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Evidence For De Novo Biosynthesis of Coelenterazine in the Bioluminescent Midwater Shrimp, Systellaspis Debilis C

Published online by Cambridge University Press:  11 May 2009

Catherine M. Thomson ,
Peter J. Herring  and
Anthony K. Campbell
Catherine M. Thomson
Affiliation:
Department of Medical Biochemistry, University of Wales College of Medicine, Heath Park, Cardiff, CF4 4XN
Peter J. Herring
Affiliation:
Institute of Oceanographic Sciences, Deacon Laboratory, Brook Road, Wormley, Godakning, Surrey, GU8 5UB
Anthony K. Campbell
Affiliation:
Institute of Oceanographic Sciences, Deacon Laboratory, Brook Road, Wormley, Godakning, Surrey, GU8 5UB
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Extract

Coelenterazine chemiluminescence is now established as the most common chemistry responsible for bioluminescence in the sea, being found in seven phyla. However, the organisms which synthesize coelenterazine have yet to be identified. In order to deter-mine whether the luminous midwater shrimp Systellaspis debilis (A. Milne Edwards) (Arthropoda: Decapoda) is capable of luciferin biosynthesis, a developmental series of eggs was assayed for its luciferin, coelenterazine. The advantages of this system are that S. debilis eggs are autonomous and therefore have no external nutrient supply, the embryos can be ranked for developmental stage and the large egg size allows clutch numbers to be determined accurately. Recombinant apo-aequorin, which requires coelenterazine for luminescence, was used to quantify coelenterazine during the developmental sequence. An increase of almost two orders of magnitude was detected in coelenterazine content per egg between the first and final stage of development (mean values of 1 pmol and 71 pmol). This demonstrates de novo biosynthesis of coelenterazine for the first time.

Type
Research Article
Information
Journal of the Marine Biological Association of the United Kingdom , Volume 75 , Issue 1 , February 1995 , pp. 165 - 171
Copyright
Copyright © Marine Biological Association of the United Kingdom 1995

