J. Cell Biol., Volume 140, Number 1, January 12, 1998 197-210

Direct and Regulated Interaction of Integrin _E7 with E-Cadherin

Jonathan M.G. Higgins,^* Didier A. Mandlebrot,^* Sunil K. Shaw,^* Gary J. Russell,^*§ Elizabeth A. Murphy,^* Yih-Tai Chen, W. James Nelson, Christina M. Parker,^* and Michael B. Brenner^*

^* The Lymphocyte Biology Section, Division of Rheumatology, Immunology and Allergy and  Renal Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115; ^§ Combined Program in Pediatric Gastroenterology and Nutrition, and Department of Pathology, Massachusetts General Hospital, Boston, Massachusetts 02115; and  Department of Molecular and Cellular Physiology, Beckman Center, Stanford University School of Medicine, Stanford, California 94305

The cadherins are a family of homophilic adhesion molecules that play a vital role in the formation of cellular junctions and in tissue morphogenesis. Members of the integrin family are also involved in cell to cell adhesion, but bind heterophilically to immunoglobulin superfamily molecules such as intracellular adhesion molecule (ICAM)-1, vascular cell adhesion molecule (VCAM)-1, or mucosal addressin cell adhesion molecule (MadCAM)-1. Recently, an interaction between epithelial (E-) cadherin and the mucosal lymphocyte integrin, _E7, has been proposed. Here, we demonstrate that a human E-cadherin-Fc fusion protein binds directly to soluble recombinant _E7, and to _E7 solubilized from intraepithelial T lymphocytes. Furthermore, intraepithelial lymphocytes or transfected JY cells expressing the _E7 integrin adhere strongly to purified E-cadherin-Fc coated on plastic, and the adhesion can be inhibited by antibodies to _E7 or E-cadherin.

The binding of _E7 integrin to cadherins is selective since cell adhesion to P-cadherin-Fc through _E7 requires >100-fold more fusion protein than to E-cadherin-Fc. Although the structure of the _E-chain is unique among integrins, the avidity of _E7 for E-cadherin can be regulated by divalent cations or phorbol myristate acetate. Cross-linking of the T cell receptor complex on intraepithelial lymphocytes increases the avidity of _E7 for E-cadherin, and may provide a mechanism for the adherence and activation of lymphocytes within the epithelium in the presence of specific foreign antigen. Thus, despite its dissimilarity to known integrin ligands, the specific molecular interaction demonstrated here indicates that E-cadherin is a direct counter receptor for the _E7 integrin.

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