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J Biol Chem, Vol. 273, Issue 37, 24139-24144, September 11, 1998
From the The
Differential Heparin Sensitivity of
-Dystroglycan Binding to
Laminins Expressed in Normal and dy/dy Mouse Skeletal
Muscle
,§
Graduate Program in Molecular and Cellular
Pharmacology, § Department of Physiology, University of
Wisconsin Medical School, Madison, Wisconsin 53706
-dystroglycan binding properties of
laminins extracted from fully differentiated skeletal muscle were
characterized. We observed that the laminins expressed predominantly in
normal adult rat or mouse skeletal muscle bound -dystroglycan in a
Ca2+-dependent, ionic strength-sensitive,
but heparin-insensitive manner as we had observed previously with
purified placental merosin (Pall, E. A., Bolton, K. M., and Ervasti,
J. M. 1996 J. Biol. Chem. 271, 3817-3821). Rat
skeletal muscle laminins partially purified by heparin-agarose affinity
chromatography also bound -dystroglycan without sensitivity to
heparin. We also confirm previous studies of dystrophic
dy/dy mouse skeletal muscle showing that the 2 chain of
merosin is reduced markedly and that the laminin 1 chain is not
up-regulated detectably. However, we further observed a quantitative
decrease in the expression of laminin 
/
chain immunoreactivity in
2 chain-deficient dy/dy skeletal muscle and reduced
-dystroglycan binding activity in laminin extracts from
dy/dy muscle. Most interestingly, the -dystroglycan binding activity of residual laminins expressed in merosin-deficient dy/dy skeletal muscle was inhibited dramatically (69 ± 19%) by heparin. These results identify a potentially important
biochemical difference between the laminins expressed in normal and
dy/dy skeletal muscle which may provide a molecular basis
for the inability of other laminin variants to compensate fully for the
deficiency of merosin in some forms of muscular dystrophy.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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