alpha-Dystroglycan, which is a cell surface component of dystroglycan compl
ex, is known to bind laminin in basal lamina of muscle cells and Schwann ce
lls. We found previously that a novel O-glycan, Sia alpha 2-3Gal beta 1-4Gl
cNAc beta 1-2Man, is the major oligosaccharide in bovine peripheral nerve a
lpha-dystroglycan, and that this structure might mediate the binding of lam
inin. In order to determine whether this structure is specific for peripher
al nerve alpha-dystroglycan or present on different forms of alpha-dystrogl
ycan, we analyzed the structures of the sialylated O-glycans of rabbit skel
etal muscle alpha-dystroglycan. Their structures were elucidated to be a mi
xture of a core 1 O-glycan and the same O-mannosyl glycan that we found in
bovine peripheral nerve. These results indicate that alpha-dystroglycan in
different species and tissues share a common structure of its major O-linke
d acidic carbohydrate, suggesting its relevance to the basic functional rol
e of alpha-dystroglycan. (C) 1998 Published by Elsevier Science B.V. All ri
ghts reserved.