Changes in the glycoprotein composition of plasma membrane during the differentiation of friend erythroleukemia cells.
Friend erythroleukemia cells display transient and permanent changes in the composition of their plasma membrane-bound glycoproteins during dimethyl sulfoxide-induced differentiation. The transient changes, as revealed by metabolic labeling with [14C]glucosamine, are most conspicuous around the time during which most cells become committed to terminal differentiation. Permanent changes are revealed by reductive tritiation after oxidation with NaIO4 or galactose oxidase. In differentiated cells one glycoprotein fraction (Mr 150 000) could not be labeled by any of these methods, although it does contain neuraminic acid. We found no evidence in support of the hypothesis that the anomalous behavior of this fraction is caused by an increased degree of O-acetylated neuraminic acid in the plasma membrane of differentiated cells.
D000818:Animals; D002453:Cell Cycle; D002454:Cell Differentiation; D002462:Cell Membrane / Q000502:physiology; D006023:Glycoproteins / Q000378:metabolism*; D007700:Kinetics; D007942:Leukemia, Experimental / Q000503:physiopathology*; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice
D006023:Glycoproteins; D008565:Membrane Proteins