The myotonin-protein kinase phosphorylates tyrosine residues in normal human skeletal muscle

Biochem Biophys Res Commun. 1994 Feb 28;199(1):89-92. doi: 10.1006/bbrc.1994.1198.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • Humans
  • Immunologic Techniques
  • Molecular Sequence Data
  • Muscle Proteins / metabolism
  • Myotonic Dystrophy / enzymology
  • Myotonin-Protein Kinase
  • Peptides / chemistry
  • Phosphotyrosine
  • Protein Kinases / metabolism*
  • Protein Serine-Threonine Kinases*
  • Protein-Tyrosine Kinases / metabolism*
  • Recombinant Fusion Proteins
  • Tyrosine / analogs & derivatives*
  • Tyrosine / metabolism

Substances

  • DMPK protein, human
  • Muscle Proteins
  • Peptides
  • Recombinant Fusion Proteins
  • Phosphotyrosine
  • Tyrosine
  • Protein Kinases
  • Protein-Tyrosine Kinases
  • Myotonin-Protein Kinase
  • Protein Serine-Threonine Kinases