1887

Abstract

Influx of Ca into was measured under experimental conditions which enabled measurements of initial rate of transport across the plasma membrane, without interference by the vacuolar Ca transport system. Addition of glucose or glycerol to the cells, after pre-incubation in glucose-free medium for 5 min, caused a rapid, transient increase in Ca influx, reaching a peak at 3–5 min after addition of substrate. Ethanol, or glycerol added with antimycin A, had no effect on Ca influx. We have shown previously that this increase is not mediated by an effect of the substrates on intracellular ATP levels. Changes in membrane potential accounted for only a part of the glucose-stimulated Ca influx. The roles of intracellular acidification and changes in cellular cAMP in mediating the effects of glucose on Ca influx were examined. After a short preincubation in glucose-free medium addition of glucose caused a decrease in the intracellular pH, [pH], which reached a minimum value after 3 min. A transient increase in the cellular cAMP level was also observed. Addition of glycerol also caused intracellular acidification, but ethanol or glycerol added with antimycin A had no effect on [pH]. Artificial intracellular acidification induced by exposure to isobutyric acid or to CCCP caused a transient rise in Ca influx but the extent of the increase was smaller than that caused by glucose, and the time-course was different. We conclude that intracellular acidification may be responsible for part of the glucose stimulation of Ca influx. The role of the increase in cAMP level on Ca influx was examined by measuring the effect of glucose and of artificial intracellular acidification on Ca influx in a strain which lacks adenylate cyclase activity. In this strain, addition of glucose or isobutyric acid still led to a transient increase in Ca transport. Therefore, we concluded that at least part of the increase in Ca influx in response to glucose is cAMP-independent.

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1990-12-01
2021-05-14
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References

  1. Alkon D. L., Rasmussen H. 1988; A spatial temporal model of cell activation. Science 239:998–1004
    [Google Scholar]
  2. Baum P. R., Furlong C., Byers B. 1986; Yeast gene required for spindle pole body duplication: homology of its product with Ca2+binding proteins. Proceedings of the National Academy of Science of the United States of America 83:5512–5516
    [Google Scholar]
  3. Beullens M., Mbonyi K., Geerts L., Gladines D., Detremerie K., Jans A. W. H., Thevelein J. M. 1988; Studies on the mechanism of the glucose-induced cAMP signal in glycolysis and glucose repression mutants of the yeast Saccharomyes cerevisiae . European Journal of Biochemistry 172:227–231
    [Google Scholar]
  4. Borst-Pauwels G. W. F. H. 1981; Ion transport in yeast. Biochimica et Biophysica Acta 650:88–127
    [Google Scholar]
  5. Broek D., Toda T., Michaeli T., Levin L., Birchmeier C., Zoller M., Powers S., Wigler M. 1987; The S. cerevisiae CDC25 gene-product regulates the RAS/adenylate cyclase pathway. Cell 48:789–799
    [Google Scholar]
  6. Caspani G., Tortora P., Hanozet G. M., Guerritore A. 1985; Glucose-stimulated cAMP increase may be mediated by intracellular acidification in Saccharomyces cerevisiae . FEBS Letters 186:75–79
    [Google Scholar]
  7. Daniel J., Becker J. M., Enari E., Levitzki A. 1987; The activation of adenylate cyclase by guanyl nucleotides in Saccharomyces cerevisiae is controlled by the CDC25 Start gene product. Molecular and Cellular Biology 7:3857–3861
    [Google Scholar]
  8. Davis T. N., Thorner J. 1986; Calmodulin and other calcium binding proteins in yeast. In Yeast Cell Biology pp. 477–503 Hicks J. B. Edited by New York: Alan R. Liss;
