Studies on Human Porin XXI: Gadolinium Opens Up Cell Membrane Standing Porin Channels Making Way for the Osmolytes Chloride or Taurine—A Putative Approach to Activate the Alternate Chloride Channel in Cystic Fibrosis

Thinnes, Friedrich P.; Hellmann, Klaus P.; Hellmann, Thea; Merker, Rolf; Schwarzer, Christian; Walter, Götz; Götz, H.; Hilschmann, Norbert

doi:10.1006/mgme.2000.2968

Cited by 19 publications

(3 citation statements)

References 64 publications

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“…Given that none of the Bcl-2 family proteins is secreted, a Bax-mediated increase of plasma membrane permeability does not seem to be physiologically relevant. However, the VDAC on the plasma membrane is involved in cell volume regulation (Thinnes et al, 2000), so there might be secreted protein(s) that modulate this VDAC in a similar fashion to Bax/Bak.…”

Section: Discussionmentioning

confidence: 99%

Essential Role of Voltage-Dependent Anion Channel in Various Forms of Apoptosis in Mammalian Cells

Shimizu

Matsuoka

Shinohara

et al. 2001

The Journal of Cell Biology

331

296

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Through direct interaction with the voltage-dependent anion channel (VDAC), proapoptotic members of the Bcl-2 family such as Bax and Bak induce apoptogenic cytochrome c release in isolated mitochondria, whereas BH3-only proteins such as Bid and Bik do not directly target the VDAC to induce cytochrome c release. To investigate the biological significance of the VDAC for apoptosis in mammalian cells, we produced two kinds of anti-VDAC antibodies that inhibited VDAC activity. In isolated mitochondria, these antibodies prevented Bax-induced cytochrome c release and loss of the mitochondrial membrane potential (Δψ), but not Bid-induced cytochrome c release. When microinjected into cells, these anti-VDAC antibodies, but not control antibodies, also prevented Bax-induced cytochrome c release and apoptosis, whereas the antibodies did not prevent Bid-induced apoptosis, indicating that the VDAC is essential for Bax-induced, but not Bid-induced, apoptogenic mitochondrial changes and apoptotic cell death. In addition, microinjection of these anti-VDAC antibodies significantly inhibited etoposide-, paclitaxel-, and staurosporine-induced apoptosis. Furthermore, we used these antibodies to show that Bax- and Bak-induced lysis of red blood cells was also mediated by the VDAC on plasma membrane. Taken together, our data provide evidence that the VDAC plays an essential role in apoptogenic cytochrome c release and apoptosis in mammalian cells.

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Section: Discussionmentioning

confidence: 99%

Essential Role of Voltage-Dependent Anion Channel in Various Forms of Apoptosis in Mammalian Cells

Shimizu

Matsuoka

Shinohara

et al. 2001

The Journal of Cell Biology

331

296

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“…The same group has reported that Gd 3+ opens VDAC channels that serve as a pathway for Cland taurine in B-lymphocytes and HeLa cells, which subsequently leads to cell swelling. Antibodies against VDAC block both VDAC channels and the observed cell swelling [297], indicating that VDAC is involved in RVD. In contrast, however, Gd 3+ and La 3+ block RVDC in Xenopus oocytes [2], Xenopus follicle cells [224] and colonic myocytes [63].…”

Section: Voltage-dependent Anion Channel (Vdac)mentioning

confidence: 98%

Molecular and functional aspects of anionic channels activated during regulatory volume decrease in mammalian cells*

Fürst

Gschwentner

Ritter

et al. 2002

Pflügers Arch - Eur J Physiol

105

119

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“…This anion channel maintains Cl -uptake, when K + influx is triggered by the IADS-activated plasma membrane cation conductance. A possible candidate is the voltage dependent anion channel, VDAC [35], which is assumed to be a part of the DIDS sensitive, CFTR-controlled ORCC [36]. In this case, influx of cations through the IADS-activated channel should depolarize the membrane and, thus, stimulate VDAC [37] (scheme 2).…”

mentioning

confidence: 99%

IADS, a Decomposition Product of DIDS Activates a Cation Conductance in <i>Xenopus</i> Oocytes and Human Erythrocytes: New Compound for the Diagnosis of Cystic Fibrosis

Stumpf

Almaça

Kunzelmann

et al. 2006

Cell Physiol Biochem

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DIDS (4,4''-diisothiocyanato-stilbene-2,2''-disulfonic acid) is a commonly used blocker of plasma membrane anion channels and transporters. We observed that DIDS undergoes decomposition while stored in DMSO (dimethyl sulfoxide) forming a biologically active compound. One decomposition product, called IADS, was identified and synthesized. Voltage-clamp and patch clamp experiments on Xenopus laevis oocytes and human erythrocytes revealed that IADS is able to activate a plasma membrane cation conductance in both cell types. Furthermore, we found that IADS induces hemolysis in red blood cells of healthy donors but fails to hemolyze erythrocytes of donors with cystic fibrosis. Thus, IADS stimulated activation of a cation conductance could form the basis for a novel diagnostic test of cystic fibrosis.

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Studies on Human Porin XXI: Gadolinium Opens Up Cell Membrane Standing Porin Channels Making Way for the Osmolytes Chloride or Taurine—A Putative Approach to Activate the Alternate Chloride Channel in Cystic Fibrosis

Cited by 19 publications

References 64 publications

Essential Role of Voltage-Dependent Anion Channel in Various Forms of Apoptosis in Mammalian Cells

Essential Role of Voltage-Dependent Anion Channel in Various Forms of Apoptosis in Mammalian Cells

Molecular and functional aspects of anionic channels activated during regulatory volume decrease in mammalian cells*

IADS, a Decomposition Product of DIDS Activates a Cation Conductance in <i>Xenopus</i> Oocytes and Human Erythrocytes: New Compound for the Diagnosis of Cystic Fibrosis

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