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(Received for publication, July 17, 1996, and in revised form, December 20, 1996)
From the Faculty of Dentistry and Department of Biochemistry and
Molecular Biology, Faculty of Medicine, University of British
Columbia, 2199 Wesbrook Mall,
Vancouver, British Columbia V6T 1Z3, Canada
The binding properties of the COOH-terminal
hemopexin-like domain (C domain) of human gelatinase A (matrix
metalloproteinase-2, 72-kDa gelatinase) were investigated to determine
whether the C domain has binding affinity for extracellular matrix and
basement membrane components. Recombinant C domain (rC domain)
(Gly417-Cys631) was expressed in
Escherichia coli, and the purified protein, identified
using two antipeptide antibodies, was determined by electrospray mass
spectrometry to have a mass of 25,925 Da, within 0.1 Da of that
predicted. As assessed by microwell substrate binding assays and by
column affinity chromatography, the matrix proteins laminin, denatured
type I collagen, elastin, SPARC (secreted protein that is acidic and
rich in cysteine), tenascin, and MatrigelTM were not bound
by the rC domain. Unlike the hemopexin-like domains of collagenase and
stromelysin, the rC domain also did not bind native type I collagen.
Nor were native or denatured types II, IV, V, and X collagen, or the
NC1 domain of type VII collagen bound. However, binding to heparin and
fibronectin (Kd, 1.1 × 10
6
M) could be disrupted by 0.58-0.76 and 0.3 M
NaCl, respectively. Using nonoverlapping chymotrypsin-generated
fragments of fibronectin, binding sites for the rC domain were found on
both the 40-kDa heparin binding and the 120-kDa cell binding
fibronectin domains (Kd values, ~4-6 × 107 M). The Ca2+ ion, but not the
potential structural Zn2+ ion, were found to be essential
for maintaining the binding properties of the protein. The apo-form of
the rC domain did not bind heparin, and both ethylenediaminetetraacetic
acid and the specific Ca2+ ion chelator
1,2-bis(2-aminophenoxy)
ethane-N,N,N
,N-tetraacetic acid, but not the
Zn2+ ion chelator 1,10-phenanthroline, eluted the holo form
of the rC domain from both heparin-Sepharose and fibronectin. Inductive coupled plasma mass spectrometry also did not detect a Zn2+
ion in the rC domain. In contrast, reduction with 65 mM
dithiothreitol did not interfere with heparin binding, further
emphasizing the crucial structural role played by the Ca2+
ion. Together, these data demonstrate for the first time that the
hemopexin-like domain of gelatinase A has a binding site for fibronectin and heparin, and that Ca2+ ions are important
in maintaining the structure and function of the domain.
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