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Laboratorio di Biologia Cellulare, Dipartimento di Genetica, Biologia e Chimica Medica, Università di Torino, Torino, Italy;
Istituto Superiore di Sanità, Roma, Italy;
Institute of Immunology-VIRCC, University of Vienna, Vienna, Austria;
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Istituto di Medicina Interna, Università di Torino, Torino, Italy;
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Dipartimento di Scienze Mediche, Università di Torino a Novara, Novara, Italy;
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Istituto di Biologia e Genetica, Università di Ancona, Ancona, Italy
Human CD38 is a cell surface molecule involved in the regulation of lymphocyte adhesion to endothelial cells. This suggests that HUVEC bear a ligand(s) for CD38 on the cell surface. By means of the mAb Moon-1, which specifically inhibits CD38-mediated cell adhesion, we have identified a trans-membrane 130-kDa molecule acting as a ligand for CD38. Here, we report that the molecule recognized by the Moon-1 mAb is CD31, a member of the Ig superfamily. This conclusion is based on 1) cross-inhibition assays between Moon-1 and reference anti-CD31 mAbs; 2) sequential immunoprecipitation experiments using Moon-1 and known anti-CD31 mAbs, and 3) reactivity of the Moon-1 mAb with CD31 transfectants. Further, CD31 and CD38 cognate interactions were found to modulate heterotypic adhesion as well as to implement cytoplasmic calcium fluxes identical to those obtained by means of agonistic anti-CD38 mAbs. Other effects tested included the synthesis of messages for a panel of cytokines, markedly increased upon receptor-ligand interactions. These results suggest that the interplay between CD38 and its ligand CD31 is an important step in the regulation of cell life and of the migration of leukocytes (and CD38+ cancer cells) through the endothelial cell wall.
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M. Konopleva, Z. Estrov, S. Zhao, M. Andreeff, and K. Mehta Ligation of Cell Surface CD38 Protein with Agonistic Monoclonal Antibody Induces a Cell Growth Signal in Myeloid Leukemia Cells J. Immunol., November 1, 1998; 161(9): 4702 - 4708. [Abstract] [Full Text] [PDF] |
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M. Morra, M. Zubiaur, C. Terhorst, J. Sancho, and F. Malavasi CD38 is functionally dependent on the TCR/CD3 complex in human T cells FASEB J, May 1, 1998; 12(7): 581 - 592. [Abstract] [Full Text] |
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A. Funaro, M. Reinis, O. Trubiani, S. Santi, R. Di Primio, and F. Malavasi CD38 Functions Are Regulated Through an Internalization Step J. Immunol., March 1, 1998; 160(5): 2238 - 2247. [Abstract] [Full Text] [PDF] |
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M. Cicmil, J. M. Thomas, T. Sage, F. A. Barry, M. Leduc, C. Bon, and J. M. Gibbins Collagen, Convulxin, and Thrombin Stimulate Aggregation-independent Tyrosine Phosphorylation of CD31 in Platelets. EVIDENCE FOR THE INVOLVEMENT OF Src FAMILY KINASES J. Biol. Chem., August 25, 2000; 275(35): 27339 - 27347. [Abstract] [Full Text] [PDF] |
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M. Zubiaur, O. Fernandez, E. Ferrero, J. Salmeron, B. Malissen, F. Malavasi, and J. Sancho CD38 Is Associated with Lipid Rafts and upon Receptor Stimulation Leads to Akt/Protein Kinase B and Erk Activation in the Absence of the CD3-zeta Immune Receptor Tyrosine-based Activation Motifs J. Biol. Chem., January 4, 2002; 277(1): 13 - 22. [Abstract] [Full Text] [PDF] |
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