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J. Biol. Chem., Vol. 275, Issue 47, 36720-36725, November 24, 2000
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From the Department of Oncology, Lombardi Cancer Center, Georgetown
University, Medical Center, Washington, DC 20007
Matriptase is an epithelial-derived, integral
membrane serine protease. The enzyme was initially isolated from human
breast cancer cells and has been implicated in breast cancer invasion and metastasis. In the current study, using active matriptase isolated
from human milk, we demonstrate that matriptase is able to cleave
various synthetic substrates with arginine or lysine as their P1 sites
and prefers small side chain amino acids, such as Ala and Gly, at P2
sites. For the most reactive substrates, N-tert-butoxycarbonyl
(N-t-Boc)-
Activation of Hepatocyte Growth Factor and Urokinase/Plasminogen
Activator by Matriptase, an Epithelial Membrane Serine
Protease*
,
-benzyl-Glu-Ala-Arg-7-amino-4-methylcoumarin (AMC) and N-t-Boc-Gln-Ala-Arg-AMC, the
Km values were determined to be 3.81 and 4.89 µM, respectively. We further demonstrated that matriptase
can convert hepatocyte growth factor/scattering factor to its active
form, which can induce scatter of Madin-Darby canine kidney epithelial
cells and can activate c-Met tyrosine phosphorylation in A549
human lung carcinoma cells. In addition, we noted that matriptase can
activate urokinase plasminogen activator but has no affect on
plasminogen. These results suggest that matriptase could act as an
epithelial, upstream membrane activator to recruit and activate
stromal-derived downstream effectors important for extracellular matrix
degradation and epithelial migration, two major events of tissue
remodeling, cancer invasion, and metastasis.
*
Supported in part by National Institutes of Health,
Specialized Program of Research Excellence Grant 1P50CA58158 in breast cancer and National Institutes of Health Grant R21-CA80897.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.
Supported by Department of Defense Fellowship DAMD
17-00-1-0269.
§
To whom correspondence should be addressed: Dept. of
Oncology/Lombardi Cancer Center, Georgetown University Medical Ctr., 3970 Reservoir Rd. NW, Washington, DC 20007. Tel.: 202-687-4304; Fax:
202-687-7505; E-mail address: lincy@gunet.georgetown.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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