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Происхождение биолюминесценции (англ)
.: Дата публикации 09-Фев-2007 :: Просмотров: 1348 :: Печатать текущую страницу :: Печатать все страницы:.


Institute of Ecology and Evolution, Russian Academy of Sciences, Leninsky Prospect 33, 117071 Moscow, Russia
E-mail: yulii_labas@mail.ru

Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117871 Moscow, Russia
E-mail: matz@mail.ibch.ru

Center for Craniofacial Molecular Biology, University of Southern California, 2250 Alcazar Street, CSA 103, Los Angeles, CA 90033, USA
E-mail: zakhartc@hsc.usc.edu


Bioluminescent systems (BS) are present in aerobic organisms on different levels of phylogenesis from bacteria to fishes. There are no bioluminescent species among autotrophs (except dinoflagellates), some groups of sea invertebrates and terrestrial animals, and for unknown reason - in fresh water organisms (exception - gastropodа Latia neritoides and some species of parasitic photobacteria).1

Charles Darwin has mentioned that the origin of the bioluminescence is the problematic questions in his theory.2 The function of the bioluminescence has a direct connection with the vision behavior of the organisms. It could be chasing the predators with flashes, camouflage, communication, and attraction with steady glowing (fungi non-symbiotic photobacteria).3-5 It means that the initial material for evolution were only such neutral mutations of non-luminescent organisms which resulted in well visible glowing, connected with certain behavior reactions in impulse mode (e.g. escape). It suggests preexistence in non-bioluminescent precursor species of all major components of the BS: luciferin (L), luciferase (E) or their analogs, and triggering mechanisms and secondary emitters (GFPs from coelenterates, blue fluorescent proteins from photobacteria, red fluorescent protein from deep-sea fish Malacosteus niger). Different phyla have different L and E. Taking in account dissimilariti between L,E and other components of BS-s in different phyla, it is reasonable to suppose that about 30 types of its were originated indepedently from preexisting nonbioluminescent reactions.6 There are some reports on conditionally bioluminescent species. In some non-bioluminescent species of Copepoda, e.g. Nannocalanus minor and Oithona plumifera occasionally could be found specimens which use to glow under stimulation.7 There are both luminous and non-luminous species in one genera: e.g. Obelia - among Hydrozoa,8 Oncaea, Oithona, among Cyclopodia.7 The close taxonomic relations of luminous species with non-luminous is evidence in favor of the recent genesis of some BS via light-emitting neutral mutations in non bioluminescent organisms.


There are many evidence that an ancestral function of L and some E was detoxification of reactive oxygen species (ROS), based on the antioxidant abilities of L.5,9-11 Coelenterazine occurs in many luminous marine species as well as in non-luminescent species.12 Some L are able to emit light with ROS in the absence of E.13-15 The luminescence of E-L photoprotein complexes also could be activated by ROS but not by molecular oxygen in Pholas dactylus,16 and in Polynoinae which have a specific reaction for superoxide.17 The calcium-activated photoprotein obelin is able to emit light in absence of calcium but in the presence of singlet oxygen.18 An activation of Е synthesis аs well as antioxidant enzymes such as SOD and catalase during hyperoxygenation may be an indication of the antioxidant origination of E in fireflies.10 Bacterial E is able to give a luminescent reaction in vitro in the presence of H2O2 or other ROS and in the absence of aliphatic aldehyde.11

In some eukaryotes an impulse luminescent flash initiates an endogenous release of ROS - e.g. in earthworms Diplocardia longa and ascidians Clavelina miniata BS is localized in phagocytes - “cells of the respiratory burst”.19,20. The content of those phagocytes in D.longa use to glow in the fluided exuded in the presence of endogenous H2O2. In non-bioluminescent earthworm Lampito mauritii phagocytes also use to glow in the presence of H2O2.21 In Polynoinae intracellular luminescence is the result of enzymatic generation of superoxide.17 . There are another mechanisms of bioluminescence triggering in Dinoflagellata through H+ or calcium in Anthozoa with an induced release of L from the complex with luciferin-binding protein (LBP).22,23 Based on this data we suggest here that an ancestral function of the L and some E could be the protection of the cells from the ROS which used to be secreted by those prophotogenic cells. In some bioluminescent eukaryotes it happens in impulse mode. The original function of LBP could be the protection of antioxidants - proluciferins from the self-oxidation prior the respiratory burst. The generation of ROS in low concentration is one of the necessary conditions for the normal physiology (functions of the secondary messengers, defense or offense, etc). An absence of BS in freshwater organisms could be explained by fact that many BS were the scavengers of HOCl- ion that could be the terminal product in ROS secretion only at the high concentration of Cl- ion in the environment. Anthozoa and Hydrozoa have different types of E and relatively close GFPs and L. It means that their BS have originated independently whereas GFPs and L were inherited from a common non-bioluminescent ancestor. Prediction of that fact resulted in a discovery of a new family of GFP-like proteins in non-bioluminescent Anthozoa.25 We also suggest that photocytes in Anthozoa originated from an entodermal pigment cells which able to secrete ROS for phagocytosis. Supposed function of GFP-like proteins could be photoactivation of enzyme reactions and tissue photoreception.

