Laminin binds specifically to sulfated glycolipids.

Previous studies of the agglutination of erythrocytes by the basement membrane glycoprotein laminin have suggested that laminin binds to gangliosides [Kennedy, D.W., Rohrbach, D.H., Martin, G.R., Momoi, T. & Yamada, K.M. (1983) J. Cell. Physiol. 114, 257-262]. Based on the following evidence, however, we find that laminin binds specifically to sulfatides, not gangliosides. Monogalactosyl sulfatides, purified from sheep erythrocytes with a yield of 4.3 mg/kg of packed cells, bound laminin with high affinity as did authentic bovine brain sulfatide (galactosylceramide-I3-sulfate). The binding activity of these lipids and of total erythrocyte lipids was stable to alkali and neuraminidase treatment but labile to dilute acid under conditions that destroy sulfatides but not gangliosides. Of various glycolipid and phospholipid standards tested, only sulfatides bound laminin with high affinity. Sulfatide binding and agglutinating activities of proteolytic fragments of laminin indicated that the globular end regions of the 200-kDa subunits are required for both activities. Thus, monogalactosylsulfatides, and possibly other more complex sulfated glycolipids, are probably involved in the agglutination of erythrocytes. These results also suggest a physiological function of sulfatides in cell adhesion. The agglutination of erythrocytes by fibronectin is also inhibited by gangliosides [Yamada, K.M., Kennedy, D.W., Grotendorst, G.R. & Momoi, T. (1981) J. Cell. Physiol. 109, 343-351]. Fibronectin, however, did not bind to sulfatides with high affinity but rather bound with low affinity to all anionic lipids tested, including phospholipids, gangliosides, and sulfatides.