TAILIEUCHUNG - Báo cáo khoa học: Integrin receptor specificity for human red cell ICAM-4 ligand

The red cell intercellular adhesion molecule-4 (ICAM-4) binds to different members of the integrin receptor families. Tobetterdefine the ICAM-4 integrinreceptor specificity, cell transfectants individually expressing various integrins were used to demonstrate thataLb2,aMb2,andaIIbb3(activated) bind specifically and dose dependently to the recombinant also showthat cell surface ICAM-4 interacts with the cell surface aVb3 integrin. | Eur. J. Biochem. 271 3729-3740 2004 FEBS 2004 doi Integrin receptor specificity for human red cell ICAM-4 ligand Critical residues for aIIbp3 and aVp3 binding Patricia Hermand1 Pierre Gane1 Isabelle Callebaut2 Nellv Kieffer3 Jean-Pierre Cartron1 and Pascal Baillv1 3INSERM U76 Institut National de la Transfusion Sanguine Paris France 2Département de Biologie Structurale LMCP CNRS UMR 7590 UP6 UP7 Paris France 3Laboratoire de Biologie et de Physiologie integree CNRS GDRE-ITI Universite du Luxembourg Luxembourg The red cell intercellular adhesion molecule-4 ICAM-4 binds to different members of the integrin receptor families. To better define the ICAM-4 integrin receptor specificity cell transfectants individually expressing various integrins were used to demonstrate that aLb2 aMb2 and aIIbb3 activated bind specifically and dose dependently to the recombinant ICAM-4-Fc protein. We also show that cell surface ICAM-4 interacts with the cell surface aVb3 integrin. In addition using a a4b1 cell transfectant and b2 integrin-deficient LAD cells we show here that ICAM-4 failed to interact with a4b1 even after a4p1 activation by phorbol ester or with the monoclonal antibody TS2 16 Mn2 . ICAM-4 amino acids that are critical for aIIbp3 and aVb3 interaction were identified by domain deletion analysis site-directed muta genesis and synthetic peptide inhibition. Our results provide evidence that the b3 integrin binding sites encompass the first and second Ig-like domains of ICAM-4. However while the aIIbb3 contact site comprises the ABED face of domain D1 with an extension in the C -E loop of domain D2 the aVb3 contact site comprises residues on both faces of D1 and in the C -E loop of D2. These data together with our previous results demonstrate that different integrins bind to different but partly overlapping sites on ICAM-4 and that ICAM-4 may accommodate multiple integrin receptors present on leukocytes platelets and endothelial cells. Keywords

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