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  • 1
    Electronic Resource
    Electronic Resource
    Effect of intracellular pH on the rate of chloride uptake and efflux in different mammalian cell lines (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 2778-2785 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00384a019
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  • 2
    Electronic Resource
    Electronic Resource
    MEMBRANE TRAFFIC EXPLOITED BY PROTEIN TOXINS (2002)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 18 (2002), S. 1-24 
    Details
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract A large number of protein toxins having enzymatically active A- and B-moieties that bind to cell surface receptors must be endocytosed before the A-moiety is translocated into the cytosol where it exerts its cytotoxic action. The accumulated information about the most well-studied toxins has provided a detailed picture of how they exploit the membrane trafficking systems of cells, and studies of toxin trafficking have revealed the existance of new pathways. The complexity of different endocytic mechanisms, as well as the multiple routes between endosomes and the Golgi apparatus and retrogradely to the endoplasmic reticulum (ER), are being unravelled by investigations of how toxins gain access to their targets. With increasing information about the internalization and intracellular trafficking of these opportunistic toxins, new avenues have been opened for their application in areas of medicine such as drug delivery and therapy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.cellbio.18.011502.142107
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  • 3
    Electronic Resource
    Electronic Resource
    Evidence for involvement of protein kinase C in regulation of intracellular pH by Cl−/HCO 3 − antiport (1991)
    Springer
    The journal of membrane biology 119 (1991), S. 179-186 
    Details
    ISSN: 1432-1424
    Keywords: anion antiport ; pH regulation ; protein kinase C ; TPA ; HCO 3 − ; Vero cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The activity of the main base-extruding mechanism in Vero cells, the Na+-independent Cl−/HCO 3 − antiport, increases 5- to 10-fold when the cytosolic pH (pH i ) is increased over a narrow range close to neutrality. We have studied the effect on this regulation of stimulation and inhibition of protein kinase C by short-term and long-term treatment with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA). After short-term treatment with TPA to stimulate the kinase, the threshold value for activation of the antiport is shifted to a more acidic pH. After prolonged treatment with TPA to downregulate protein kinase C the sensitivity of the antiport to variation in proton concentration was lowered, possibly by reducing the number of essential protonbinding sites. Concomitantly, the steady state pH i of the cells was increased. The data indicate that protein kinase C is involved in the regulation of the Na+-independent Cl−/HCO 3 − antiport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871417
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  • 4
    Electronic Resource
    Electronic Resource
    Rapid increase in pH set-point of the Na+-in-dependent chloride/bicarbonate antiporter in vero cells exposed to heat shock (1993)
    Springer
    The journal of membrane biology 134 (1993), S. 143-153 
    Details
    ISSN: 1432-1424
    Keywords: Anion antiportkw]pH regulation ; HCO 3 + ; Heat shock ; Hyperthermia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Internal pH (pH i ) is in Vero cells regulated mainly by three antiports. Na+/H+ antiport and Na+-dependent Cl+/HCO 3 + antiport increase pH i in acidified cells, and Na+-independent Cl+/HCO 3 + antiport lowers pH i in cells after alkalinization. The activities of the antiporters were altered in cells after exposure to 41–45°C. Under such conditions the Na+/H+ antiport and the Na+-dependent Cl+/HCO 3 + antiport were both stimulated, whereas the Na+-independent Cl+/HCO 3 + antiport was inhibited in such a way that a higher pH value was required to activate it. This alteration was also induced by some other forms of cellular stress, but did most likely not involve stress proteins as protein synthesis was not required. The possibility of regulation by alteration in protein phosphorylation is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232750
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  • 5
    Electronic Resource
    Electronic Resource
    Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum (1992)
    [s.l.] : Nature Publishing Group
    Nature 358 (1992), S. 510-512 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A431 cells bind and internalize Shiga toxin but are completely resistant to it. Butyric acid sensitizes MCDK cells to Shiga toxin4, so we tested whether A431 cells could also be sensitized by this compound and found that incubation of A431 cells with butyric acid for 48 h did indeed sensitize the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/358510a0
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  • 6
    Electronic Resource
    Electronic Resource
    Protein toxins acting on intracellular targets: cellular uptake and translocation to the cytosol (1993)
    Springer
    Medical microbiology and immunology 182 (1993), S. 51-61 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00189373
