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(Received for publication, July 21, 1994; and in revised form, December 12,
1994) Because syndecans are present at sites of cell-cell contact in vivo it has been hypothesized that they play a role in
mediating cell-cell adhesion. However, there has been no direct
evidence to support this notion. To address this question, B lymphoid
(ARH-77) cells were transfected with the cDNA for murine syndecan-1.
Unlike the parental cells, the transfectants form large multicellular
aggregates in suspension cultures and stain intensely for syndecan-1 at
sites of cell-cell contact. Using rotation-mediated aggregation assays,
we find that aggregation of syndecan-1-transfected cells is dependent
on divalent cations and is inhibited by the following: (i) addition of
heparin and heparin-like glycosaminoglycans, (ii) removal of heparan
sulfate from the cell surface, or (iii) addition of exogenous purified
syndecan-1. Mixing of syndecan-1-transfected and control-transfected
cells results in aggregates containing both cell types indicating that
aggregation occurs through a heterophilic adhesion mechanism in which
heparan sulfate chains bind to a counter-receptor present on these
cells. Importantly, syndecan-4-transfected cells also aggregate in a
heparan sulfate-dependent manner, while in contrast,
betaglycan-transfected cells aggregate poorly. Thus, syndecans may be
important mediators of cell-cell adhesion, but this function may not be
common to all transmembrane heparan sulfate-bearing proteoglycans.
Volume 270,
Number 10,
Issue of March 10, 1995 pp. 5077-5083
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
SYNDECANS-1 AND -4 MEDIATE INTERCELLULAR ADHESION FOLLOWING THEIR
TRANSFECTION INTO HUMAN B LYMPHOID CELLS
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