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Chemical Compound Review

CLZN     5-benzyl-3-(4-hydroxyphenyl)- 8-[(4...

Synonyms: coelenterazine, SureCN64690, CHEMBL276558, CHEBI:2311, AG-K-40209, ...
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Disease relevance of Renilla luciferin


High impact information on Renilla luciferin


Biological context of Renilla luciferin


Anatomical context of Renilla luciferin

  • We have measured the [Ca2+] in the endoplasmic reticulum ([Ca2+]er) of intact HeLa cells at both 22 degrees C and 37 degrees C using endoplamsic reticulum-targeted, low Ca2+ affinity aequorin reconstituted with coelenterazine n [12].
  • In human whole blood or isolated leukocytes, the sensitivity of the luminol analogue L-012 to detect superoxide was higher as compared with luminol, lucigenin, coelenterazine, and the fluorescence dye dihydroethidine [13].
  • For spatial and quantitative kinetic analysis of protein-protein interactions (PPIs) in living mammalian cells, a method was developed in which PPI-induced complementation of split Renilla luciferase triggers spontaneous emission of luminescence using a cell membrane permeable substrate, coelenterazine [14].
  • This coelenterazine analogue could be used as a model compound for investigating the action mechanism of imidazolopyrazinones in mammalian hepatocytes [15].
  • In our hands, only 0.3% of this apo-aequorin combined with coelenterazine entering from the medium to form aequorin, which was not enough for calcium imaging of the oocytes, but did allow in vivo imaging of the ovaries [16].

Associations of Renilla luciferin with other chemical compounds


Gene context of Renilla luciferin


Analytical, diagnostic and therapeutic context of Renilla luciferin

  • Furthermore, d-luciferin (a substrate for FL) does not serve as a substrate for RL, and coelenterazine does not serve as a substrate for FL either in cell culture or in living mice [6].
  • Recombinant aequorin proteins were synthesized by PCR followed by in vitro transcription/translation, and characterized by specific activity, stability, and affinity for coelenterazine [26].
  • Continuous perfusion of HeLa cells, expressing ER-targeted apoaequorin, with coelenterazine allowed the apoprotein to act as a pseudo-luciferase capable of reporting free Ca2+ from 0.1-100 microM [27].


