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J. Biol. Chem., Vol. 278, Issue 18, 15661-15668, May 2, 2003
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From the Laminin-5, a major adhesive ligand for epithelial
cells, undergoes processing of its
Mammalian Tolloid Metalloproteinase, and Not Matrix
Metalloprotease 2 or Membrane Type 1 Metalloprotease, Processes
Laminin-5 in Keratinocytes and Skin*
,§,,,,
,**
Program in Epithelial Biology, Stanford
University, Stanford, California 94305, § FibroGen,
Inc., South San Francisco, California 94080, ¶ Department of
Pathology and Laboratory Medicine, University of Wisconsin, Madison,
Wisconsin 53706, Imaging Center, Shriners Hospital for Crippled
Children, Portland, Oregon 97201, and ** Dermatology
Service, Veterans Affairs Medical Center, Palo Alto, California
94304
2 and 
3 chains. This study
investigated the mechanism of laminin-5 processing by keratinocytes.
BI-1 (BMP-1 isoenzyme inhibitor-1), a selective inhibitor of a small
group of astacin-like metalloproteinases, which includes bone
morphogenetic protein 1 (BMP-1), mammalian Tolloid (mTLD), mammalian
Tolloid-like 1 (mTLL-1), and mammalian Tolloid-like 2 (mTLL-2),
inhibited the processing of laminin-5 2 and 3 chains in
keratinocyte cultures in a dose-dependent manner. In a
proteinase survey, all BMP-1 isoenzymes processed human laminin-5 2
and 3 chains to 105- and 165-kDa fragments, respectively. In
contrast, MT1-MMP and MMP-2 did not cleave the 2 chain of human
laminin-5 but processed the rat laminin 2 chain to an 80-kDa
fragment. An immunoblot and quantitative PCR survey of the BMP-1
isoenzymes revealed expression of mTLD in primary keratinocyte cultures
but little or no expression of BMP-1, mTLL-1, or mTLL-2. mTLD was shown
to cleave the 2 chain at the same site as the previously identified
BMP-1 cleavage site. In addition, mTLD/BMP-1 null mice were shown to
have deficient laminin-5 processing. Together, these data
identify laminin-5 as a substrate for mTLD, suggesting a role for
laminin-5 processing by mTLD in the skin.
*
This work was funded through the Office of Research, Palo
Alto Veterans Affairs Medical Center, National Institutes of Health Grants P01-AR44012-01 and R01-AR47223-01 (to M. P. M.), and a grant
from the Skin Cancer Foundation.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: Program in
Epithelial Biology, 269 Campus Dr., Rm. 2145, Stanford, CA 94305. Tel.: 650-498-5425; Fax: 650-723-8762; E-mail: mpm@stanford.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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