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Specific binding of cytotactin to sulfated glycolipids
Author(s) -
Crossin K. L.,
Edelman G. M.
Publication year - 1992
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490330416
Subject(s) - glycolipid , biochemistry , polyclonal antibodies , sulfation , glycoprotein , chemistry , receptor , divalent , chondroitin sulfate , monoclonal antibody , antibody , biology , glycosaminoglycan , immunology , organic chemistry
The binding of the glial glycoprotein, cytotactin, to a variety of purified glycolipids was examined. Clear‐cut evidence was found for binding of radiolabeled cytotactin to sulfatides purified from bovine brain, but the molecule did not bind to gangliosides or cerebrosides. The sulfatide binding was sensitive to pH and ionic strength and was dependent on the presence of divalent cations. Binding was inhibited by purified unlabeled cytotactin, by polyclonal antibodies to cytotactin, and by several monosaccharides and polysaccharides. It was not inhibited by fibronectin, a chondroitin sulfate proteoglycan, or the HNK‐1 monoclonal antibody, all of which are known to bind to cytotactin. These findings raise the possibilities that sulfated glycolipids may function as cellular receptors for cytotactin and that binding by sulfatides may modulate the varied effects of cytotactin on cellular processes. © 1992 Wiley‐Liss, Inc.