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(Received for publication, January 6, 1997, and in revised form, February 24, 1997)
From the Wellcome Trust Centre for Cell-Matrix Research, School of
Biological Sciences, University of Manchester, Manchester,
M13 9PT, United Kingdom, the § Dana-Farber Cancer
Institute, Harvard Medical School, Boston, Massachusetts 02115, and
the ¶ Max-Planck-Institut für Biochemie,
82152 Martinsreid, Germany
The integrin
Volume 272, Number 19,
Issue of May 9, 1997
pp. 12311-12317
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
1 A-domain Is a Ligand Binding Site for Collagens
and Laminin
1
1 is a cell surface receptor
for collagens and laminin. The 1 subunit contains an A-domain, and
the A-domains of other integrins are known to mediate ligand binding.
To determine the role of the 1 A-domain in ligand binding and the
extent to which it reproduced the ligand binding activity and
specificity of the parent molecule, we produced recombinant 1
A-domain and tested its ability to bind collagens and laminin. In solid
phase assays, the A-domain from 1 was found to bind to collagen I, collagen IV, and laminin in a largely cation-dependent
manner. The 2 A-domain, from the 21 integrin, also bound to
these ligands, but the binding hierarchy differed from that seen for
1. This is the first demonstration of laminin binding by A-domains.
Specificity of A-domain-ligand binding was further investigated using
the triple-helical proteolytic fragment of collagen IV, CB3, and its subfragments, F1 and F4. 1 A-domain bound to all three fragments, while the 2 A-domain bound CB3 less well and exhibited little binding to F1 and no binding to F4. These differences mirror previous reports of distinct integrin binding sites in collagen IV and for the
first time identify a limited proteolytic fragment of a ligand that
contains integrin A-domain binding activity. To gain insight into the
contribution that the A-domain makes to ligand binding within the whole
integrin heterodimer, we measured binding constants for
A-domain-collagen interactions using surface plasmon resonance
biosensor technology. The values obtained were similar to those
reported for intact integrin binding, suggesting that the A-domain is
the major collagen binding site in the 11 and 21
integrins.
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