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Cranin was described in 1987 as a membrane glycoprotein
expressed in brain and many other tissues, which binds laminin with
high affinity in a calcium-dependent manner. Dystrophin-associated
glycoprotein (``dystroglycan'') is a laminin-binding protein
cloned in 1992 whose relation to cranin has remained uncertain. Here we
describe the purification of cranin to homogeneity from sheep brain,
show cranin to be a form of dystroglycan, and localize the N terminus
of
Volume 270,
Number 25,
Issue of June 23, pp. 15425-15433, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
IDENTITY WITH DYSTROGLYCAN AND REASSESSMENT OF ITS CARBOHYDRATE
MOIETIES
-dystroglycan to amino acid residue 654. We find that brain
-dystroglycan is tightly associated with membranes, and localizes
to regions of synaptic contact as assessed by immunocytochemistry of
rat cerebellum. Brain -dystroglycan expresses high mannose/hybrid N-linked saccharides, terminal GalNAc residues, and the HNK-1
epitope. Although dystroglycan has previously been presumed to be a
proteoglycan, the amino acid sequence, pI, O-sialoglycoprotease susceptibility, lectin-binding profile,
and laminin-binding properties of brain dystroglycan are more typical
of mucin-like proteins. Furthermore, using CHO mutant cell lines
deficient in xylosyltransferase and galactosyltransferase I, which are
required for glycosaminoglycan biosynthesis, it is shown that
chondroitin sulfate and heparan sulfate are not critical for laminin
binding, and indeed are apparently not expressed at all in dystroglycan
from CHO cells.
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