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Physiological control of bioluminescence in a deep-sea planktonic worm, Tomopteris helgolandica
Gouveneaux, A.; Mallefet, J. (2013). Physiological control of bioluminescence in a deep-sea planktonic worm, Tomopteris helgolandica. J. Exp. Biol. 216(22): 4285-4289. dx.doi.org/10.1242/jeb.090852
In: Journal of Experimental Biology. Cambridge University Press: London. ISSN 0022-0949, more
Peer reviewed article  

Available in  Authors 
    VLIZ: Open Repository 279260 [ OMA ]

Keywords
    Tomopteridae Grube, 1850 [WoRMS]; Marine
Author keywords
    Tomopteridae; yellow light; annelid; cholinergic control; nervouscontrol; plankton

Authors  Top 
  • Gouveneaux, A., more
  • Mallefet, J., more

Abstract
    Tomopteris helgolandica Greeff 1879 (Tomopteridae) is a transparent holoplanktonic polychaete that can emit a bright light. In this study, we investigated the emission pattern and control of this deep-sea worm's luminescence. Potassium chloride depolarisation applied on anaesthetized specimens triggered a maximal yellow light emission from specific parapodial sites, suggesting that a nervous control pathway was involved. Pharmacological screening revealed a sensitivity to carbachol, which was confirmed by a dose–light response associated with a change in the light emission pattern, where physiological carbachol concentrations induced flashes and higher concentrations induced glows. The light response induced by its hydrolysable agonist, acetylcholine, was significantly weaker but was facilitated by eserine pretreatment. In addition, a specific inhibitory effect of tubocurarine was observed on carbachol-induced emission. Lastly, KCl- and carbachol-induced light responses were significantly reduced when preparations were pre-incubated in Ca2+-free artificial seawater or in different calcium channel blockers (verapamil, diltiazem) and calmodulin inhibitor (trifluoperazine) solutions. All of these results strongly suggest that T. helgolandica produces its light flashes via activation of nicotinic cholinergic receptors and a calcium-dependent intracellular mechanism involving L-type calcium channels.

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