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Glycobiology, 2000, Vol. 10, No. 2 131-140
© 2000 Oxford University Press

Involvement of CD2 and CD3 in galectin-1 induced signaling in human Jurkat T-cells

Hermann Walzel1, Matthias Blach, Jun Hirabayashi2, Ken-Ichi Kasai2 and Josef Brock

Institute of Medical Biochemistry and Molecular Biology, Schillingallee 70, University of Rostock, D-18057 Rostock, Germany and 2Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa 199–01, Japan

Galectin-1 (gal-1) a member of the mammalian ß-galactoside-binding proteins recognizes preferentially Galß1–4GlcNAc sequences of oligosaccharides associated with several cell surface glycoconjugates. In the present work, gal-1 has been identified to be a ligand for the CD3-complex as well as for CD2 as detected by affinity chromatography of Jurkat T-cell lysates on gal-1 agarose and by binding of the biotinylated lectin to CD3 and CD2 immunoprecipitates on blots. In CD45+ Jurkat E6.1 cells, the lectin stimulates a sustained increase in the intracytoplasmic calcium concentration ([Ca2+]i) consisting of both the release of calcium from intracellular stores and the calcium influx from the extracellular space. This effect of gal-1 on [Ca2+]i is completely inhibited by lactose at 10 mM and was absent in CD45– Jurkat J45.01 cells. Preincubation of Jurkat E6.1 cells with cholera toxin or with the protein tyrosine kinase inhibitor herbimycin A reduced the gal-1 induced calcium response whereas the increase in [Ca2+]i stimulated by CD2 or CD3 monoclonal antibodies (mAbs) was completely inhibited. Depolarization of E6.1 cells in a high-potassium buffer, a standard method to activate voltage-operated calcium channels, was without effect on [Ca2+]i. Membrane depolarization with gramicidin or by a high-potassium buffer was without effects on the lectin-mediated calcium release from intracellular stores but inhibited the gal-1 induced receptor-operated calcium influx. In Jurkat E6.1 cells the lectin stimulates the transient generation of inositol-1,4,5-trisphosphate and the tyrosine phosphorylation of phospholipase C{gamma}1. The results suggest that the ligation of CD2 and CD3 by gal-1 induces early events in T-cell activation comparable with that elicited by CD2 or CD3 mAbs.

1 To whom correspondence should be addressed


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