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References

Barnes, A.T., Case, J.F. & Tsuji, F.I., 1973. Induction of bioluminescence in a luciferin deficient form of the marine teleost, Porichthys, in response to exogenous luciferin. Comparative Bio-chemistry and Physiology, 46A, 709–723.CrossRefGoogle Scholar
Campbell, A.K., 1988. Chemiluminescence: principles and applications in biology and medicine. Chichester: Horwood/VCH.Google Scholar
Campbell, A.K. & Herring, P.J., 1990. Imidazolopyrazine bioluminescence in copepods and other marine organisms. Marine Biology, 104, 219–225.CrossRefGoogle Scholar
Chomczynski, P. & Sacchi, N., 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry, 162, 156–159.CrossRefGoogle ScholarPubMed
Frank, T.M., Widder, E.A., Latz, M.I. & Case, J.F., 1984. Dietary maintenance of bioluminescence in a deep-sea mysid. Journal of Experimental Biology, 109, 385–389.CrossRefGoogle Scholar
Haddock, S.H.D. & Case, J.F., 1994. A bioluminescent chaetognath. Nature, London, 367, 225–226.CrossRefGoogle Scholar
Haneda, Y., Johnson, F.H. & Shimomura, O., 1966. The origin of luciferin in the luminous ducts of Parapriacanthus ransonneti, Pempheris klunzingeri, and Apogon ellioti. In Bioluminescence in progress (ed. F.H., Johnson and Y., Haneda), pp. 533–545. Princeton University Press.Google Scholar
Haneda, Y., Johnson, F.H. & Sie, E.H.-C., 1958. Luciferin and luciferase extracts of a fish, Apogon marginatus, and their luminescent cross-reactions with those of a crustacean, Cypridina hilgendorfii. Biological Bulletin. Marine Biological Laboratory, Woods Hole, 115, 336.Google Scholar
Haneda, Y., Johnson, F.H. & Sie, E.H.-C., 1959. The luminescent cross-reaction between extracts of the luminous fish Apogon ellioti Day and extracts of the crustacean, Cypridina. Science Reports of the Yokosuka City Museum, 4, 13–17.Google Scholar
Harvey, E.N., 1952. Bioluminescence. New York: Academic Press.Google Scholar
Herring, P.J., 1974. Observations on the embryonic development of some deep-living decapod crustaceans, with particular reference to species of Acanthephyra. Marine Biology, 25, 25–33.CrossRefGoogle Scholar
Herring, P.J., 1978. Bioluminescence of invertebrates other than insects. In Bioluminescence in action (ed. P.J., Herring), pp. 199–240. London: Academic Press.Google Scholar
Herring, P.J., 1985. How to survive in the dark: bioluminescence in the deep sea. Symposia of the Society for Experimental Biology. Cambridge, no. 39, 323–350.Google ScholarPubMed
Herring, P.J., 1990a. Bioluminescent communication in the sea. In Light and life in the sea (ed. P.J., Herring et al.), pp. 245–264. Cambridge University Press.Google Scholar
Herring, P.J., 1990b. Bioluminescent responses of a deep-sea scyphozoan Atolla wyvillei. Marine Biology, 106, 413–417.CrossRefGoogle Scholar
Inoue, S., Kakoi, H., Murata, M., Goto, T. & Shimomura, O., 1977. Complete structure of Renilla luciferin and luciferyl sulfate. Tetrahedron Letters, 31, 2685–2688.CrossRefGoogle Scholar
McCapra, F., 1990. The chemistry of bioluminescence: origins and mechanism. In Light and life in the sea (ed. P.J., Herring et al.), pp. 265–278. Cambridge University Press.Google Scholar
Shimomura, O., 1987. Presence of coelenterazine in non-bioluminescent marine organisms. Comparative Biochemistry and Physiology, 86B, 361–363.Google Scholar
Shimomura, O., Inoue, S., Johnson, F.H. & Haneda, Y., 1980. Widespread occurrence of coelenterazine in marine bioluminescence. Comparative Biochemistry and Physiology, 65B, 435–437.Google Scholar
Studier, F.W., Rosenberg, A.H., Dunn, J.J. & Dubendorff, J.W., 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods in Enzymology, 185, 60–89.CrossRefGoogle ScholarPubMed
Stults, N.L. et al., 1992. Use of recombinant biotinylated aequorin in microtiter and membrane-based assays: purification of recombinant apoaequorin from Escherichia coli. Biochemistry, 31, 1433–1442.CrossRefGoogle ScholarPubMed
Thompson, E.M., Nafpaktitis, B.G. & Tsuji, F.I., 1987. Induction of bioluminescence in the marine fish, Porichthys, by Vargula (crustacean) luciferin. Evidence for de novo synthesis or recycling of luciferin. Photochemistry and Photobiology, 45, 529–533.CrossRefGoogle Scholar
Thompson, E.M., Nafpaktitis, B.G. & Tsuji, F.I., 1988. Dietary uptake and blood transport of Vargula (crustacean) luciferin in the bioluminescent fish, Porichthys notatus. Comparative Bio-chemistry and Physiology, 89A, 203–209.CrossRefGoogle Scholar
Watkins, N.J. & Campbell, A.K., 1993. Requirement of the C-terminal proline residue for stability of the Ca2+-activated photoprotein aequorin. Biochemical Journal, 293, 181–185.CrossRefGoogle Scholar
Watkins, N.J., Herring, P.J. & Campbell, A.K., 1993. An evolutionary pathway for aequorin and coelenterazine bioluminescence. In Bioluminescence and chemiluminescence status report. Proceedings of the seventh International Symposium on bioluminescence and chemiluminescence (ed. P.E, Stanley et al.), pp. 64–68. Chichester: Wiley.Google Scholar