Studies on Human Porin XXII: Cell Membrane Integrated Human Porin Channels Are Involved in Regulatory Volume Decrease (RVD) of HeLa Cells

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

doi:10.1006/mgme.2000.2976

Cited by 33 publications

(13 citation statements)

References 45 publications

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“…There is evidence that anti-porin antibodies that have their epitopes in the extracytoplasmic side can be used as functional agents that alter the porin channel. The monoclonal antibody we used in our studies, that has the epitope in the N-terminal region of porin, is functional in the sense that it blocks the large-conductance porin channel (Dermietzel et al, 1994), and it prevents regulatory volume decrease in HeLa cells (Thinnes et al, 2000). This antibody was also functional in that it reduced the ischaemia-induced mitochondrial depolarization in neurons, and prevented the deterioration of neuronal electrical characteristics (Perez Velazquez et al, 2000).…”

Section: Discussionmentioning

confidence: 89%

Anti-Porin Antibodies Prevent Excitotoxic and Ischemic Damage to Brain Tissue

Velázquez

Kokarovtseva

Weisspapir

et al. 2003

Journal of Neurotrauma

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The mitochondrial permeability transition (MPT) is a converging event for different molecular routes leading to cellular death after excitotoxic/oxidative stress, and is considered to represent the opening of a pore in the mitochondrial membrane. There is evidence that the outer mitochondrial membrane protein porin is involved in the MPT and apoptosis. We present here a proof-of-principle study to address the hypothesis that anti-porin antibodies can prevent excitotoxic/ischemia-induced cell death. We generated anti-porin antibodies and show that the F(ab)(2) fragments penetrate living cells, reduce Ca(2+)-induced mitochondrial swelling as other MPT blockers do, and decrease neuronal death in dissociated and organotypic brain slice cultures exposed to excitotoxic and ischemic episodes. These observations present direct evidence that anti-porin antibody fragments prevent cell damage in brain tissue, that porin is a crucial protein involved in mitochondrial and cell dysfunction, and that it is conceivable that antibodies can be used as therapeutic agents.

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Section: Discussionmentioning

confidence: 89%

Anti-Porin Antibodies Prevent Excitotoxic and Ischemic Damage to Brain Tissue

Velázquez

Kokarovtseva

Weisspapir

et al. 2003

Journal of Neurotrauma

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“…According to this hypothesis the appearance of one or the other channel type would depend on the prevailing -as yet not determined exactly -physiological regulation state of VDAC under certain experimental conditions [298]. The hypothesis of VDAC being the molecular candidate of RVDC or being involved in RVD is based primarily on the finding that preincubation of HeLa cells with monoclonal antibodies to VDAC blocks RVD in these cells [296]. 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.…”

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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“…The first evidence for the idea that VDAC play a role in cell volume regulation was reported for HeLa cells where the regulatory volume decrease (RVD) was blocked after hypotonic challenge by pre-incubation of the cells with anti-hVDAC1 antibodies [47]. Recently, Okada et al [30] reported that tracheal and nasal epithelial cells from VDAC1 knockout mice show a slower RVD than wildtype cells.…”

Section: Discussionmentioning

confidence: 97%

“…The presence of VDAC in the plasma membrane has also been reported [3,5]. Several studies suggest that VDAC present in the plasma membrane act as anion channels involved in the volume regulatory mechanisms of the cell [30,47].…”

Section: Introductionmentioning

confidence: 90%

Localisation and function of voltage-dependent anion channels (VDAC) in bovine spermatozoa

Triphan

Menzel

Petrunkina

et al. 2007

Pflugers Arch - Eur J Physiol

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Sperm motility, regulation of cell volume, sperm capacitation, acrosome reaction and tight binding of spermatozoa to the zona pellucida are crucial events in the process of fertilisation. Voltage-dependent anion channels (VDAC) are highly conserved pore-forming proteins implicated in apoptosis, metabolite transport between mitochondria and cytosol, energy metabolism, and cell volume regulation in somatic cells. Several studies have demonstrated the presence of VDAC in cell compartments other than mitochondria. In previous studies using immunofluorescence, we were able to localise VDAC2 and VDAC3 in outer dense fibres of the bovine sperm flagellum. Furthermore, we described the presence of VDAC2 in the head of bovine sperm. In the present study, we confirm the localisation of VDAC2 in the acrosomal region of bovine spermatozoa using immunoelectron microscopy. After incubation with anti-VDAC antibodies raised against each VDAC isoform, bovine spermatozoa showed an increased loss of the acrosomal cap, noticeable changes in the surface of the head, coiled tails and an increased cell volume. The incubation of bovine spermatozoa with anti-VDAC antibodies might lead to alteration of the intracellular ion concentration that causes changes in the cell volume, followed by destabilization of the cytoskeleton and, finally, to loss of the acrosomal cap.

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Studies on Human Porin XXII: Cell Membrane Integrated Human Porin Channels Are Involved in Regulatory Volume Decrease (RVD) of HeLa Cells

Cited by 33 publications

References 45 publications

Anti-Porin Antibodies Prevent Excitotoxic and Ischemic Damage to Brain Tissue

Anti-Porin Antibodies Prevent Excitotoxic and Ischemic Damage to Brain Tissue

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

Localisation and function of voltage-dependent anion channels (VDAC) in bovine spermatozoa

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