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[3H]Cytochalasin B was used as a ligand to identify and characterize the glucose transporter in cerebral microvessels of the rat and the pig. Specific cytochalasin B binding, defined as that fraction of the total binding that is stereospecifically displaced by excess (500 mM) D-glucose, is saturable. Kinetic studies of this specific binding to cerebral microvessel preparations showed a dissociation constant (Kd) of 0.65-0.88 microM and a maximal binding (Bmax) of 60-80 pmol/mg of protein. In comparison, the Bmax of particulate fractions of the cerebral cortex was about one-tenth that of cerebral microvessels. The ability of various hexoses to displace specific cytochalasin B binding to cerebral microvessels in vitro correlated well with the capability of these hexoses to cross the blood-brain barrier in vivo. Irreversible photoaffinity labeling of the glucose transporter of cerebral microvessels with cytochalasin B followed by solubilization and polyacrylamide gel electrophoresis labeled a polypeptide(s) with a molecular weight of about 53,000. Antibodies prepared against the glucose transporter of human erythrocytes also reacted with a polypeptide(s) with a molecular weight of about 53,000 on electrophoresed preparations of cerebral microvessels. These results indicate that cerebral microvessels are richly endowed with a glucose transporter moiety of similar molecular weight and antigenic characteristics as the glucose transporter of human erythrocytes and other mammalian tissues.

Identification and characterization of the glucose transporter of the blood-brain barrier by cytochalasin B binding and immunological reactivity.