[Supported by Russian Foundation for Fundamental research (grant 99-04-48873)].


1. Harvey EN. Bioluminescence. New York: Academic Press, 1952: 542.

2. Darwin CR. The origin of species by means of natural selection. London: John Murray, 1859: 502.

3. Hastings JW. Bioluminescence. In: Speralakis N, ed. Cell Physiology. New York: Academic Press, 1995: 651-681.

4. Sivinski JM. Phototropism, bioluminescence, and the Diptera. Florida Entomologist 1998; 81: 282-292.

5. Wilson T, Hastings JW. Bioluminescence. Annu Rev Cell Dev Biol 1998; 14: 197-230.

6. Buck JB. Function and evolution of bioluminescence. In: Herring PJ, ed. Bioluminescence in Action. London: Academic Press, 1978: 419-460.

7. Evstigneev PV, Bitjukov EP. Bioluminescencija morskich copepod. Kiev: Naukova dumka, 1990: 145.

8. Morin JG. Coelenterate bioluminescence. In: Muscatine L, Lenhoff H, eds. Coelenterates Biology. Review of New Perspectives. New York: Academic Press, 1974: 397-438.

9. Rees JF, de Wergifoss B, Noiset O, Dubuisson M, Janssens B, Thompson EM. The origins of marine bioluminescence: turning oxygen defense mechanisms into deep-sea communication tools. J Exp Biol 1998; 201: 1211-1221.

10. Barros MP, Bechara EJ. Bioluminescence as a possible auxiliary oxygen detoxifying mechanism in elaterid larvae. Free Radic Biol Med 1998; 24: 767-777.

11. Watanabe H, Nagoshi T, Inaba, H. Luminescence of bacterial luciferase intermediate by reaction with H2O2: The evolutionary origin of luciferase and source of endogenous light-emission. Biochem Biophys Acta 1993; 1141: 297-302.

12. Thompson CM, Herring PJ, Campbell AK. The widespread occurrence and tissue distribution of the imidazolopyrazine luciferins. J Biolumin Chemilumin 1997; 12: 87-91.

13. Skatchkov MP, Sperling D, Hink U, Anggard E, Munzel T. Quantification of superoxide radical formation in intact vascular tissue using a Cypridina luciferin analog as an alternative to lucigenin. Biochem Biophys Res Commun 1998; 248: 382-386.

14. Akutsu K, Nakajima H, Katoh T, Kino S, Fujimori K. Chemiluminescence of Cipridina luciferin analogs. 2. Kinetic studies on the reaction of 2-methyl-6-phenylimidazo(1,2-a)pyrazin-3(7H)-one(CLA) with superoxide-hydroperoxyl radical is an actual active species used in initiate the reaction. J Chem Soc - Perkin Trans 1995; 2: 1699-1706.

15. Shimomura O. Superoxide triggered chemiluminescence of the extract of luminous mushroom Pannelus stripticus after treatment with methylamine. J Exp Bot 1991; 41: 555-560.

16. Roberts PA, Knight J, Campbell AK. Pholasin--a bioluminescent indicator for detecting activation of single neutrophils. Anal Biochem 1987; 160: 139-148.

17. Bassot JM, Nicolas MT. Bioluminescence in scale-worm photosomes: the photoprotein polynoidin is specific for the detection of superoxide radicals. Histochem Cell Biol 1995; 104: 199-210.

18. Vysotsky ES, Trofimov KP, Bondar VS, Gitelson JJ. Luminescence of Ca2+-activated photoprotein obelin iniciated by NaOCl and MnCl2. J Biolumin Chemilumin 1993; 6: 301-305.

19. Belissario R, Spencer TE, Cormier MJ. Isolation and properties of luciferase, a non-heme peroxidase from the bioluminescent earthworm, Diplocardia longa. Biochemistry 1972; 11: 2256-2266.

20. Chiba K.,Hoshi M.,Isobe M.,Hirose E.Bioluminescence in the tunic of the colonial ascidian, Clavelina miniata: identification of luminous cells in vitro. J.of Exper.Zool.1998. 281:546-553

21. Sanhanam KSV, Limaye NM. Electrobioluminescence of cells extracted from Lampito mauritii. Biochem Bioenerg 1989; 22: 219-229.

22. Lee DH, Mittag M, Sczekan S, Morse D, Hastings JW. Molecular cloning and genomic organization of a gene for luciferin-binding protein from the dinoflagellate Gonyaulax polyedra. J Biol Chem 1993; 268: 8842-8850.

23. Anderson JM, Carbonneau H, Cormier MJ. Mechanism of calcium induction of Renilla bioluminescence. Involvement of calcium-trigged luciferin binding protein. Biochemistry 1974; 13: 1195-1200.

24. Kumar S, Harrylock M, Walsh KA, Cormier MJ, Charbonneau H. Amino acid sequence of the Ca2(+)-triggered luciferin binding protein of Renilla reniformis. FEBS Letters 1990; 268: 287-290.

25. Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AZ, Markelov ML, Lukyanov SA. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat Biotech 1999; 17: 969-973.

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