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J Biol Chem, Vol. 273, Issue 5, 2601-2609, January 30, 1998
From the Department of Pathology and Laboratory Medicine,
University of Wisconsin Medical School, Madison, Wisconsin 53706
Fibronectin matrix assembly is thought to involve
binding interactions between the amino-terminal I1-5
repeats and the first type III repeat (III1). Here we
report that a third site, located within the III12-14
repeats of the carboxyl-terminal heparin II domain of fibronectin, is
also involved in fibrillogenesis. Heparin II fragments inhibited fibril
formation and binding of 125I-labeled fibronectin and/or
70-kDa fragments to the cell surface, deoxycholate-insoluble matrix,
and adsorbed 160-kDa cell adhesion fragments of fibronectin. The
inhibitory effects of heparin II fragments were as large or up to 20 times larger than those of a 44-kDa fibronectin fragment containing the
III1 repeat. Under physiological conditions, amino-terminal
fragments of fibronectin containing the I1-5 repeats
interacted preferentially with proteolytically derived heparin II
fragments and a recombinant III12-14 peptide both in
solution and in solid phase, indicating that matrix assembly may
involve direct interactions between I1-5 and
III12-14 repeats. Interactions between the
I1-5 repeats and 160-kDa fragments containing the
III12-14 and III1 repeats could be inhibited
by 
90% by either an anti-III13-14 monoclonal
antibody (mAb) (IST-2) or an anti-III1 mAb (9D2),
suggesting that cooperative interactions between III12-14
and III1 repeats may also promote binding of the
I1-5 repeats. Neither mAb IST-2 nor mAb 9D2, alone or in
combination, inhibited binding of 125I-labeled 70-kDa
fragments to cycloheximide-treated cells plated on the 160-kDa
substrate, suggesting that additional I1-5 binding sites,
independent of the III1 and III12-14 repeats, may be involved in fibrillogenesis.
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