Fol. Biol. 2015, 61, 134-139

https://doi.org/10.14712/fb2015061040134

Aequorin as Intracellular Ca2+ Indicator Incorporated in Follicular Lymphoma Cells by Hypoosmotic Shock Treatment

M. Klabusay1,2, J. Skopalík3, S. Erceg4, Aleš Hrdlička5

1Department of Comprehensive Cancer Care, Masaryk Memorial Cancer Institute, Brno, Czech Republic
2Department of Haemato-Oncology and Department of Internal Medicine – Cardiology, Faculty of Medicine, Palacký University, Olomouc, Czech Republic
3International Clinical Research Center – Center of Biomedical Engineering, St. Anne’s University Hospital, Brno, Czech Republic
4Stem Cells Therapies in Neurodegenerative Diseases Lab, Research Centre “Principe Felipe”, Valencia, Spain
5International Clinical Research Center – Integrated Center of Cellular Therapy and Regenerative Medicine, St. Anne’s University Hospital, Brno, Czech Republic

Received November 2014
Accepted June 2015

References

1. Allen, D. G., Blinks, J. R., Prendergast, F. G. (1977) Aequorin luminescence: relation of light emission to calcium concentration – a calcium-independent component. Science 195, 996-998. <https://doi.org/10.1126/science.841325>
2. Alvarez, J., Montero, M. (2002) Measuring [Ca2+] in the endoplasmic reticulum with aequorin. Cell Calcium 32, 251-260. <https://doi.org/10.1016/S0143416002001860>
3. Barber, K., Mala, R. R., Lambert, M. P., Qiu, R., MacDonald, M. C., Klein, W. L. (1996) Delivery of membrane-impermeant fluorescent probes into living neural cell populations by lipotransfer. Neurosci. Lett. 207, 17-20. <https://doi.org/10.1016/0304-3940(96)12497-6>
4. Borle, A. B., Snowdowne, K. W. (1982) Measurement of intracellular free calcium in monkey kidney cells with aequorin. Science 217, 252-254. <https://doi.org/10.1126/science.6806904>
5. Borle, A. B., Freudenrich C. C., Snowdowne, K. W. (1986) A simple method for incorporating aequorin into mammalian cells. Am. J. Physiol. 25, C323-C326. <https://doi.org/10.1152/ajpcell.1986.251.2.C323>
6. Brini, M., Marsault, R., Bastianutto, C. B., Alvarez, J., Pozzan, T., Rizutto, R. (1995) Transfected aequorin in the measurement of cytosolic Ca2+ concentration ([Ca2+]c). A critical evaluation. J. Biol. Chem. 270, 9896-9903. <https://doi.org/10.1074/jbc.270.17.9896>
7. Dikici, E., Qu, X., Rowe, L., Millner, L., Logue, C., Deo, S. K., Ensor M., Daunert S. (2009) Aequorin variants with improved bioluminescence properties. Protein Eng. Des. Sel. 22, 243-248. <https://doi.org/10.1093/protein/gzn083>
8. Feske, S. (2007) Calcium signalling in lymphocyte activation and disease. Nat. Rev. Immunol. 7, 690-702. <https://doi.org/10.1038/nri2152>
9. Hallett, M. B., Campbell A. K. (1982) Measurement of changes in cytoplasmic free Ca2+ in fused cell hybrids. Nature 295, 155-158. <https://doi.org/10.1038/295155a0>
10. Hauschildt, S., Lückhoff, A., Langhorne, J., Wiesmüller, K.- H., Jung, G., Bessler, W., Cambier, J. C. (1991) Increase in the intracellular free calcium concentration is not an obligatory early event in lipopeptide-induced B-cell activation. Immunology 73, 366-368.
11. Johnson, P. C., Ware, J. A., Cliveden, P. B., Smith, M., Dvorak, A. M., Salzman, E. W. (1985) Measurement of ionized calcium in blood platelets with the photoprotein aequorin. Comparison with Quin 2. J. Biol. Chem. 260, 2069-2076. <https://doi.org/10.1016/S0021-9258(18)89517-5>
12. Kendall, J. M., Dormer, R. L., Campbell, A. K. (1992) Targeting aequorin to the endoplasmic reticulum of living cells. Biochem. Biophys. Res. Commun. 189, 1008-1016. <https://doi.org/10.1016/0006-291X(92)92304-G>