    [Google Scholar]
  9. Davis T. N., Urdea M. S., Masiarz F. R., Thorner J. 1986; Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47:423–431
    [Google Scholar]
  10. De La Peña P., Barros F., Gascon S., Ramos S., Lazo P. 1982; The electrochemical proton gradient of Saccharomyces. The role of potassium. Journal of Biochemistry 123:447–453
    [Google Scholar]
  11. Eilam Y. 1982a; Studies on calcium efflux in the yeast Saccharomyces cerevisiae . Microbios 35:95–110
    [Google Scholar]
  12. Eilam Y. 1982b; Effect of monovalent cations on calcium efflux in yeasts. Biochimica et Biophysica Acta 687:8–16
    [Google Scholar]
  13. Eilam Y. 1984; The effect of phenothiazines on the inhibition of plasma membrane ATPase and hyperpolarization of cell membranes in the yeast Saccharomyces cerevisiae . Biochimica et Biophysica Acta 769:601–610
    [Google Scholar]
  14. Eilam Y., Chernichovsky D. 1987; Uptake of Ca2+driven by membrane potential in energy depleted yeast cells. Journal of General Microbiology 133:1641–1649
    [Google Scholar]
  15. Eilam Y., Chernichovsky D. 1988; Low concentrations of trifluoperazine arrest the cell division cycle of Saccharomyces cerevisiae at two specific stages. Journal of General Microbiology 134:1063–1069
    [Google Scholar]
  16. Eilam Y., Othman M. 1990; Activation of Ca2+ influx by metabolic substrates in Saccharomyces cerevisiae : role of membrane potential and cellular ATP levels. Journal of General Microbiology 136:861–866
    [Google Scholar]
  17. Eilam Y., Lavi H., Grossowicz N. 1985a; Cytoplasmic Ca2+ homeostasis maintained by a vacuolar Ca2+ transport system in the yeast Saccharomyces cerevisiae . Journal of General Microbiology 131:623–629
    [Google Scholar]
  18. Eilam Y., Lavi H., Grossowicz N. 1985b; Active extrusion of potassium in the yeast Saccharomyces cerevisiae induced by low concentrations of trifluoperazine. Journal of General Microbiology 131:2555–2564
    [Google Scholar]
  19. Engelberg D., Perlman R., Levitzki A. 1989; Transmembrane signalling in Saccharomyces cerevisiae . Cellular Signalling 1:1–7
    [Google Scholar]
  20. Eraso P., Gancedo J. M. 1985; Use of glucose analogues to study the mechanism of glucose-mediated cAMP increase in yeast. FEBS Letters 191:51–54
    [Google Scholar]
  21. Eraso P., Mazon M. J., Gancedo J. M. 1987; Internal acidification and cAMP increase are not correlated in Saccharomyces cerevisiae . European Journal of Biochemistry 165:671–674
    [Google Scholar]
  22. Field J., Broek D., Kataoka T., Wigler M. 1987; Guanine nucleotide activation of, and competition between RAS proteins from Saccharomyces cerevisiae . Molecular and Cellular Biology 7:2128–2133
    [Google Scholar]
  23. Halachmi D., Eilam Y. 1989; Cytosolic and vacuolar Ca2+ concentration in yeast cells measured with Ca2+ sensitive fluorescence dye indo-1. FEBS Letters 256:55–61
    [Google Scholar]
  24. Hosey M., Borsotto M., Lazdunski M. 1986; Phosphorylation and dephosphorylation of the major component of the voltage dependent Ca2+ channel in skeletal muscle membranes by cyclic AMP and Ca2+ dependent processes. Proceedings of the National Academy of Sciences of the United States of America 83:3733–3737
    [Google Scholar]
  25. Kaibuchi K., Miyajima A., Arai K. -I., Matsumoto K. 1986; Possible involvement of Ras-encoded proteins in glucose-induced inositol phosphate turnover in Saccharomyces cerevisiae . Proceedings of the National Academy of Sciences of the United States of America 83:8172–8176
    [Google Scholar]
  26. Matsumoto K., Uno I., Oshuma Y., Ishikawa T. 1982; Isolation and characterization of yeast mutants deficient in adenylate cyclase and cAMP-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America 79:2355–2539
