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J. Biol. Chem., Vol. 277, Issue 21, 18928-18937, May 24, 2002
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From the The
Contributions of the LG Modules and Furin Processing to Laminin-2
Functions*
,,
Department of Pathology & Laboratory
Medicine, Robert Wood Johnson Medical School, Piscataway, New
Jersey 08854, the § Department Physiology, University of
Wisconsin, Madison, Wisconsin 53706, and the ¶ Department of
Medical Biochemistry & Biophysics, Karolinska Institute,
S-17177 Stockholm, Sweden
2-laminin subunit contributes to basement
membrane functions in muscle, nerve, and other tissues, and mutations
in its gene are causes of congenital muscular dystrophy. The 2
G-domain modules, mutated in several of these disorders, are thought to mediate different cellular interactions. To analyze these
contributions, we expressed recombinant laminin-2
(2
1
1) with LG4-5,
LG1-3, and LG1-5 modular deletions. Wild-type and LG4-5
deleted-laminins were isolated from medium intact and cleaved within
LG3 by a furin-like convertase. Myoblasts adhered predominantly through
LG1-3 while -dystroglycan bound to both LG1-3 and LG4-5.
Recombinant laminin stimulated acetylcholine receptor (AChR)
clustering; however, clustering was induced only by the proteolytic
processed form, even in the absence of LG4-5. Furthermore, clustering
required 61 integrin and -dystroglycan
binding activities available on LG1-3, acting in concert with laminin
polymerization. The ability of the modified laminins to mediate
basement membrane assembly was also evaluated in embryoid bodies where
it was found that both LG1-3 and LG4-5, but not processing, were
required. In conclusion, there is a division of labor among LG-modules
in which (i) LG4-5 is required for basement membrane assembly but not
for AChR clustering, and (ii) laminin-induced AChR clustering requires
furin cleavage of LG3 as well as -dystroglycan and
61 integrin binding.
*
This work was supported by National Institutes of Health
Grants DK36425 and NS38469 (to P. D. Y.) and ARO1985 (to
J. E.), the Muscular Dystrophy Association (to J. E.),
BioStratum, Inc. (to P. D. Y.), and an American Heart
Association-Northland Affiliate Pre-doctoral 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 Pathology & Laboratory Medicine, UMDNJ-Robert Wood Johnson Medical
School, Piscataway, NJ 08854. Tel./Fax: 732-235-5166 (4825); E-mail:
yurchenc@umdnj.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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