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Protein composition of thick filaments from molluscan catch muscle and the role of twitchin in the catch-state formation.

Authors
  • Vyatchin, Ilya G1
  • Shevchenko, Ulyana V2
  • Shelud'ko, Nikolay S2
  • 1 Laboratory of Cell Biophysics, A.V. Zhirmunsky Institute of Marine Biology, National Scientific Center of Marine Biology, Far Eastern Branch of the Russian Academy of Sciences, 17 Palchevsky Str., Vladivostok, 690041, Russia. Electronic address: [email protected]
  • 2 Laboratory of Cell Biophysics, A.V. Zhirmunsky Institute of Marine Biology, National Scientific Center of Marine Biology, Far Eastern Branch of the Russian Academy of Sciences, 17 Palchevsky Str., Vladivostok, 690041, Russia.
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier
Publication Date
Dec 10, 2019
Volume
520
Issue
3
Pages
634–639
Identifiers
DOI: 10.1016/j.bbrc.2019.10.029
PMID: 31627898
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

In the work, we performed densitometry of thick filaments of the Gray's mussel catch muscle; densitometry included determination of electrophoretic dye binding constants of proteins. The results of densitometry showed that the content of twitchin in thick filaments is significantly (10 times) lower than the content of myosin. We performed an in vitro simulation of the contractile apparatus of the catch muscle and showed that with such content, links formed by twitchin cannot stop "relaxation". So, we doubt that the role of twitchin in the formation of the catch state is to form load-bearing links between thin and thick filaments that keep the muscle in the contracted state. At the same time, densitometry has shown that the content of the unique catch-muscle protein - myorod - significantly exceeds the content of twitchin and reaches the level of myosin. Like twitchin, myorod is capable of forming regulated cross-links between thick and thin filaments. Such a high content of this protein may indicate that it is myorod, and not twitchin, that is responsible for the formation of catch load-bearing cross-links. Copyright © 2019 Elsevier Inc. All rights reserved.

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