µM free Mg# + ,

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Stoichiometry of Proton Translocation through the Respiratory Chain and Adenosine Triphosphatase Systems of Rat Liver Mitochondria

Cited by 271 publications

References 7 publications

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

Traditional and emerging roles for the SLC9 Na+/H+ exchangers

Effects of magnesium and nucleotides on the proton conductance of rat skeletal-muscle mitochondria

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