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

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 (1 micromoll(-1)) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10 mmoll(-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 30 kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30 kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin I.

• Authors: B Brüstle, S Kreissl, D L Mykles, W Rathmayer
• Journal: The Journal of experimental biology (J Exp Biol) Vol. 204 Issue Pt 15 Pg. 2627-35 (Aug 2001) ISSN: 0022-0949 [Print] England
• PMID: 11533112 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Immune Sera
• Muscle Proteins
• Neuropeptides
• Oligopeptides
• Phosphoproteins
• Troponin I
• Caffeine
• proctolin

Topics

• Animals
• Blotting, Western
• Caffeine (pharmacology)
• Crustacea (metabolism)
• Drug Synergism
• Immune Sera
• Immunohistochemistry
• Male
• Molecular Weight
• Muscle Contraction (drug effects)
• Muscle Proteins (metabolism)
• Muscles (chemistry, innervation)
• Neuropeptides
• Oligopeptides (pharmacology)
• Phosphoproteins (metabolism)
• Phosphorylation
• Troponin I (analysis, immunology)