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J. Biol. Chem., Vol. 277, Issue 12, 10539-10546, March 22, 2002
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From the We describe here a novel biological function of
sphingosine 1-phosphate (S1P): the activation of a serine protease,
matriptase. Matriptase is a type II integral membrane serine protease,
expressed on the surface of a variety of epithelial cells; it may play
an important role in tissue remodeling. We have previously reported that the activation of matriptase is regulated by serum. We have now
identified the bioactive component from serum. First, the activity was
observed to co-purify with lipoproteins by conventional liquid
chromatography and immunoaffinity chromatography. The ability of
lipoproteins to induce the activation of matriptase was further confirmed with commercial preparations of low density lipoprotein (LDL)
and very low density lipoprotein (VLDL). Next, we observed that the
bioactive component of LDL is associated with the phospholipid components of LDL. Fractionation of lipid components of LDL by thin
layer chromatography (TLC) revealed that the bioactive component of LDL
comigrates with S1P. Nanomolar concentrations of commercially obtained
S1P were then observed to induce the rapid activation of matriptase on
the surfaces of nontransformed human mammary epithelial cells. Other
structurally related sphingolipids, including dihydro-S1P, ceramide
1-phosphates, and sphingosine phosphocholine as well as
lysophosphatidic acid, can also induce the activation of matriptase,
but at significantly higher concentrations than S1P. Furthermore,
S1P-dependent matriptase activation is dependent on
Ca2+ but not via Gi protein-coupled
receptors. Our results demonstrate that bioactive phospholipids can
function as nonprotein activators of a cell surface protease,
suggesting a possible mechanistic link between S1P and normal and
possibly pathologic tissue remodeling.
Sphingosine 1-Phosphate, Present in
Serum-derived Lipoproteins, Activates Matriptase*
,,, and¶
Lombardi Cancer Center and
§ Department of Biochemistry and Molecular Biology,
Georgetown University Medical Center, Washington, D. C. 20007
*
This work was supported by National Institutes of Health
Specialized Program of Research Excellence Grants 1P50CA58185 and R21CA
80897 and by Department of Defense Career Development Award DAMD17-01-1-0252. This work was supported in part by the Lombardi Cancer Center Microscopy and Imaging Shared Resource, U.S. Public Health Service, Grant 2P30-CA-51008.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.
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