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Journal of Cell Science, Vol 114, Issue 7 1321-1329, Copyright © 2001 by Company of Biologists
JOURNAL ARTICLES |
IM van Den Nieuwenhof, C Renardel De Lavalette, N Diaz, I van Die and TK van Den Berg
Departments of Medical Chemistry and Cell Biology and Immunology, Research Institute Immunology and Inflammatory diseases, Vrije Universiteit, Van der Boechorststraat 7, The Netherlands. t.van_den_berg.cell@med.vu.nl
Signal regulatory protein-(&agr;) (SIRP(&agr;)) is a member of the Ig superfamily selectively expressed by neuronal and myeloid cells. The molecule mediates functional interactions with CD47/integrin-associated protein. Here we provide evidence for the tissue-specific glycosylation of neuronal and haematopoietic SIRP(&agr;). We demonstrate a major difference in the galactosylation of N-linked glycans isolated from neuronal (i.e. brain-derived) SIRP(&agr;) as compared to myeloid (i.e. spleen-derived) SIRP(&agr;), with neuronal SIRP(&agr;) almost completely lacking galactose. (&bgr;)4-galactosyltransferase assays demonstrated that this is most likely due to a low galactosylation capacity of the brain. In order to investigate the role of galactosylation of SIRP(&agr;) in cellular interactions, soluble recombinant SIRP(&agr;) glycoforms containing galactose (SIRP(&agr;)-Fc) or lacking galactose (SIRP(&agr;)((&Dgr;)Gal)-Fc) were produced. Binding studies demonstrated superior binding of SIRP(&agr;)((&Dgr;)Gal)-Fc to cerebellar neurons and isolated lymphocytes. In contrast, SIRP(&agr;)-Fc bound relatively strong to macrophages. These data show that the galactosylation of SIRP(&agr;) determines its cellular binding specificity.
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