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J Biol Chem, Vol. 273, Issue 35, 22825-22832, August 28, 1998
From the ARH-77 cells do not adhere to type I collagen and
readily invade into collagen gels, but following expression of the
transmembrane heparan sulfate proteoglycan syndecan-1, they bind
collagen and fail to invade. We now show that cells transfected with
syndecan-2 or syndecan-4 also bind collagen and are non-invasive. In
contrast, cells transfected with the
glycosylphosphatidylinositol-anchored proteoglycan glypican-1 do not
bind to collagen and remain invasive, even though glypican- and
syndecan-expressing cells have similar surface levels of heparan
sulfate, and their proteoglycans have similar affinities for collagen.
Analysis of cells expressing syndecan-1-glypican-1 chimeric
proteoglycans reveals that inhibition of invasion requires the
extracellular domain of syndecan but not its transmembrane or
cytoplasmic domain. Surprisingly, cells bearing a chimera composed of
the glypican extracellular domain fused to the syndecan transmembrane
and cytoplasmic domains bind to collagen but remain invasive, implying
that adhesion to collagen is not by itself sufficient to inhibit
invasion. Apparently, the extracellular domain of syndecan-1,
presumably by interacting with cell-surface signal transducing
molecules, directly regulates complex cell behaviors such as motility
and invasiveness. These results also show for the first time that
syndecans and glypicans can have distinct functions, even when
expressed by the same cell type.
Heparan Sulfate Proteoglycans as Adhesive and Anti-invasive
Molecules
SYNDECANS AND GLYPICAN HAVE DISTINCT FUNCTIONS
,,,
Department of Pathology and
Department of Anatomy, University of Arkansas for Medical
Sciences, Little Rock, Arkansas 72205, the § Department
of Biology, Massachusetts Institute of Technology,
Cambridge, Massachusetts 02139, and the ¶ Department of
Developmental and Cell Biology, University of California,
Irvine, California 92697
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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