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(Received for publication, September 13, 1996, and in revised form, March 3, 1997)
From the ¶ Department of Neurology and Neuroscience, Teikyo
University School of Medicine, Tokyo 173, Japan, Dystroglycan is encoded by a single gene and
cleaved into two proteins
Volume 272, Number 21,
Issue of May 23, 1997
pp. 13904-13910
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
Department of
Glycobiology, Tokyo Metropolitan Institute of Gerontology, Tokyo 173, Japan, the ** University School of Neuroscience and Muscular Dystrophy
Group Laboratories, Regional Neuroscience Centre, Newcastle General
Hospital, Newcastle-upon-Tyne NE4 6BE, United Kingdom, the
Department of Neurology, Institute of Brain Research,
University of Tokyo Faculty of Medicine, Tokyo 113, Japan, and the
¶¶ Howard Hughes Medical Institute and Department of
Physiology and Biophysics, University of Iowa College of Medicine,
Iowa City, Iowa 52242
- and 
-dystroglycan by
posttranslational processing. Recently, -dystroglycan was
demonstrated to be an extracellular laminin-binding protein anchored to
the cell membrane by a transmembrane protein -dystroglycan in
striated muscle and Schwann cells. However, the biological functions of
the dystroglycan-laminin interaction remain obscure, and in particular,
it is still unclear if dystroglycan plays a role in cell adhesion. In
the present study, we characterized the role of dystroglycan in the
adhesion of schwannoma cells to laminin-1. Immunochemical analysis
demonstrated that the dystroglycan complex, comprised of - and
-dystroglycan, was a major laminin-binding protein complex in the
surface membrane of rat schwannoma cell line RT4. It also demonstrated
the presence of -dystroglycan, but not -dystroglycan, in the
culture medium, suggesting secretion of -dystroglycan by RT4 cells.
RT4 cells cultured on dishes coated with laminin-1 became spindle in
shape and adhered to the bottom surface tightly. Monoclonal antibody
IIH6 against -dystroglycan was shown previously to inhibit the
binding of laminin-1 to -dystroglycan. In the presence of IIH6, but
not several other control antibodies in the culture medium, RT4
cells remained round in shape and did not adhere to the bottom surface.
The adhesion of RT4 cells to dishes coated with fibronectin was not
affected by IIH6. The known inhibitors of the interaction of
-dystroglycan with laminin-1, including EDTA, sulfatide, fucoidan,
dextran sulfate, heparin, and sialic acid, also perturbed the adhesion
of RT4 cells to laminin-1, whereas the reagents which do not inhibit
the interaction, including dextran, chondroitin sulfate, dermatan
sulfate, and GlcNAc, did not. Altogether, these results support a role
for dystroglycan as a major cell adhesion molecule in the surface
membrane of RT4 cells.
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