Function of the carbohydrates in contact site A glycoprotein of Dictyostelium discoideum affected by tunicamycin.
1. The relationship between glycosylation of contact site A (csA) of 80 kDa with two types of N-linked carbohydrates, I and II, and EDTA-resistant cell contact of Dictyostelium was investigated by tunicamycin treatment. 2. Carbohydrate I glycosylation, involved in a shift of csA from 66 to 80 kDa, was more sensitive to tunicamycin than carbohydrate II glycosylation in its shift from 53 to 66 kDa. 3. The appearance of csA of 80 kDa corresponded to that of EDTA-resistant cell contact. Carbohydrate I may be essential for EDTA-resistant cell contact. 4. In starved cells treated with tunicamycin, only 4-8% of moieties labeled with wheat germ agglutinin in carbohydrate II were modified.
Yoshida
M
M
Research Institute of Food Science, Kinki University, Osaka, Japan.
D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002448:Cell Adhesion / Q000187:drug effects; D004023:Dictyostelium / Q000502:physiology*; D004492:Edetic Acid / Q000494:pharmacology; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D008970:Molecular Weight; D014415:Tunicamycin / Q000494:pharmacology*
D006023:Glycoproteins; D014415:Tunicamycin; D004492:Edetic Acid