Human Molecular Genetics, Vol 7, 1957-1965, Copyright © 1998 by Oxford University Press
YC Pham, N Man, LT Lam and GE Morris
There is considerable confusion in the literature about the size of the
myotonic dystrophy protein kinase (DMPK) and its localization within
tissues. We have used a new panel of monoclonal antibodies (mAbs) to begin
to resolve these issues, which are important for understanding the possible
role of DMPK in myotonic dystrophy. Antisera raised against the catalytic
and coil domains of DMPK recognized a major 55 kDa protein and a minor
72-80 kDa doublet on western blots of human skeletal muscle. Ten mAbs, five
against the catalytic domain and five against the coil region, recognized
only the 72-80 kDa doublet. The 72 kDa protein was present in all tissues
tested, whereas the 80 kDa component was variably expressed, mainly in
skeletal and cardiac muscles. The 72 kDa protein was absent in a DMPK
knockout mouse and was greatly increased in a transgenic mouse
overexpressing human DMPK, confirming its identity as authentic DMPK. Two
mAbs against the catalytic domain recognized only the more abundant 55 kDa
protein, which was found only in skeletal muscle. Nine out of 10 mAbs
located DMPK to intercalated discs in human heart, an affected tissue in
myotonic dystrophy. However, co-localization of DMPK with acetylcholine
receptors at neuromuscular junctions was not observed with any of the mAbs.
Subcellular fractionation and sedimentation analysis suggest that a major
proportion of the DMPK in skeletal muscle and brain is cytosolic.
ARTICLES
Localization of myotonic dystrophy protein kinase in human and rabbit tissues using a new panel of monoclonal antibodies
MRIC Biochemistry Group, NE Wales Institute, Mold Road, Wrexham LL11 2AW, UK.
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