Thromb Haemost 1995; 73(03): 543-545
DOI: 10.1055/s-0038-1653810
Original Articles
Platelets
Schattauer GmbH Stuttgart

A Structural/Functional Domain on Human CD36 Is Involved in the Binding of Anti-Nakα Antibodies

Authors

  • Laurent Daviet

    1   The INSERM Unit 331, Faculty of Medicine Alexis Carrel, Lyon, France
  • Marie-Christine Morel-Kopp

    2   Service d’lmmunologie Leuco-Plaquettaire, I.N.T.S, Etablissement Cabanel, Paris, France
  • Cécile Kaplan

    2   Service d’lmmunologie Leuco-Plaquettaire, I.N.T.S, Etablissement Cabanel, Paris, France
  • John L McGregor

    1   The INSERM Unit 331, Faculty of Medicine Alexis Carrel, Lyon, France
    3   Stanford Medical School, Division of Hematology (S161), Stanford, CA, USA
Further Information

Publication History

Received 08 August 1994

Accepted after resubmission 25 November 1994

Publication Date:
09 July 2018 (online)

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Summary

The human CD36 antigen is an integral membrane glycoprotein expressed by platelets, monocytes, endothelial cells and various tumor cell lines. CD36 acts as a receptor for thrombospondin, collagen, Plasmodium falciparum-infected erythrocytes and oxidized low- density lipoprotein. Individuals possessing the Naka-negative phenotype do not express CD36 and risk developing anti-CD36 isoantibodies upon blood transfusion or during pregnancy. In the present study, we have examined the interaction of an anti-Naka serum with recombinantly expressed CD36. Results obtained show that five functional CD36 monoclonal antibodies (OKM5, FA6-152, L103, ESIV-C7 and 10/5) prevent the binding of the anti-Naka serum whereas a single monoclonal antibody (13/10) has no effect. Consistent with this result, an epitope map of CD36 generated using cross-blocking experiments, indicates that the inhibitory monoclonal antibodies recognize closely- related epitopes whereas 13/10 reacts with a distinct CD36 determinant. Furthermore, we have demonstrated, in a recent study, that OKM5, FA6-152, L103 and 10/5 bind to the same CD36 domain defined by amino acids 155 to 183. Taken together, our results indicate that the 155-183 sequence is important for the binding of the anti-Naka serum to CD36 and may represent a surface-exposed, immunogenic and presumably functional region on human CD36.