Volume 271, Number 27,
Issue of July 5, 1996
pp. 16119-16125
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Isolation of a Sponge-derived Extracellular Matrix Adhesion
Protein
(Received for publication, January 29, 1996, and in revised form, April 9, 1996)
Judith A.
Varner
From the Department of Medicine 0063, University of California, San
Diego, La Jolla, California 92093-0063
The development of stable intercellular adhesions
in the animal kingdom permitted the evolution of the metazoans, of
which the sponges are primitive examples. Intercellular adhesion in
these simple animals is mediated by a high affinity interaction between
the sponge cell surface and aggregation factor, a 2 × 107-Da proteoglycan that is one of the major components of
the sponge extracellular matrix. This report describes a sponge cell
surface and extracellular matrix ligand for the sponge proteoglycan,
aggregation factor. The 210-kDa protein binds aggregation factor
proteoglycan with high affinity (Kd = 7 × 10
9 M). Importantly, in soluble form, it also
inhibits aggregation factor-mediated cell adhesion. This glycoprotein
is expressed on the sponge cell surface and within the extracellular
matrix. This novel sponge extracellular matrix protein may represent a
primitive antecedent of the extracellular matrix adhesion proteins of
higher organisms.