13. Klabusay, M., Blinks, J. R. (1996) Some commonly overlooked properties of calcium buffer systems: a simple method for detecting and correcting stoichiometric imbalance in CaEGTA stock solutions. Cell Calcium 20, 227-234. <https://doi.org/10.1016/S0143-4160(96)90028-7>
14. McNeil, P. L., Murphy, R. F., Lanni, F., Taylor, D. L. (1984) A method for incorporating macromolecules into adherent cells. J. Cell Biol. 98, 1556-1564. <https://doi.org/10.1083/jcb.98.4.1556>
15. Meech, R. W. (1981) Microinjection. In: Techniques in Cellular Physiology, ed. Baker, P. F., pp. 1-16, Elsevier/ North Holland Scientific, Amsterdam.
16. Merrit, J. E., McCarthy, S. A., Davies, M. P., Moores, K. E. (1990) Use of fluo-3 to measure cytosolic Ca2+ in platelets and neutrophils. Loading cells with the dye, calibration of traces, measurements in the presence of plasma, and buffering of cytosolic Ca2+. Biochem. J. 269, 513-519. <https://doi.org/10.1042/bj2690513>
17. Núñez, L., Villalobos, C., Alonso, M. T., García-Sancho, J. (2010): Ca2+ imaging of intracellular organelles: mitochondria. In: Calcium Measurement Methods, Neuromethods, vol. 43, eds. Verkhratsky, A., Petersen, O. H., pp. 169-188, Humana Press, Totowa, NJ
18. Pozzan, T., Rizzuto, R. (2008) Imaging calcium dynamics using targeted recombinant aequorins. CSH Protocols 8. <https://doi.org/10.1101/pdb.top26>
19. Radošević, K., de Grooth, B. G., Greve, J. (1995) Changes in intracellular calcium concentration and pH of target cells during the cytotoxic process: a quantitative study at the single cell level. Cytometry 20, 281-289. <https://doi.org/10.1002/cyto.990200403>
20. Rink, T. J., Tsien, R. Y., Pozzan, T. (1982) Cytoplasmic pH and free Mg2+ in lymphocytes. J. Cell Biol. 95, 189-196. <https://doi.org/10.1083/jcb.95.1.189>
21. Rowe, L., Rothert, A., Logue, C., Ensor, C. M., Deo, S. K., Daunert, S. (2008) Spectral tuning of photoproteins by partnering site-directed mutagenesis strategies with the incorporation of chromophore analogs. Protein Eng. Des. Sel. 21, 73-81. <https://doi.org/10.1093/protein/gzm073>
22. Rowe, L., Dikici, E., Daunert, S. (2009) Engineering bioluminescent proteins: expanding their analytical potential. Anal. Chem. 81, 8662-8668. <https://doi.org/10.1021/ac9007286>
23. Shimomura, O., Johnson, F. H., Saiga, Y. (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59, 223-239. <https://doi.org/10.1002/jcp.1030590302>
24. Shimomura, O. (1995) A short story of aequorin. Biol. Bull. 189, 1-5. <https://doi.org/10.2307/1542194>
25. Snowdowne, K. W., Borle, A. B. (1984) Measurement of cytosolic free calcium in mammalian cells with aequorin. Am. J. Physiol. 247, C396-C408. <https://doi.org/10.1152/ajpcell.1984.247.5.C396>
26. Snowdowne, K. W., Ertel, R. J., Borle, A. B. (1985) Measurement of cytosolic calcium with aequorin in dispersed rat ventricular cells, J. Mol. Cell. Cardiol. 17, 233-241. <https://doi.org/10.1016/S0022-2828(85)80006-7>
27. Takahashi, A., Camacho, P., Lechleiter, J. D., Herman, B. (1999) Measurement of intracellular calcium. Physiol. Rev. 79, 1089-1125. <https://doi.org/10.1152/physrev.1999.79.4.1089>
28. Vysotski, E. S., Markova, S. V., Frank, L. A. (2006) Calciumregulated photoproteins of marine coelenterates. Mol. Biol. 40, 355-367. <https://doi.org/10.1134/S0026893306030022>
29. Ware, J. A., Smith, M., Fossel, E. T., Salzman, E. W. (1988) Cytoplasmic Mg2+ concentration in platelets: implications for determination of Ca2+ with aequorin. Am. J. Physiol. 255, H855-H859.
30. Ware, J. A., Saitoh, M., Smith, M., Johnson, P. C., Salzman, E. W. (1989) Response of aequorin-loaded platelets to activators of protein kinase C. Am. J. Physiol. 256, C35-C43. <https://doi.org/10.1152/ajpcell.1989.256.1.C35>
front cover

ISSN 0015-5500 (Print) ISSN 2533-7602 (Online)

Open access journal

Submissions

Archive