Glycobiology, 2000, Vol. 10, No. 6 559-563
© 2000 Oxford University Press
Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1
Sir William Dunn School of Pathology, South Parks Road, University of Oxford, Oxford, OX1 3RE, UK and 3Department of Psychiatry, University of California San Francisco, 401 Parnassus Avenue, San Francisco, CA 94143–0984, USA
Galectin-1 is a sugar binding protein specific for ß-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoreTM. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at ~5 µM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed.
1 Present address: The R.W. Johnson Pharmaceutical Research Institute, 3535 General Atomics Center, La Jolla, CA
2 To whom correspondence should be addressed
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