J. Cell Biol., Volume 144, Number 3, February 8, 1999 549-561

Evidence that Distinct States of the Integrin 61 Interact with Laminin and an ADAM

M.S. Chen,^* E.A.C. Almeida,^* A.-P.J. Huovila,^* Y. Takahashi,^* L.M. Shaw, A.M. Mercurio, and J.M. White^*

^* Department of Cell Biology, University of Virginia, Charlottesville, Virginia 22908; and  Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02115

Integrins can exist in different functional states with low or high binding capacity for particular ligands. We previously provided evidence that the integrin 61, on mouse eggs and on 6-transfected cells, interacted with the disintegrin domain of the sperm surface protein ADAM 2 (fertilin ). In the present study we tested the hypothesis that different states of 61 interact with fertilin and laminin, an extracellular matrix ligand for 61. Using 6-transfected cells we found that treatments (e.g., with phorbol myristate acetate or MnCl₂) that increased adhesion to laminin inhibited sperm binding. Conversely, treatments that inhibited laminin adhesion increased sperm binding. Next, we compared the ability of fluorescent beads coated with either fertilin  or with the laminin E8 fragment to bind to eggs. In Ca²⁺-containing media, fertilin  beads bound to eggs via an interaction mediated by the disintegrin loop of fertilin  and by the 6 integrin subunit. In Ca²⁺-containing media, laminin E8 beads did not bind to eggs. Treatment of eggs with phorbol myristate acetate or with the actin disrupting agent, latrunculin A, inhibited fertilin bead binding, but did not induce laminin E8 bead binding. Treatment of eggs with Mn²⁺ dramatically increased laminin E8 bead binding, and inhibited fertilin bead binding. Our results provide the first evidence that different states of an integrin (61) can interact with an extracellular matrix ligand (laminin) or a membrane-anchored cell surface ligand (ADAM 2).

integrin;  ADAM;  cell adhesion;  "avidity/affinity modulation";  fertilin

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