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J. Biol. Chem., Vol. 278, Issue 5, 3386-3394, January 31, 2003
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From the MUC1 clearance from the uterine epithelial cell
surface is a prerequisite for the creation of an environment conducive
to embryo implantation. In some species, reduced mRNA levels along with metabolic turnover account for loss of MUC1 during the receptive phase throughout the uterine epithelium. In other species, MUC1 is
rapidly lost solely at the site of blastocyst attachment, suggesting the action of a protease. Correlative studies also indicate the presence of soluble forms of MUC1 in cell culture supernatants in
vitro and in bodily fluids in vivo. To characterize
the proteolytic activity mediating MUC1 release, shedding of MUC1 was
analyzed in a human uterine epithelial cell line (HES) that abundantly expresses and readily sheds MUC1. MUC1 release was stimulated by
phorbol 12-myristate 13-acetate and was markedly inhibited by the
synthetic peptide hydroxamate metalloprotease inhibitor, tumor necrosis
factor-
Tumor Necrosis Factor-
Converting Enzyme/ADAM 17 Mediates MUC1
Shedding*
,¶
Department of Biological Sciences,
University of Delaware, Newark, Delaware 19716 and the
§ Cellular Biochemistry and Biophysics Program,
Sloan-Kettering Institute, Memorial Sloan Kettering Cancer Center,
New York, New York 10021
protease inhibitor (TAPI), as well as by an
endogenous inhibitor of matrix metalloproteases, tissue inhibitor of
metalloproteases (TIMP)-3. These characteristics along with studies
conducted with cell lines genetically deficient in various ADAMs (for
a disintegrin and
metalloprotease) identified tumor necrosis factor-
converting enzyme (TACE)/ADAM 17 as a MUC1 sheddase. Furthermore, both
TACE and MUC1 were expressed in human uterine epithelia during the
receptive phase, and co-immunoprecipitation experiments revealed a
physical interaction between TACE and MUC1 in HES cells. These
studies establish a proteolytic mechanism for MUC1 clearance
from a human uterine epithelial cell line and identify TACE as a MUC1 sheddase.
*
This work was supported by National Institutes of Health
Grant HD 29963 (to D. D. C.) as part of the National
Cooperative Program on Trophoblast-Maternal Tissue Interactions.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.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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