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Originally published In Press as doi:10.1074/jbc.M103843200 on July 17, 2001

J. Biol. Chem., Vol. 276, Issue 37, 35078-35086, September 14, 2001
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Differential Vicia villosa Agglutinin Reactivity Identifies Three Distinct Dystroglycan Complexes in Skeletal Muscle*

Erin L. McDearmonDagger , Ariana C. Combs§, and James M. ErvastiDagger §

From the Dagger  Graduate Program in Molecular and Cellular Pharmacology and the § Department of Physiology, University of Wisconsin-Madison Medical School, Madison, Wisconsin 53706

We present evidence for the expression of three alpha -dystroglycan glycoforms in skeletal muscle cells, including two minor glycoforms marked by either patent or latent reactivity with the N-acetylgalactosamine-specific lectin Vicia villosa agglutinin. Both minor glycoforms co-isolated with beta -dystroglycan, but not with other dystrophin/utrophin-glycoprotein complex components, suggesting that they may perform distinct or modified cellular functions. We also confirmed that both patent and latent V. villosa agglutinin-reactive alpha -dystroglycan glycoforms are expressed in C2C12 myotubes. However, we found that the combined effect of saturating concentrations of V. villosa agglutinin and laminin-1 were strictly additive with respect to acetylcholine receptor cluster formation in C2C12 myotubes, which suggests that laminin-1 and V. villosa agglutinin do not compete for the same binding site on the cell surface. Finally, although beta -N-acetylhexosaminidase digestion dramatically inhibited agrin-, V. villosa agglutinin-, and laminin-1-induced acetylcholine receptor clustering in C2C12 myotubes, treatment with this enzyme had no effect on the amount of alpha -dystroglycan that was bound to V. villosa agglutinin-agarose. We conclude that alpha -dystroglycan is not the V. villosa agglutinin receptor implicated in acetylcholine receptor cluster formation. However, our data provide new support for the hypothesis that different glycoforms of alpha -dystroglycan may perform distinct functions even within the same cell.

* This work was supported by a grant from the Muscular Dystrophy Association, National Institutes of Health Grant ARO1985 to (J. M. E.), and an American Heart Association-Northland Affiliate Predoctoral Fellowship (to E. L. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Physiology, University of Wisconsin-Madison, 127 Service Memorial Inst., 1300 University Ave., Madison, WI 53706. Tel.: 608-265-3419; Fax: 608-265-5512; E-mail: ervasti@physiology.wisc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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