Glycoprotein composition and turnover in subcellular fractions from the cerebral cortex of normal and reeler mutant mice.

Twenty-day-old reeler and normal mice were either injected intraventricularly with radiolabelled fucose before subcellular fractionation of the cerebral cortex followed by SDS-PAGE, or gels of such fractions were overlaid with [125I]concanavalin A (ConA). While there were no differences in polypeptide profiles of normal and reeler subcellular fractions there were marked differences in the abundance of particular ConA-binding glycoproteins and in fucose incorporation into particular glycoproteins, especially in the synaptic plasma membrane (SPM) and 100,000 g soluble fractions. In addition there was a significantly lower binding (greater than 50%) of quinuclidinyl benzilate to reeler microsomal and SPM fractions as compared with normal. The differences in glycoprotein expression may be pertinent to anatomical observations of abnormal interactions between neurons and glial fibres during development of the reeler cerebrum.