Abstract
Calcium has been studied for some time in animal cells because of its action as an intracellular second messenger. In recent years a similarly exciting role for calcium has been emerging in plant cells. To begin to understand the role of calcium in cellular processes it is essential to be able to measure fluctuations in the concentration of this ion, and for this reason developments in the technology of calcium measurement have increased along with the developing interest in calcium as a second messenger. Not all techniques that are useful for measuring cytosolic calcium in animal cells are suitable for use with plants. The use of calcium-sensitive fluorescent dyes has met with a number of problems in plants and fungi [1, 2]. Recombinant aequorin technology described in this chapter was developed in order to counter some of these problems. It also has advantages of its own [3].
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Callaham DA, Hepler PK (1991) Measurement of free calcium in plant cells. In Cellular Calcium. A practical approach. (JG McCormack, PH Cobbold, eds.), pp 383–412. Oxford University Press, Oxford, England.
Knight H, Trewavas AJ, Read ND (1993) Confocal microscopy of living fungal hyphae microinjected with Ca2+-sensitive fluorescent dyes. Mycol Res 97: 1505–1515.
Knight MR, Campbell AK, Smith SM, Trewavas AJ (1991) Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium. Nature 352: 524–526.
Shimomura O, Johnson FH (1978) Peroxidised coelenterazine the active group in the photoprotein aequorin. Proc Natl Acad Sci USA 75: 2611–2615.
Charbonneau H, Walsh KA, McCann RO, Prendergast FG, Cormier MJ, Vanaman TC (1985) Amino acid sequence of the calcium-dependent photoprotein aequorin. Biochem 24: 6762–6771.
Musicki B, Kishi Y, Shimomura O (1986) Structure of the functional part of photoprotein Aequorin. J Chem Soc Chem Commun 21: 1566–1568.
Ridgway EB, Ashley CC (1967) Intracellular injection of the Ca2+-sensitive bioluminescent protein aequorin into giant single muscle fibers of the corn barnacle Balanus nubilis. Biochem Biophys Res Commun 29: 229–234.
Williamson RE, Ashley CC (1982) Free Ca2+ and cytoplasmic streaming in the alga Chara. Nature: 296, 647–650.
Cobbold PH, Rink TJ (1987) Fluorescence and bioluminescence measurement of cytoplasmic free calcium. Biochem J 248: 313–328.
Campbell AK (1988) Chemiluminescence Principles and Applications in Biology and Medicine. Ellis Horwood Ltd., Chichester, England.
Gilroy S, Hughes WA, Trewavas AJ (1989) A comparison between quin-2 and aequorin as indicators of cytoplasmic calcium levels in higher plant cell protoplasts. Plant Physiol 90: 482–491.
Watkins NJ, Campbell AK (1993) Requirement of the C-terminal proline residue for stability of the Ca2+-activated photoprotein aequorin. Biochem J 293: 181–185.
Johnson CH, Knight MR, Kondo T, Masson P, Sedbrook J, Haley A, Trewavas AJ (1995) Circadian oscillations in cytosolic and chloroplastic free calcium in transgenic luminous plants. Science 269: 1863–1865.
Knight H, Trewavas AJ, Knight MR (1996) Cold calcium signaling involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8: 489–503.
Stanley PE (1992) A survey of more than 90 commercially available luminometers and imaging devices for low-light measurements of chemiluminescence and bioluminescence, including instruments for manual, automatic and specialised operation, for HPLC, LC, GLC and microtitre plates. Part 1 Descriptions. J Biolumin Chemilumin 7: 77–108.
Knight MR, Read ND, Campbell AK, Trewavas AJ (1993) Imaging calcium dynamics in living plants using semi-synthetic recombinant aequorins. J Cell Biol 121: 83–90.
Campbell AK, Trewavas AJ, Knight MR (1996) Calcium imaging shows differential sensitivity to cooling and communication in luminous transgenic plants. Cell Calcium (in press).
An G, Ebert PR, Mitra A, Ha SB (1988) Binary vectors. In Plant Molecular Biology Manual (SB Gelvin, RA Schilperoort, eds.), pp A3: 1–19. Kluwer Academic Publishers, Dordrecht.
Valvekens D, van Montagu M, van Lijsebettens M (1988) Agrobacterium tumifaciens-mediated transformation of Arabidopsis thaliana root expiants by using kanamycin selection. Proc Natl Acad Sc. USA 85: 5536–5540.
Balcells L (1992) Valvekens’s protocol: A guide to high efficiency transformation. In Arabidopsis: The Compleat Guide (D Flanders, C Dean, eds.). Agriculture and Food Research Program Plant Molecular Biology Arabidopsis Program, Norwich, UK.
Murashige T, Skoog F (1962) A revised medium for rapid growth an bioassays with tobacco tissue cultures. Plant Physiol 15: 473–497.
Birch RG, Franks T (1991) Development and optimisation of microprojectile systems for plant genetic transformation. Austr J Plant Physiol 18: 453–69.
Watkins NJ (1995) Engineering the calcium activated photoprotein aequorin as an intracellular calcium indicator in bacteria and plants. PhD Thesis, University of Wales.
Bevan M (1984) Binary Agrobacterium vectors for plant transformation. Nucleic acids res 12: 8711–8721.
Badminton MN, Kendall JM, Sala-Newby G, Campbell AK (1995) Nucleoplasmin-targeted aequorin provides evidence for a nuclear calcium barrier. Exp. Cell Res. 216: 236–243.
Kendall JM, Dormer RL, Campbell AK (1992) Targeting aequorin to the endoplasmic reticulum of living cells. Biochem. Biophys. Res Commun. 189: 1008–1016.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Kluwer Academic Publishers
About this chapter
Cite this chapter
Knight, H., Trewavas, A.J., Knight, M.R. (1997). Recombinant aequorin methods for measurement of intracellular calcium in plants. In: Gelvin, S.B., Schilperoort, R.A. (eds) Plant Molecular Biology Manual. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5400-0_1
Download citation
DOI: https://doi.org/10.1007/978-94-011-5400-0_1
Publisher Name: Springer, Dordrecht
Print ISBN: 978-0-7923-4205-2
Online ISBN: 978-94-011-5400-0
eBook Packages: Springer Book Archive