Permeability change in transformed mouse fibroblasts caused by ionophores, and its relationship to membrane permeabilization by exogenous ATP

Friedberg, Ilan; Weisman, Gary A.; De, Barun K.

doi:10.1007/bf01868699

Cited by 29 publications

(13 citation statements)

References 44 publications

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“…Extracellular ATP and other nucleoside triphosphates, apparently binding to specific receptors, affect cell metabolism in many ways (4)(5)(6). Of interest here are reports that extracellular ATP elevates myo-inositol 1,4,5-trisphosphate (InsP3) and Ca2+ levels in isolated hepatocytes (7) and InsP3 levels in A-431 epidermoid carcinoma cells (3).…”

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confidence: 99%

“…Receptor from TPA-treated cells was phosphorylated largely on serine, and receptor from ATP-treated cells was phosphorylated on both serine and threonine (Fig. 5) Nucleosides and nucleoside phosphates, particularly ATP, have many effects on cells (3,5), changing inositol phosphate levels (5) and intracellular Ca2+ concentrations (7,26) and inducing phosphorylation of surface membrane proteins (27,28). Most of these effects appear to be moderated through nucleoside phosphate-specific receptors.…”

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confidence: 99%

“…Most of these effects appear to be moderated through nucleoside phosphate-specific receptors. These so-called P2 receptors vary in nucleoside phosphate specificity, depending upon cell type (5 (31).…”

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confidence: 99%

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Exogenous ATP and other nucleoside phosphates modulate epidermal growth factor receptors of A-431 epidermoid carcinoma cells.

Hosoi

Edidin

1989

Proc. Natl. Acad. Sci. U.S.A.

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The binding of epidermal growth factor (EGF) by A-431 human epidermoid carcinoma cells was reduced after exposure of the cells to low concentrations (0.01-1 mM) of ATP and other nucleoside 5'-triphosphates at 37C, but not at 00C. This was due to loss of high-affinity EGF binding sites. The modulation was associated with transient increases in inositol phosphate synthesis and intracellular Ca2+ and with phosphorylation of the EGF receptor on serine and threonine. There was no evidence for entry of labeled ATP into the cells. ATP appeared to bind to specific cell surface receptors. Such binding was demonstrated directly with the nonmetabolizable ATP analogue adenosine 5'-[.8,r-imidojtriphosphate.The binding of epidermal growth factor (EGF) to its cell surface receptors is regulated by many different molecules, including EGF itself, other peptide hormones, and tumorpromoting phorbol esters (1, 2). Regulation of EGF binding by all of these agents appears to be mediated through activation of protein kinase C and consequent phosphorylation of the EGF receptor on threonine (3). The phosphorylated EGF receptor has reduced affinity for EGF and a lower tyrosine kinase activity than the unmodified receptor (1).Extracellular ATP and other nucleoside triphosphates, apparently binding to specific receptors, affect cell metabolism in many ways (4-6). Of interest here are reports that extracellular ATP elevates myo-inositol 1,4,5-trisphosphate (InsP3) and Ca2+ levels in isolated hepatocytes (7) (DMEM) supplemented with 10% fetal bovine serum (Reheis) and 2.4 mg of glucose per ml. Cells were fed every 3-4 days and passed at 1:20 dilution once a week.Incubation with Nucleotides and EGF Binding Assay. Two days before an experiment, cells were seeded in wells of a 24-well culture plate to reach about 106 cells per well on the day of the experiment. For assay, each well was washed twice with 0.5 ml of phosphate-buffered saline (PBS: 0.14 M NaCl/0.02 M phosphate buffer/0.01 M KCI, pH 7.0) containing 0.1% bovine serum albumin (BSA). Washed cells were first incubated in serum-free DMEM supplemented with 0.1% BSA and 2.4 mg of glucose per ml, with added nucleoside phosphates as appropriate. Unless otherwise stated, the final pH of the mixture was 7.5. After this incubation at 0°C or at 37°C, cells were chilled and washed twice with 0.5 ml of PBS/0.1% BSA. Mixtures of 0.1-0.2 nM 1251-labeled EGF and 0.1-40 nM unlabeled EGF were added to washed cells in 250 ,ld ofbinding buffer (140 mM NaCl/5 mM KCI/1.8 mM CaCl2/1 mM MgCl2/20 mM Hepes/0.1% BSA, final pH 7.0) and the plates were incubated on ice for 4 hr, by which time specific binding reached a plateau. Nonspecific binding was always <5% of the total binding. After incubation, cells were washed three times with cold PBS/0.1% BSA and then lysed in 0.1 M NaOH/1% SDS/2% Na2CO3 (250 IlI per well).Two hundred microliters of the lysate was taken for 1251I determination with a Beckman 'y counter. All experiments were done in duplicate and mean values were computed after normalization...

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confidence: 99%

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Exogenous ATP and other nucleoside phosphates modulate epidermal growth factor receptors of A-431 epidermoid carcinoma cells.

Hosoi

Edidin

1989

Proc. Natl. Acad. Sci. U.S.A.

