Effect of in vivo gamma-irradiation on the binding of wheat germ agglutinin on lymphocyte plasma membranes.
Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and N-acetyl-D-glucosamine. Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism / Q000528:radiation effects; D005720:Gamma Rays; D008214:Lymphocytes / Q000378:metabolism / Q000528:radiation effects*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011975:Receptors, Mitogen / Q000528:radiation effects*; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
D011975:Receptors, Mitogen; D014909:Wheat Germ Agglutinins; C027503:wheat germ agglutinin receptor