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© 1993 Oxford University Press

RESEARCH-ARTICLE

Myotonic dystrophy kinase is a component of neuromuscular junctions

Peter F.M.van der Ven, Gert Jansen, Toln H.M.S.M.van Kuppevelt1, M.Benjamin Perryman2, Mark Lupa3, Patrick W. Dunne4, Henk J.ter Laak5, Paul H.K. Jap, Jacques H. Veerkamp1, Henry F. Epstein4 and Bé Wieringa*

Department of Cell Biology and Histology, Medical Faculty University Nijmegen, Tngon Building PO Box 9101, 6500 HB Nijmegen 1Department of Biochemistry, Medical Faculty University Nijmegen, Trigon Building Nijmegen, The Netherlands 2Division of Cardiology, University of Colorado Health Science Center Denver, CO 80262 3Departments of Cellular and Structural Biology and Physiology and the Neuroscience Program, University of Colorado Health Science Centre Denver, CO 80262 4Department of Neurology, Baylor College of Medicine Houston, TX 77030, USA 5Department of Neurology, Medical Faculty University Nijmegen, Radbound Hospital Nijmegen, The Netherlands

*To whom correspondence should be addressed

Received June 21, 1993; Revised August 25, 1993; Accepted August 25, 1993

The clinical manifestation of myotonic dystrophy (DM) is correlated to the extent of expansion of an unstable [CTG]n DNA motif. Recent studies have demonstrated that this trinucleotide motif forms part of the last, 3' untranslated exon of a gene which potentially encodes multiple protein Isoforms of a serine/threonine protein klnase (myotonic dystrophy protein kinase, DM-PK). We report here on the development of antisera against synthetic DM-PK peptide antigens and their use In blochemical and histochemlcal studies. Immunoreactlve DM-kinase protein of 53 kD is present at low levels In skeletal and cardiac muscle extracts of DM patients and normal controls. Immunohlstochemical staining revealed that DM-PK Is localised prominently at sites of neuromuscular and myotendinous junctions (NMJs and MTJs) of human and rodent skeletal muscles. Furthermore, very low levels of Immunoreactive DM-PK protein are present in the sarcoplasm of predominantly type I fibres in various muscles. Strikingly, presence of the protein can also be demonstrated for NMJs of muscular tissues of adult and congenital cases of DM, with no gross changes In structural organisation. Our findings provide a basis for further characterisation of the role of the kinase in protein assembly processes or signal mediation at synaptic sites and ultimately for the understanding of the complex pathophysiology of DM.


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