2. Academic Validation
  3. Induction of insulin-like growth factor 1 splice forms by subfragments of myofibrillar proteins

Induction of insulin-like growth factor 1 splice forms by subfragments of myofibrillar proteins

  • Mol Cell Endocrinol. 2015 Jan 5:399:69-77. doi: 10.1016/j.mce.2014.08.010.
Irina V Kravchenko 1,  Vladimir A Furalyov 1,  Spyros Chatziefthimiou 2,  Matthias Wilmanns 2,  Vladimir O Popov 3
Affiliations

Affiliations

  • 1 Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskiy Prospect 33, 119071 Moscow, Russia.
  • 2 European Molecular Biology Laboratory, Hamburg Unit, c/o DESY, Notkestraße 85, 22603 Hamburg, Germany.
  • 3 Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskiy Prospect 33, 119071 Moscow, Russia; Kurchatov NBIC Centre, Russian National Research Centre "Kurchatov Institute", Akademika Kurchatova sq. 1, 123182 Moscow, Russia. Electronic address: vpopov@inbi.ras.ru.
PMID: 25152160 DOI: 10.1016/j.mce.2014.08.010
Abstract

Expression of insulin-like growth factor 1 (IGF-1) mRNAs splice forms was recently shown to be stimulated by myofibrillar proteins released from the damaged muscle. In this study, we report that individual subfragments of titin and myomesin composed of Fn type III and Ig-like domains can activate expression of two IGF-1 splice forms in cultured myoblasts, both at protein and mRNA levels. Competition studies showed that each of the domain-types interacts with its own receptor. Induction of IGF-1 expression caused by domains of different types showed dissimilar sensitivity to inhibitors of regulatory cascades. The effect of Fn type III domains was more sensitive to inhibition of CA(2+)/Calmodulin dependent protein kinase, whereas the effect of Ig-like domains showed greater sensitivity to the inhibition of the adenylyl cyclase-cAMP-PKA pathway.

Keywords

Fn type III domain; Ig-like domain; Insulin-like growth factor 1; Mechano-growth factor; Myomesin; Titin.

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