Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

Benz, Roland

doi:10.1016/0304-4157(94)90004-3

Cited by 403 publications

(404 citation statements)

References 184 publications

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“…[38,40]). However, it has been recently proven that VDAC also has a cation selective open state [55].…”

Section: Discussionmentioning

confidence: 99%

“…It is well known that VDAC behavior in planar phospholipid membranes made of asolectin is voltage dependent and symmetrical [38][39][40], meaning that the channel closes at about the same rate and to about the same extent depending on the applied potential value but regardless its sign. Thus, VDAC reconstituted into planar phospholipid membranes displays 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 Garcia-Martinez EM et al,…”

Section: Minocycline Affects Vdac Conductance and Voltage Dependencementioning

confidence: 99%

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Mitochondria and calcium flux as targets of neuroprotection caused by minocycline in cerebellar granule cells

García-Martínez

Sanz-Blasco

Karachitos

et al. 2010

Biochemical Pharmacology

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 Garcia-Martinez EM et al., 2 AbstractMinocycline, an antibiotic of the tetracycline family, has attracted considerable interest for its theoretical therapeutic applications in neurodegenerative diseases. However, the mechanism of action underlying its effect remains elusive. Here we have studied the effect of minocycline under excitotoxic conditions. Fluorescence and bioluminescence imaging studies in rat cerebellar granular neuron cultures using fura-2/AM and mitochondria-targeted aequorin revealed that minocycline, at concentrations higher than those shown to block inflammation and inflammation-induced neuronal death, inhibited NMDA-induced cytosolic and mitochondrial rises in Ca 2+ concentrations in a reversible manner. Moreover, minocycline added in the course of NMDA stimulation decreased Ca 2+ intracellular levels, but not when induced by depolarization with a high K + medium. We also found that minocycline, at the same concentrations, partially depolarized mitochondria by about 5-30 mV, prevented mitochondrial Ca 2+ uptake under conditions of environmental stress, and abrogated NMDAinduced reactive oxygen species (ROS) formation. Consistently, minocycline also abrogates the rise in ROS induced by 75 M Ca 2+ in isolated brain mitochondria. In search for the mechanism of mitochondrial depolarization, we found that minocycline markedly inhibited state 3 respiration of rat brain mitochondria, although distinctly increased oxygen uptake in state 4. Minocycline inhibited NADH-cytochrome c reductase and cytochrome c oxidase activities, whereas the activity of succinate-cytochrome c reductase was not modified, suggesting selective inhibition of complex I and IV. Finally, minocycline affected activity of voltage-dependent anion channel (VDAC) as determined in the reconstituted system. Taken together, our results indicate that mitochondria are a critical factor in minocycline-mediated neuroprotection.

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“…[38,40]). However, it has been recently proven that VDAC also has a cation selective open state [55].…”

Section: Discussionmentioning

confidence: 99%

Section: Minocycline Affects Vdac Conductance and Voltage Dependencementioning

confidence: 99%

Mitochondria and calcium flux as targets of neuroprotection caused by minocycline in cerebellar granule cells

García-Martínez

Sanz-Blasco

Karachitos

et al. 2010

Biochemical Pharmacology

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“…VDAC1 structure and FLAG-epitope positions. (A) Three-dimensional model of hsVDAC1 drawn with Pymol [DeLano Scientific] using PDB coordinates 2K4T from [11] (see also 2JK4 [12] and 3EMN [13]) indicating FLAG-epitope locations used in the current study (1)(2)(3)(4)(5). FLAG3, which contradicts the structure, is highlighted (Ã).…”

Section: Localization Of Flag-tagged Vdac1mentioning

confidence: 99%

Probing the orientation of yeast VDAC1 in vivo

et al. 2009

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a b s t r a c tVoltage dependent anion channel (VDAC) is a vital ion channel in mitochondrial outer membranes and its structure was recently shown to be a 19 stranded b-barrel. However the orientation of VDAC in the membrane remains unclear. We probe here the topology and membrane orientation of yeast Saccharomyces cerevisiae in vivo. Five FLAG-epitopes were independently inserted into scVDAC1 and their surface exposure in intact and disrupted mitochondria detected by immunoprecipitation. Functionality was confirmed by measurements of respiration. Two epitopes suggest that VDAC (scV-DAC) has its C-terminus exposed to the cytoplasm whilst two others are more equivocal and, when combined with published data, suggest a dynamic behavior.

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“…1 A particular property of the VDAC is the dependence of its channel activity on an external transmembrane potential. 5 Experiments with the VDAC reconstituted into planar bilayer lipid membranes demonstrated that low potentials between ca. À20 mV and 20 mV yield an open state with a conductance of ca.…”

Section: Introductionmentioning

confidence: 99%

Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy

Kozuch

Weichbrodt

Millo

et al. 2014

Phys. Chem. Chem. Phys.

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The voltage-dependent anion channel (VDAC) is a transmembrane protein that regulates the transfer of metabolites between the cytosol and the mitochondrium. Opening and partial closing of the channel is known to be driven by the transmembrane potential via a mechanism that is not fully understood. In this work, we employed a spectroelectrochemical approach to probe the voltage-induced molecular structure changes of human VDAC1 (hVDAC1) embedded in a tethered bilayer lipid membrane on a nanostructured Au electrode. The model membrane consisted of a mixed self-assembled monolayer of 6-mercaptohexanol and (cholesterylpolyethylenoxy)thiol, followed by the deposition of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine vesicles including hVDAC1. The stepwise assembly of the model membrane and the incorporation of hVDAC1 were monitored by surface enhanced infrared absorption and electrochemical impedance spectroscopy. Difference spectra allowed for identifying the spectral changes which may be associated with the transition from the open to the ''closed'' states by shifting the potential above or below the transmembrane potential determined to be ca. 0.0 V vs. the open circuit potential. These spectral changes were interpreted on the basis of the orientation-and distancedependent IR enhancement and indicate alterations of the inclination angle of the b-strands as crucial molecular events, reflecting an expansion or contraction of the b-barrel pore. These protein structural changes that do not confirm nor exclude the reorientation of the a-helix are either directly induced by the electric field or a consequence of a potential-dependent repulsion or attraction of the bilayer.

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Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

Cited by 403 publications

References 184 publications

Mitochondria and calcium flux as targets of neuroprotection caused by minocycline in cerebellar granule cells

Mitochondria and calcium flux as targets of neuroprotection caused by minocycline in cerebellar granule cells

Probing the orientation of yeast VDAC1 in vivo

Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy

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