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Updated: Oct 2, 2026

Modeling Myotonic Dystrophy 1 in C2C12 Myoblast Cells
Published on: July 29, 2016
The myotonin-protein kinase phosphorylates tyrosine residues in normal human skeletal muscle
P Etongué-Mayer1, R Faure, J P Bouchard
1Department of Medicine and Molecular Genetics, CHU Laval Research Center, Ste-Foy, Quebec, Canada.
Abstract:
As a first approach to study the cellular events involved in myotonic dystrophy, we have produced a polyclonal antibody against a peptide sequence of the predicted gene product. This antibody specifically recognizes a 54 kDa protein in human skeletal muscle. This protein phosphorylates a co-polymer Glu/Tyr but not Myelin Basic Protein. This indicates that the myotonin-protein kinase has a tyrosine kinase activity in human skeletal muscle. This is the first demonstration of the kinase activity of the myotonin-protein kinase.
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