The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle

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bruestlekreissletal.pdf
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2001
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Brüstle, Berit
Mykles, Donald L.
Rathmayer, Werner
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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 Biowissenschaften, Biologie
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Idotea emarginata, nervous system, motoneurone, modulation, actin, myosin, contraction, caffeine
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ISO 690BRÜSTLE, 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. 2001, 204(15), pp. 2627-2635
BibTex
@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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    <dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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