Compartmentation of Ca2+ and its Possible Role in Volume Regulation of Poterioochromonas

  • H. Kauss
  • U. Rausch
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

There is growing evidence from animal systems that the concentration of free Ca2+ in the extra-organelle cytoplasm of resting cells is in the range of 10-7 M. External stimuli (e.g., antibody binding, light, hormones, nerve pulses) can induce an increase in the [Ca2+]cyt which in turn regulates many metabolic and developmental steps, rendering Ca2+ an important “second messenger”. Indirect evidence has often led to the suggestion, that Ca2+ may be equally important for plant cells, although in most cases measurements of [Ca2+]cyt and its changes have not been performed (Williamson 1981). There appears to be only one plant example where direct measurements of [Ca2+]cyt are available, namely internodal cells of Chara (Williamson and Ashley 1982). Using injection of the photoprotein aequorin the [Ca2+]cyt was found to be about 0.2 μM and was raised by electrical stimulation to 7 μM with a concommitant cessation of cytoplasmic streaming. Total Ca2+ in the cytoplasm of Chara is 2-8 mM, indicating that great amounts must be sequestered in organelles (as far as known mainly in mitochondria and endoplasmatic reticulumn, and vesicles derived from it). According to the above reference, short-term regulation of [Ca2+]cyt appears to occur in Chara at transport processes into and out of these organelles. Long-term regulation additionally involves transport over the tonoplast and plasma membrane, as the vacuolar and external concentrations of Ca2+ are in the mM range.

Keywords

Sucrose Albumin DMSO Shrinkage CaCl2 

Abbreviations

CTC

chorotetracycline

DCF

dichlofluanide

DMSO

dimethylsulfoxide

EGTA

ethylene glycol-bis-(2-aminoethyl ether)-N,N,N’,N’,-tetraacetic acid

IF

isofloridoside = α-D-galactosyl-1 → 1-glycerol

IFP

α-D-galactosyl-1 → 1-glycerol-3-phosphoric acid

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Beatrice MC, Palmer JW, Pfeiffer DR (1980) J Biol Chem 255: 8663–8671PubMedGoogle Scholar
  2. Blinks JR, Wier WG, Hess P, Prendergast FG (1982) Prog Biophys Mol Biol 40: 1–114PubMedCrossRefGoogle Scholar
  3. Bradford MM (1976) Anal Biochem. 72: 248–254PubMedCrossRefGoogle Scholar
  4. Hertel H, Quader H, Robinson DG, Marm6 D (1980) Plants (Berl) 149: 336–340CrossRefGoogle Scholar
  5. Jewell BR, Rfiegg JC (1966) Proc R Soc B 164: 428–459CrossRefGoogle Scholar
  6. Kauss H (1973) Plant Physiol (Bethesda) 52: 613–615CrossRefGoogle Scholar
  7. Kauss H (1981) Plant Physiol (Bethesda) 68: 420–424CrossRefGoogle Scholar
  8. Kauss H (1983) Plant Physiol (Bethesda) 71: 169–172CrossRefGoogle Scholar
  9. Kauss H. Thomson KS (1982) In: Marm6 D, Mane E, Hertel R (eds) Plasmalemma and tonoplast: their function in the plant cell. Elsevier Biomedical Press, NY, pp 255–262Google Scholar
  10. Quader H, Filner P (1980) Eur J Cell Biol 21: 301–304PubMedGoogle Scholar
  11. Reiss HD, Herth W, Schnepf E, Nobiling R (1983) Protoplasma 115: 153–159CrossRefGoogle Scholar
  12. Ringboom AJ (1979) Complexation in analytical chemistry. Krieger Publishing Co, New York, p 42Google Scholar
  13. Robinson DG, Quader H (1980) Plants (Berl) 148: 84–88CrossRefGoogle Scholar
  14. Schobert B, Untner E, Kauss H (1972) Z Pflanzenphysiol 67: 385–398Google Scholar
  15. Thomas MV (1982) Techniques in calcium research. Academic Press, London, pp 125–128Google Scholar
  16. Williamson RE (1981) What’s New in plant Physiology 12: 45–48Google Scholar
  17. Williamson RE, Ashley CC (1982) Nature (Lond) 296: 647–651CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1984

Authors and Affiliations

  • H. Kauss
    • 1
  • U. Rausch
    • 1
  1. 1.FB BiologieUniversität KaiserslauternKaiserslauternGermany

Personalised recommendations