Abnormal lipid-linked oligosaccharides in class E Thy-1-negative mutant lymphomas.

Abstract

The glycosylation defect of Thy-1-mutant lymphomas of the class E complementation group has been identified as a block in the synthesis of the lipid-linked oligosaccharide precursor of the asparagine-linked oligosaccharides of glycoproteins. Two major lipid-linked oligosaccharides were isolated from the mutant cells. Both oligosaccharides were smaller than the lipid-linkid oligosaccharides of wild-type lymphomas and, in contrast to the lipid-linked oligosaccharides isolated from wild-type cells, both were resistant to digestion with endoglycosidase H. The oligosaccharides of newly synthesized polypeptides in class E Thy-1-cells were also resistant to endoglycosidase H digestion, providing strong evidence that they are derived from the abnormal lipid-linked oligosaccharides.

• Authors: I S Trowbridge, R Hyman
• Journal: Cell (Cell) Vol. 17 Issue 3 Pg. 503-8 (Jul 1979) ISSN: 0092-8674 [Print] United States
• PMID: 476828 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Glycoproteins
• Isoantigens
• Membrane Proteins
• Neoplasm Proteins
• Oligosaccharides

Topics

• Animals
• Cell Line
• Glycoproteins (genetics, metabolism)
• Isoantigens (genetics)
• Lipid Metabolism
• Lymphoma (genetics, metabolism)
• Membrane Proteins (genetics, metabolism)
• Mice
• Mutation
• Neoplasm Proteins (metabolism)
• Neoplasms, Experimental (metabolism)
• Oligosaccharides (metabolism)