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J Biol Chem, Vol. 273, Issue 27, 17258-17268, July 3, 1998
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From the Departments of Biosynthesis and processing of amphiregulin (AR)
have been investigated in human colorectal (HCA-7, Caco-2) and mammary
(MCF-7) cancer cell lines, as well as in Madin-Darby canine kidney
cells stably expressing various human AR precursor (pro-AR) forms. Both cells expressing endogenous and transfected AR produce multiple cellular and soluble forms of AR with an N-glycosylated
50-kDa pro-AR form being predominant. Our results demonstrate that
sequential proteolytic cleavage within the ectodomain of the 50-kDa
pro-AR form leads to release of a predominant
N-glycosylated 43-kDa soluble AR, as well as the appearance
of other cellular and soluble AR forms. Cell surface biotinylation
studies using a C-terminal epitope-tagged pro-AR indicate that all cell
surface forms are membrane-anchored and support that AR is released by
ectodomain cleavage of pro-AR at the plasma membrane. We also show that
pro-AR ectodomain cleavage is a regulated process, which can be
stimulated by phorbol 12-myristate 13-acetate and inhibited by the
metalloprotease inhibitor, batimastat. In addition, we provide evidence
that high molecular mass AR forms may retain the full-length N-terminal
pro-region, which may influence the biological activities of these
forms.
Cell Biology and
Medicine,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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