Metabolic correction of defects in the lipid anchoring of Thy-1 in lymphoma mutants

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Science  09 Dec 1988:
Vol. 242, Issue 4884, pp. 1446-1448
DOI: 10.1126/science.2904699


Many plasma membrane proteins, including Thy-1, are anchored by a carboxyl terminal glycophospholipid. This unit is absent from the Thy-1 of several lymphoma mutants that synthesize the Thy-1 polypeptide but fail to express it at the cell surface. Recessive mutants of complementation groups A to C, E, and F contain Thy-1 mRNA of normal size, which suggests that their Thy-1 polypeptide is normal. To identify possible metabolic lesions, each mutant was grown with various supplements. The class F and B mutants exhibited a reversible induction of surface lipid anchored Thy-1 when grown with the aminoglycoside G418. Other aminoglycosides, sugars, and ethanolamine were inactive. These unexpected observations are discussed in the context of lipid anchor biosynthesis.

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