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  2. A study of protein-protein interactions in living cells using luminescence resonance energy transfer (LRET) from Renilla luciferase to Aequorea GFP. Wang, Y., Wang, G., O'Kane, D.J., Szalay, A.A. Mol. Gen. Genet. (2001) [Pubmed]
  3. Lucigenin and coelenterazine as superoxide probes in mitochondrial and bacterial membranes. Kervinen, M., Pätsi, J., Finel, M., Hassinen, I.E. Anal. Biochem. (2004) [Pubmed]
  4. Imaging calcium dynamics in living plants using semi-synthetic recombinant aequorins. Knight, M.R., Read, N.D., Campbell, A.K., Trewavas, A.J. J. Cell Biol. (1993) [Pubmed]
  5. Imaging reversal of multidrug resistance in living mice with bioluminescence: MDR1 P-glycoprotein transports coelenterazine. Pichler, A., Prior, J.L., Piwnica-Worms, D. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  6. Optical imaging of Renilla luciferase reporter gene expression in living mice. Bhaumik, S., Gambhir, S.S. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Oxygen radical inhibition of nitric oxide-dependent vascular function in sickle cell disease. Aslan, M., Ryan, T.M., Adler, B., Townes, T.M., Parks, D.A., Thompson, J.A., Tousson, A., Gladwin, M.T., Patel, R.P., Tarpey, M.M., Batinic-Haberle, I., White, C.R., Freeman, B.A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Chemiluminescent detection of oxidants in vascular tissue. Lucigenin but not coelenterazine enhances superoxide formation. Tarpey, M.M., White, C.R., Suarez, E., Richardson, G., Radi, R., Freeman, B.A. Circ. Res. (1999) [Pubmed]
  9. Thermostable mutants of the photoprotein aequorin obtained by in vitro evolution. Tsuzuki, K., Tricoire, L., Courjean, O., Gibelin, N., Rossier, J., Lambolez, B. J. Biol. Chem. (2005) [Pubmed]
  10. Involvement of MAP kinase in insulin signalling revealed by non-invasive imaging of luciferase gene expression in single living cells. Rutter, G.A., White, M.R., Tavaré, J.M. Curr. Biol. (1995) [Pubmed]
  11. Design, synthesis, and evaluation of the transition- state inhibitors of coelenterazine bioluminescence: probing the chiral environment of active site. Nakamura, H., Wu, C., Inouye, S., Murai, A. J. Am. Chem. Soc. (2001) [Pubmed]
  12. Dynamics of [Ca2+] in the endoplasmic reticulum and cytoplasm of intact HeLa cells. A comparative study. Barrero, M.J., Montero, M., Alvarez, J. J. Biol. Chem. (1997) [Pubmed]
  13. Measurement of NAD(P)H oxidase-derived superoxide with the luminol analogue L-012. Daiber, A., August, M., Baldus, S., Wendt, M., Oelze, M., Sydow, K., Kleschyov, A.L., Munzel, T. Free Radic. Biol. Med. (2004) [Pubmed]
  14. Locating a protein-protein interaction in living cells via split Renilla luciferase complementation. Kaihara, A., Kawai, Y., Sato, M., Ozawa, T., Umezawa, Y. Anal. Chem. (2003) [Pubmed]
  15. Antioxidative properties of natural coelenterazine and synthetic methyl coelenterazine in rat hepatocytes subjected to tert-butyl hydroperoxide-induced oxidative stress. Dubuisson, M.L., de Wergifosse, B., Trouet, A., Baguet, F., Marchand-Brynaert, J., Rees, J.F. Biochem. Pharmacol. (2000) [Pubmed]
  16. Expression of apo-aequorin during embryonic development; how much is needed for calcium imaging? Créton, R., Steele, M.E., Jaffe, L.F. Cell Calcium (1997) [Pubmed]
  17. Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence. Haddock, S.H., Rivers, T.J., Robison, B.H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  18. Recombinant Gaussia luciferase. Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridization. Verhaegent, M., Christopoulos, T.K. Anal. Chem. (2002) [Pubmed]
  19. Mechanism of photoinactivation and re-activation in the bioluminescence system of the ctenophore Mnemiopsis. Anctil, M., Shimomura, O. Biochem. J. (1984) [Pubmed]
  20. Mitochondrial adaptations within chronically ischemic swine myocardium. McFalls, E.O., Sluiter, W., Schoonderwoerd, K., Manintveld, O.C., Lamers, J.M., Bezstarosti, K., van Beusekom, H.M., Sikora, J., Ward, H.B., Merkus, D., Duncker, D.J. J. Mol. Cell. Cardiol. (2006) [Pubmed]
  21. Regeneration and luminescence of aequorin in Chinese hamster ovary cells transformed with cDNA for apoaequorin. Sanchez-Bueno, A., Yoshida, R., Tsuji, F.I. Int. J. Biochem. Cell Biol. (1996) [Pubmed]
  22. Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils. Lucas, M., Solano, F. Anal. Biochem. (1992) [Pubmed]
  23. Coelenterazine: a two-stage antioxidant in lipid micelles. de Wergifosse, B., Dubuisson, M., Marchand-Brynaert, J., Trouet, A., Rees, J.F. Free Radic. Biol. Med. (2004) [Pubmed]
  24. Endothelin-1 induces NAD(P)H oxidase in human endothelial cells. Duerrschmidt, N., Wippich, N., Goettsch, W., Broemme, H.J., Morawietz, H. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  25. Expression, purification and characterization of calcium-triggered luciferin-binding protein of Renilla reniformis. Inouye, S. Protein Expr. Purif. (2007) [Pubmed]
  26. Requirement of the C-terminal proline residue for stability of the Ca(2+)-activated photoprotein aequorin. Watkins, N.J., Campbell, A.K. Biochem. J. (1993) [Pubmed]
  27. Recombinant apoaequorin acting as a pseudo-luciferase reports micromolar changes in the endoplasmic reticulum free Ca2+ of intact cells. Kendall, J.M., Badminton, M.N., Sala-Newby, G.B., Campbell, A.K., Rembold, C.M. Biochem. J. (1996) [Pubmed]
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