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  • 7
    Electronic Resource
    Electronic Resource
    Anion requirement and effect of anion transport inhibitors on the response of vero cells to diphtheria toxin and modeccin (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 119 (1984), S. 7-14 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The anion requirement for toxic action of diphtheria toxin and modeccin was studied. In Cl--free Hepes buffer made isotonic with mannitol, cells were insensitive to diphtheria toxin and modeccin. Just 2 mM NaCl was sufficient to obtain full toxic activity of modeccin, whereas 140 mM NaCl was required for maximal intoxication with diphtheria toxin. Br- could substitute for Cl-. NO3-, I- and ClO3- were less efficient than Cl-, whereas SO42- and SCN- were unable to replace Cl-. Cl- deprivation both reduced the ability of cells to bind diphtheria toxin and prevented bound toxin from intoxicating the cells. The binding of modeccin was not reduced. SITS (4-acetamide-4′-isothio-cyano-stilbene-2,2′-disulfonic acid), an inhibitor of Cl- entry, protected against diphtheria toxin and modeccin, indicating that Cl- transport is required for intoxication.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041190103
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of potassium depletion of cells on their sensitivity to diphtheria toxin and pseudomonas toxin (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 124 (1985), S. 54-60 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When Vero cells were depleted of potassium, the cells were protected against diphtheria toxin, Potassium deletion of Vero cells strongly reduced the binding of the toxin to cell surface receptors. Likewise, potassium depleted L-cells were protected against pseudomonas toxin. Diphtheria toxin binding was completely restored upon addition of potassium to the cells. This restoration was not prevented by inhibition of protein synthesis by cycloheximide. When cells were depleted of potassium in the presence of metabolic inhibitors, and then treated with diphtheria toxin, protein synthesis was reduced to the same extent as in cells with normal intracellular level of potassium. The results indicate that potassium depletion of Vero cells reduces the ability of the cells of bind diphtheria toxin by an ATP requiring process, and that binding, endocytosis and transfer of diphtheria fragment A across the membrane may occur at low intracellular levels of potassium.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041240110
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  • 9
    Electronic Resource
    Electronic Resource
    Calmodulin antagonists sensitize cells to pseudomonas toxin (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 119 (1984), S. 15-22 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: L cells and mouse 3T3 cells, which are very sensitive to Pseudomonas aeruginosa exotoxin A (PEA), were protected with weak bases and low concentrations of monensin. BHK cells and a number of other cell lines which are much less sensitive to PEA were much less protected under these conditions. Trifluoperazine, dansylcadaverine, and several other calmodulin antagonists strongly sensitized BHK cells to the toxin whereas they did not affect the sensitivity of the mouse 3T3 and L cells. The sensitization of the BHK cells was counteracted by treatment with weak bases or low concentrations of monensin. Calmodulin antagonists also sensitized cells to toxin which had become inaccessible to antitoxin, indicating that the effect of the calmodulin antagonists is exerted on a process taking place after the toxin is endocytosed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041190104
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  • 10
    Electronic Resource
    Electronic Resource
    Entry of diphtheria toxin linked to concanavalin A into primate and murine cells (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 122 (1985), S. 193-199 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Diphtheria toxin linked by a disulfide bridge to concanavalin A was highly toxic to HeLa S3 and Vero cells, as well as to murine L cells. The cells could be protected with α-methyl mannoside, indicating that the conjugate binds mainly through its concanavalin A moiety. Treatment of Vero cells with phospholipase C, TPA (12-O-tetradecanoylphorbol-13-acetate), and vanadate, which strongly reduce the ability of the cells to bind free diphtheria toxin, had little protective effect against the conjugate, whereas SITS (L-acetamido-4′-isothiocyano-stilbene-2,2′disulfonic acid), which inhibits diphtheria toxin binding, as well as the subsequent entry, protected Vero cells, but not L cells. Both types of cells are protected against the conjugate by NH4Cl and monensin, indicating that an acidified compartment is necessary for entry into the cytosol. Exposure of cells, bound with surface conjugate, to low pH induced entry of the toxin into Vero cells, but not into L Cells. Phospholipase C, TPA, and vanadate did not protect L cells against the conjugate. It is concluded that toxin in the conjugate enters L cells by a route which involves low pH, but which is not identical to that in Vero cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041220205
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