    [Google Scholar]
  27. Matsumoto K., Uno I., Ishikawa T. 1985; Genetic anlaysis of the role of cAMP in yeast. Yeast 1:15–24
    [Google Scholar]
  28. Mbonyi K., Beullens M., Detremerie K., Geerts L., Thevelein J. M. 1988; Requirement of one functional RAS gene and inability of an oncogenic ras variant to mediate the glucose-induced-cyclic AMP signal in the yeast Saccharomyces cerevisiae . Molecular and Cellular Biology 8:3051–3057
    [Google Scholar]
  29. Mean A. R., Rasmussen C. D. 1988; Calcium calmodulin and cell proliferation. Cell Calcium 9:313–319
    [Google Scholar]
  30. Ohsumi Y., Anraku Y. 1983; Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae . Journal of Biological Chemsitry 258:5614–5617
    [Google Scholar]
  31. Ohya Y., Miyamoto S., Ohsumi Y., Anraku Y. 1986; Calcium sensitive cls4 mutant of Saccharomyces cerevisiae with a defect in bud formation. Journal of Bacteriology 165:28–33
    [Google Scholar]
  32. Ohya Y., Ohsumi Y., Anraku Y. 1984; Genetic study of the role of calcium ions in the cell division cycle of Saccharomyces cerevisiae: a calcium dependent mutant and its trifluoperazine-dependent pseudoreverants. Molecular and General Genetics 193:389–394
    [Google Scholar]
  33. Purwin P., Leidig F., Holzer H. 1982; Cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase in yeast. Biochemical and Biophysical Research Communications 107:1482–1489
    [Google Scholar]
  34. Purwin C., Nicolay K., Scheffers W. A., Holzer H. 1986; Mechanism of control of adenylate cyclase activity in yeast by fermentable sugars and carbonylcyanide m-chlorophenylhydrazone. Journal of Biological Chemistry 19:8744–8749
    [Google Scholar]
  35. Reuter H. 1983; Calcium channel modulation by neurotransmitters, enzymes and drugs. Nature; London: 301569–574
    [Google Scholar]
  36. Roomans G. M., Theuvenet A. P. R., Van Den Berg TH. P. R., Borst-Pauwels G. W. F. H. 1979; Kinetics of Ca2+ and Sr2+ uptake by yeast. Effect of pH, cations and phosphate. Biochimica et Biophysica Acta 551:187–196
    [Google Scholar]
  37. Schmit H. D., Duzicha M., Gallwitz D. 1988; Study of a temperature-sensitive mutant of the ras related YPTI gene product in yeast suggests a role in the regulation of intracellular calcium. Cell 53:635–647
    [Google Scholar]
  38. Toda T., Uno I., Ishikawa T., Powers S., Kataoka T., Broek D., Cameron S., Broach J., Matsumoto K., Wigler M. 1985; In yeast, RAS proteins are controlling elements of adenylate cyclase. Cell 40:27–36
    [Google Scholar]
  39. Thevelein J. M., Beullens M., Honshoven F., Hoebeek G., Detremeris K., Griewel B., Den Hollander J. A., Jans A. W. H. 1987; Regulation of the cAMP level in the yeast Saccharomyces cerevisiae: the glucose-induced cAMP signal is not mediated by a transient drop in the intracellular pH. Journal of General Microbiology 133:2197–2205
    [Google Scholar]
  40. Valle E., Bergillos L., Gascon S., Parra F., Ramos S. 1986; Trehalase activation in yeast is mediated by an internal acidification. European Journal of Biochemistry 154:247–251
    [Google Scholar]
  41. Valle E., Bergillos L., Ramos S. 1987; External K+ affects the internal acidification caused by the addition of glucose to yeast cells. Journal of General Microbiology 133:535–538
    [Google Scholar]
  42. Ulaszewski S., Hilger F., Goffeau A. 1989; Cyclic AMP controls the plasma membrane H+-ATPase activity from Saccharomyces cerevisiae . FEBS Letters 245:131–136
    [Google Scholar]
  43. Watson J. D., Hopkins N. H., Roberts J. W., Steiz J. A., Weiner A. M. 1987 The Molecular Biology of the Gene 1 pp. 550–618 Amsterdam: Benjamin Cummings Publishing Co;
    [Google Scholar]
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