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)


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.


Cell Shrinkage Cytoplasmic Streaming Storage Vacuole Internodal Cell Algal Pellet 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.









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


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


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


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  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