The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle
The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle
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2001
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Journal of experimental biology ; 204 (2001), 15. - pp. 2627-2635
Abstract
In the isopod Idotea emarginata, the neuropeptide proctolin is contained in a single pair of motoneurones located in pereion ganglion 4. The two neurones supply dorsal extensor muscle fibres of all segments. Proctolin (1μmoll−1) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10mmoll−1 caffeine. In western blots of myofibrillar proteins isolated from single muscle fibres and treated with an anti-phosphoserine antibody, a protein with an apparent molecular mass of 30kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin I.
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570 Biosciences, Biology
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Idotea emarginata,nervous system,motoneurone,modulation,actin,myosin,contraction,caffeine
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BRÜSTLE, Berit, Sabine KREISSL, Donald L. MYKLES, Werner RATHMAYER, 2001. The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle. In: Journal of experimental biology. 204(15), pp. 2627-2635BibTex
@article{Brustle2001neuro-16257, year={2001}, title={The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle}, number={15}, volume={204}, journal={Journal of experimental biology}, pages={2627--2635}, author={Brüstle, Berit and Kreißl, Sabine and Mykles, Donald L. and Rathmayer, Werner} }
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