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• W1996274786 abstract "The α-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 α-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 α-dystroglycan without sensitivity to heparin. We also confirm previous studies of dystrophicdy/dy mouse skeletal muscle showing that the α2 chain of merosin is reduced markedly and that the laminin α1 chain is not up-regulated detectably. However, we further observed a quantitative decrease in the expression of laminin β/γ chain immunoreactivity in α2 chain-deficient dy/dy skeletal muscle and reduced α-dystroglycan binding activity in laminin extracts fromdy/dy muscle. Most interestingly, the α-dystroglycan binding activity of residual laminins expressed in merosin-deficientdy/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." @default.
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• W1996274786 date "1998-09-01" @default.
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• W1996274786 title "Differential Heparin Sensitivity of α-Dystroglycan Binding to Laminins Expressed in Normal and dy/dy Mouse Skeletal Muscle" @default.
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• W1996274786 doi "https://doi.org/10.1074/jbc.273.37.24139" @default.
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