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(Received for publication, February 20, 1997, and in revised form, March 18, 1997)
From the Program in Cellular and Molecular Biology and Department
of Pathology and Laboratory Medicine, University of Wisconsin-Madison,
Madison, Wisconsin, 53706-1532
The syndecan family of cell surface proteoglycans
regulates cell adhesion and growth factor signaling by binding
components of the extracellular matrix and growth factors. To date, all
known ligand interactions are via the covalently attached
glycosaminoglycan chains. To assay for potential extracellular
interactions via the core proteins directly, the recombinant
extracellular domain of syndecan-4 (S4ED), one of the four syndecan
family members, was tested as a substratum for the attachment of
mammalian cells. Human foreskin fibroblasts bind to mouse S4ED, and
both mouse and chicken S4ED can block this binding, with 50%
inhibition observed between 0.1 and 1 × 10
Volume 272, Number 20,
Issue of May 16, 1997
pp. 12901-12904
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
7
M. The extracellular domain of another syndecan family
member, syndecan-1, fails to compete for cell binding to mouse S4ED.
Amino acids 56-109 of the 120-amino acid mouse S4ED compete fully,
suggesting that the cell binding domain is within this region. The
ability of syndecan-4 to interact with molecules at the cell surface
via its core protein as well as its glycosaminoglycan chains may
uniquely regulate the formation of cell surface signaling complexes
following engagement of this proteoglycan with its extracellular
ligands.
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