J. Biochem, 2003, Vol. 134, No. 4 497-504
© 2003 Japanese Biochemical Society
CELL |
Characterization of the Ligand-Binding Specificities of Integrin 
3ß1 and 6ß1 Using a Panel of Purified Laminin Isoforms Containing Distinct Chains
1 Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871; and 2 Research Institute, Osaka Medical Center for Maternal and Child Health, 840 Murodo, Izumi, Osaka 594-1101
Integrins 
3ß1 and 6ß1 are two major laminin receptors expressed on the surface of mammalian cells. Interactions of cells with laminins through these integrins play important roles in cell adhesion, differentiation, motility, and matrix assembly. To determine the binding specificity and affinity of these integrins toward various types of laminins at the level of direct protein-protein interactions, we purified integrins 3ß1 and 6ß1 from human placenta, and examined their binding to a panel of laminin isoforms, each containing distinct chains (i.e., laminin-1, laminin-2/4, laminin-5, laminin-8, and laminin-10/11). Integrin 3ß1 showed clear specificity for laminin-5 and laminin-10/11, with no significant binding to laminin-1, laminin-2/4, and laminin-8. In contrast, integrin 6ß1 showed a broad spectrum of specificity, with apparent binding affinity in the following order: laminin-10/11 > laminin-5 > laminin-1 > laminin-2/4 
laminin-8. Integrin titration assays demonstrated that laminin-10/11 was the most preferred ligand among the five distinct laminin isoforms for both 3ß1 and 6ß1 integrins. Given that laminin-10/11 is the major basement membrane component of many adult tissues, the interaction of laminin-10/11 with these integrins should play a central role in the adhesive interactions of epithelial cells with underlying basement membranes.
* To whom correspondence should be addressed. Tel: +81-6-6879-8617, Fax: +81-6-6879-8619, E-mail: sekiguch{at}protein.osaka-u.ac.jp
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