Identification of αvβ3 as a heterotypic ligand for CD31/PECAM-1

DOI PDF 被引用文献4件
  • C. D. Buckley
    1 Cell Adhesion Laboratory, Imperial Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, UK
  • R. Doyonnas
    3 MRC Molecular Haematology Unit, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, UK
  • J. P. Newton
    1 Cell Adhesion Laboratory, Imperial Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, UK
  • S. D. Blystone
    Washington University School of Medicine 4 Department of Medicine, Infectious Diseases Division , , St Louis, Missouri 63110, USA
  • E. J. Brown
    Washington University School of Medicine 4 Department of Medicine, Infectious Diseases Division , , St Louis, Missouri 63110, USA
  • S. M. Watt
    3 MRC Molecular Haematology Unit, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, UK
  • D. L. Simmons
    1 Cell Adhesion Laboratory, Imperial Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, UK

説明

<jats:title>ABSTRACT</jats:title> <jats:p>CD31 (PECAM-1) is a member of the immunoglobulin gene superfamily (IgSF) and has an important role in a number of endothelial cell functions including angiogenesis, inflammation, integrin activation and cell-cell adhesion. CD31 has both homotypic and heterotypic adhesive properties and in common with other IgSF members contains multiple functional domains. Using chimaeric fusion proteins of CD31 and a panel of haematopoietic cell lines we show that CD31 can bind cells in a predominantly homotypic or heterotypic manner depending on the cell line used. Heterotypic binding was found to be cation and temperature dependent and enhanced by Mn2+: all features of integrin mediated binding. Using a panel of anti-CD31 and anti-integrin antibodies we show that αvβ3 is a ligand for CD31 on the monocytic cell line U937. The specificity of the interaction between αvβ3 and CD31 was further confirmed by solid phase binding assays and the use of αvβ3 transfected cells which bound CD31 specifically. Furthermore, we have mapped the binding site for αvβ3 to domains 1 and 2 of CD31. The interaction of CD31 with αvβ3 may be important in many aspects of endothelial function including leukocyteendothelial transmigration and angiogenesis.</jats:p>

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