The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle-Reference-Cited by-同舟云学术

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

Published:2001-08-01 Issue:15 Volume:204 Page:2627-2635
ISSN:1477-9145
Container-title:Journal of Experimental Biology
language:en
Short-container-title:

Author:

Brüstle Berit¹,Kreissl Sabine¹,Mykles Donald L.²,Rathmayer Werner¹

Affiliation:

1. Department of Biology, University of Konstanz, D-78457 Konstanz, Germany, and

2. Department of Biology, Colorado State University, Fort Collins, CO 80523, USA

Abstract

SUMMARYIn 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.

Publisher

The Company of Biologists

Subject

Insect Science,Molecular Biology,Animal Science and Zoology,Aquatic Science,Physiology,Ecology, Evolution, Behavior and Systematics

Link

http://journals.biologists.com/jeb/article-pdf/204/15/2627/1237804/2627.pdf

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