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Several clones of Chinese hamster ovary cells resistant to the cytotoxicity of the phytohemagglutinin from Phaseolus vulgaris show decreased binding of 125I-labeled phytohemagglutinin and contain decreased levels of a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase (EC 2.4.1.51; UDP-2-acetamido-2-deoxy-D-glucose:glycoprotein 2-acetamido-2-deoxy-D-glucosyltransferase) activity when compared to wild-type cells. The decrease in transferase activity varies from 45% to 96%, depending on the exogenous acceptor used in the enzyme assay. No differences between lectin-resistant and wild-type cells were noted for several other glycosyltransferases. The absence of a particular N-acetylglucosaminyltransferase in the lectin-resistant cells apparently results in defective glycosylation of lectin-binding glycoproteins on the cell surface. A phytohemagglutinin-resistant clone which shows decreased binding of 125I-labeled phytohemagglutinin but does not exhibit the enzyme deficiency has also been isolated.

proceedings of the national academy of sciences of the united states of america

Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase activity.