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“…0.05 mM). Our previous studies have shown that the increase in the membrane permeability is preceded by ion fluxes across the cell membrane and a reduction of the membrane potential [16,18,19]. The membrane potential was measured by the accumulation of the hydrophobic cation TPP + in the cells.…”

Section: Figurementioning

confidence: 99%

Combined effects of ATP and its analogs on the membrane permeability in transformed mouse fibroblasts

Arav

Friedberg

1996

FEBS Letters

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Extracellular ATP (0.6 mM) induces a marked decrease in the membrane potential, followed by an increase in cell membrane permeability in transformed mouse fibroblasts. The effects of the ATP analogs, pICHaIppA and p[NH]ppA (0.6 m VI), on the membrane potential and permeability are much less pronounced. ATP at 0.05 mM has no effect by itself, but markedly increases the analog-induced membrane potential di~ipation and permeability. The data suggest that ATP-induced membrane permeation is composed of two processes: One is common to ATP and its analogs and appears to be a receptormediated process. The second is unique for ATP, effective even at low concentration (0.05 mM), and might be mediated by cell surface enzymes, for which ATP, but not its analogs, serves as a substrate.

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“…Gramicidins A, B, and C have alternating D and L residues, and their most relevant property is the ability to form helical dimers that penetrate cell membranes to form an ion channel, rendering the membrane permeable to protons and the monovalent cations Na ϩ and K ϩ (74). Gramicidin D has been used extensively for structural studies of ion channels in model membranes and has been shown to cause Na ϩ influx and K ϩ efflux in mammalian cells (28,39,44,74). The selective permeabilization of membranes presumably accounts for the neutralization of human immunodeficiency virus and HSV by gramicidin D (5).…”

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Induction of Cellular Stress Overcomes the Requirement of Herpes Simplex Virus Type 1 for Immediate-Early Protein ICP0 and Reactivates Expression from Quiescent Viral Genomes

Preston

Nicholl

2008

J Virol

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Herpes simplex virus type 1 (HSV-1) mutants impaired in the activities of the structural protein VP16 and the immediate-early (IE) proteins ICP0 and ICP4 establish a quiescent infection in human fibroblasts, with most cells retaining an inactive, repressed viral genome for sustained periods in culture. To date, the quiescent state has been considered stable, since it has been reversed only by provision of herpesviral proteins, such as ICP0, not by alteration of the cell physiological state. We report that the interaction of HSV-1 with human fibroblasts can be altered significantly by transient treatment of cultures with sodium arsenite, an inducer of heat shock and oxidative stress, or gramicidin D, a toxin that selectively permeabilizes cell membranes, prior to infection. These regimens stimulated gene expression from IE-deficient HSV-1 mutants in a promoter sequence-independent manner and also overcame the replication defect of ICP0-null mutants. Reactivation of gene expression from quiescent HSV-1 genomes and the resumption of virus replication were observed following addition of arsenite or gramicidin D to cultures. Both agents induced reorganization of nuclear domain 10 structures, the sites of quiescent genomes, but appeared to do so through different mechanisms. The results demonstrate that the physiological state of the cell is important in determining the outcome of infection with IE-deficient HSV-1 and show novel methods for reactivating quiescent HSV-1 in fibroblasts with a high efficiency.Transcription of the herpes simplex virus type 1 (HSV-1) genome at early stages of infection is controlled by the activities of three viral proteins, VP16, ICP4, and ICP0. VP16 is a virion component that stimulates immediate-early (IE) transcription through interaction with the cellular proteins Oct-1 and HCF-1 (51, 77). ICP4 is an IE protein that is essential for early and late gene expression, acting on basal cellular transcription factors (10,64,80). The IE protein ICP0 exerts a general stimulatory effect on HSV-1 transcription and is important for initiation of the viral gene expression program (17,19,31,61,68).The VP16 and ICP4 proteins can be viewed as conventional transcription activators since they interact with cellular factors that localize to promoter regions of the viral genome. In contrast, the effects of ICP0 are not promoter specific or even restricted to the HSV-1 genome, since the protein stimulates gene expression from a variety of plasmids and viruses (3,18,30,31,48,52). One of the most striking features of ICP0 is its effect on cellular intranuclear structures known as promyelocytic leukemia (PML) bodies or nuclear domain 10 (ND10). Early in infection, ICP0 localizes to ND10 and directs the disruption of these bodies (21,22). Protein components of ND10, including the PML protein itself, are targeted for degradation due to a ubiquitin E3 ligase activity that requires the RING domain of ICP0 (6,21,25). HSV-1 mutants that lack the ICP0 coding region exhibit a multiplicity-and cell type-dependent def...

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Permeability change in transformed mouse fibroblasts caused by ionophores, and its relationship to membrane permeabilization by exogenous ATP

Cited by 29 publications

References 44 publications

Exogenous ATP and other nucleoside phosphates modulate epidermal growth factor receptors of A-431 epidermoid carcinoma cells.

Exogenous ATP and other nucleoside phosphates modulate epidermal growth factor receptors of A-431 epidermoid carcinoma cells.

Combined effects of ATP and its analogs on the membrane permeability in transformed mouse fibroblasts

Induction of Cellular Stress Overcomes the Requirement of Herpes Simplex Virus Type 1 for Immediate-Early Protein ICP0 and Reactivates Expression from Quiescent Viral Genomes

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