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First published online January 19, 2006
Journal of Experimental Biology 209, 531-540 (2006)
Published by The Company of Biologists 2006
doi: 10.1242/jeb.02011
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The neuropeptide proctolin potentiates contractions and reduces cGMP concentration via a PKC-dependent pathway

Berit Philipp, Nicole Rogalla and Sabine Kreissl*

Department of Biology, University of Konstanz, 78457 Konstanz, Germany

* Author for correspondence (e-mail: s.kreissl{at}uni-konstanz.de)

Accepted 22 November 2005

As in many other arthropods, the neuropeptide proctolin enhances contractures of muscles in the crustacean isopod Idotea emarginata. The enhancement of high K+-induced contractures by proctolin (1 µmol l-1) was mimicked upon application of the protein kinase C (PKC) activator phorbol-12-myristate 1-acetate (PMA) and was inhibited by the PKC inhibitor bisindolylmaleimide (BIM-1). The potentiation was not inhibited by H89, a protein kinase A (PKA) inhibitor. Proctolin did not change the intracellular concentration of 3',5'-cyclic adenosine monophosphate (cAMP) whereas it significantly reduced the intracellular concentration of 3',5'-cyclic guanosine monophosphate (cGMP). The reduction of cGMP was not observed in the presence of the PKC inhibitor BIM-1. 8-Bromo-cGMP, a membrane-permeable cGMP analogue, reduced the potentiating effect of proctolin on muscle contracture. We thus conclude that proctolin in the studied crustacean muscle fibres induces an activation of PKC, which leads to a reduction of the cGMP concentration and, consequently, to the potentiation of muscle contracture.

Key words: Idotea emarginata, neuropeptide, modulation, cAMP, cGMP, PKC, PKA


Related articles in JEB:

PROCTOLIN MEDIATES EFFECT THROUGH cGMP
Kathryn Phillips
JEB 2006 209: ii. [Full Text]  



This article has been cited by other articles:


Home page
 J. Exp. Biol.Home page
K. Phillips
PROCTOLIN MEDIATES EFFECT THROUGH cGMP
J. Exp. Biol., February 1, 2006; 209(3): ii - ii.
[Full Text] [PDF]


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